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  1. HEADER TRANSFERASE 15-OCT-12 4HKD
  2. TITLE CRYSTAL STRUCTURE OF HUMAN MST2 SARAH DOMAIN
  3. COMPND MOL_ID: 1;
  4. COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 3;
  5. COMPND 3 CHAIN: A, B, C, D;
  6. COMPND 4 FRAGMENT: SARAH DOMAIN, UNP RESIDUES 436-484;
  7. COMPND 5 SYNONYM: MAMMALIAN STE20-LIKE PROTEIN KINASE 2, MST-2, STE20-LIKE
  8. COMPND 6 KINASE MST2, SERINE/THREONINE-PROTEIN KINASE KRS-1, SERINE/THREONINE-
  9. COMPND 7 PROTEIN KINASE 3 36KDA SUBUNIT, MST2/N, SERINE/THREONINE-PROTEIN
  10. COMPND 8 KINASE 3 20KDA SUBUNIT, MST2/C;
  11. COMPND 9 EC: 2.7.11.1;
  12. COMPND 10 ENGINEERED: YES
  13. SOURCE MOL_ID: 1;
  14. SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
  15. SOURCE 3 ORGANISM_COMMON: HUMAN;
  16. SOURCE 4 ORGANISM_TAXID: 9606;
  17. SOURCE 5 GENE: STK3, KRS1, MST2;
  18. SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
  19. SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
  20. SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS;
  21. SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
  22. SOURCE 10 EXPRESSION_SYSTEM_PLASMID: HT-PET28A
  23. KEYWDS HOMODIMERIZATION, HETERODOMERIZATION, SAV1, NEK2, RASSF, TRANSFERASE
  24. EXPDTA X-RAY DIFFRACTION
  25. AUTHOR G.G.LIU,Z.B.SHI,Z.C.ZHOU
  26. REVDAT 1 04-SEP-13 4HKD 0
  27. JRNL AUTH G.G.LIU,Z.B.SHI,Z.C.ZHOU
  28. JRNL TITL CRYSTAL STRUCTURE OF HUMAN MST2 SARAH DOMAIN
  29. JRNL REF TO BE PUBLISHED
  30. JRNL REFN
  31. REMARK 2
  32. REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
  33. REMARK 3
  34. REMARK 3 REFINEMENT.
  35. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
  36. REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
  37. REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
  38. REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
  39. REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
  40. REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
  41. REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
  42. REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
  43. REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
  44. REMARK 3 : ZWART
  45. REMARK 3
  46. REMARK 3 REFINEMENT TARGET : ML
  47. REMARK 3
  48. REMARK 3 DATA USED IN REFINEMENT.
  49. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
  50. REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.86
  51. REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
  52. REMARK 3 COMPLETENESS FOR RANGE (%) : 91.9
  53. REMARK 3 NUMBER OF REFLECTIONS : 29481
  54. REMARK 3
  55. REMARK 3 FIT TO DATA USED IN REFINEMENT.
  56. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
  57. REMARK 3 R VALUE (WORKING SET) : 0.195
  58. REMARK 3 FREE R VALUE : 0.231
  59. REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
  60. REMARK 3 FREE R VALUE TEST SET COUNT : 1497
  61. REMARK 3
  62. REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
  63. REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
  64. REMARK 3 1 34.8685 - 3.3427 0.97 2878 149 0.1998 0.2322
  65. REMARK 3 2 3.3427 - 2.6535 0.98 2711 175 0.2033 0.2452
  66. REMARK 3 3 2.6535 - 2.3182 0.96 2660 155 0.1968 0.2148
  67. REMARK 3 4 2.3182 - 2.1063 0.94 2620 114 0.1875 0.2318
  68. REMARK 3 5 2.1063 - 1.9553 0.91 2533 113 0.1909 0.2295
  69. REMARK 3 6 1.9553 - 1.8400 0.91 2476 143 0.1883 0.2137
  70. REMARK 3 7 1.8400 - 1.7479 0.90 2465 128 0.1840 0.2029
  71. REMARK 3 8 1.7479 - 1.6718 0.90 2446 130 0.1783 0.2144
  72. REMARK 3 9 1.6718 - 1.6074 0.90 2419 129 0.1864 0.2400
  73. REMARK 3 10 1.6074 - 1.5520 0.90 2487 120 0.1938 0.2588
  74. REMARK 3 11 1.5520 - 1.5030 0.85 2289 141 0.1993 0.2471
  75. REMARK 3
  76. REMARK 3 BULK SOLVENT MODELLING.
  77. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
  78. REMARK 3 SOLVENT RADIUS : 1.11
  79. REMARK 3 SHRINKAGE RADIUS : 0.90
  80. REMARK 3 K_SOL : NULL
  81. REMARK 3 B_SOL : NULL
  82. REMARK 3
  83. REMARK 3 ERROR ESTIMATES.
  84. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.130
  85. REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.520
  86. REMARK 3
  87. REMARK 3 B VALUES.
  88. REMARK 3 FROM WILSON PLOT (A**2) : NULL
  89. REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
  90. REMARK 3 OVERALL ANISOTROPIC B VALUE.
  91. REMARK 3 B11 (A**2) : NULL
  92. REMARK 3 B22 (A**2) : NULL
  93. REMARK 3 B33 (A**2) : NULL
  94. REMARK 3 B12 (A**2) : NULL
  95. REMARK 3 B13 (A**2) : NULL
  96. REMARK 3 B23 (A**2) : NULL
  97. REMARK 3
  98. REMARK 3 TWINNING INFORMATION.
  99. REMARK 3 FRACTION: NULL
  100. REMARK 3 OPERATOR: NULL
  101. REMARK 3
  102. REMARK 3 DEVIATIONS FROM IDEAL VALUES.
  103. REMARK 3 RMSD COUNT
  104. REMARK 3 BOND : 0.007 1771
  105. REMARK 3 ANGLE : 1.179 2367
  106. REMARK 3 CHIRALITY : 0.083 255
  107. REMARK 3 PLANARITY : 0.006 317
  108. REMARK 3 DIHEDRAL : 14.379 737
  109. REMARK 3
  110. REMARK 3 TLS DETAILS
  111. REMARK 3 NUMBER OF TLS GROUPS : NULL
  112. REMARK 3
  113. REMARK 3 NCS DETAILS
  114. REMARK 3 NUMBER OF NCS GROUPS : NULL
  115. REMARK 3
  116. REMARK 3 OTHER REFINEMENT REMARKS: NULL
  117. REMARK 4
  118. REMARK 4 4HKD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
  119. REMARK 100
  120. REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-12.
  121. REMARK 100 THE RCSB ID CODE IS RCSB075574.
  122. REMARK 200
  123. REMARK 200 EXPERIMENTAL DETAILS
  124. REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
  125. REMARK 200 DATE OF DATA COLLECTION : 16-APR-12
  126. REMARK 200 TEMPERATURE (KELVIN) : 100
  127. REMARK 200 PH : 4.6
  128. REMARK 200 NUMBER OF CRYSTALS USED : 1
  129. REMARK 200
  130. REMARK 200 SYNCHROTRON (Y/N) : Y
  131. REMARK 200 RADIATION SOURCE : SSRF
  132. REMARK 200 BEAMLINE : BL17U
  133. REMARK 200 X-RAY GENERATOR MODEL : NULL
  134. REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
  135. REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
  136. REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
  137. REMARK 200 OPTICS : NULL
  138. REMARK 200
  139. REMARK 200 DETECTOR TYPE : CCD
  140. REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
  141. REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
  142. REMARK 200 DATA SCALING SOFTWARE : HKL-2000
  143. REMARK 200
  144. REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29548
  145. REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
  146. REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
  147. REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
  148. REMARK 200
  149. REMARK 200 OVERALL.
  150. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
  151. REMARK 200 DATA REDUNDANCY : 5.300
  152. REMARK 200 R MERGE (I) : NULL
  153. REMARK 200 R SYM (I) : NULL
  154. REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
  155. REMARK 200
  156. REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
  157. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
  158. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
  159. REMARK 200 COMPLETENESS FOR SHELL (%) : 85.7
  160. REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
  161. REMARK 200 R MERGE FOR SHELL (I) : NULL
  162. REMARK 200 R SYM FOR SHELL (I) : NULL
  163. REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
  164. REMARK 200
  165. REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
  166. REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
  167. REMARK 200 SOFTWARE USED: AUTOSOL
  168. REMARK 200 STARTING MODEL: NULL
  169. REMARK 200
  170. REMARK 200 REMARK: NULL
  171. REMARK 280
  172. REMARK 280 CRYSTAL
  173. REMARK 280 SOLVENT CONTENT, VS (%): 34.45
  174. REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
  175. REMARK 280
  176. REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M CALCIUM CHLORIDE DIHYDRATE, 0.1M
  177. REMARK 280 SODIUM ACETATE TRIHYDRATE, 5%(V/V) 2-PROPANOL, PH 4.6, VAPOR
  178. REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
  179. REMARK 290
  180. REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
  181. REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
  182. REMARK 290
  183. REMARK 290 SYMOP SYMMETRY
  184. REMARK 290 NNNMMM OPERATOR
  185. REMARK 290 1555 X,Y,Z
  186. REMARK 290 2555 -X,-Y,Z+1/2
  187. REMARK 290 3555 -X,Y,-Z+1/2
  188. REMARK 290 4555 X,-Y,-Z
  189. REMARK 290 5555 X+1/2,Y+1/2,Z
  190. REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
  191. REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
  192. REMARK 290 8555 X+1/2,-Y+1/2,-Z
  193. REMARK 290
  194. REMARK 290 WHERE NNN -> OPERATOR NUMBER
  195. REMARK 290 MMM -> TRANSLATION VECTOR
  196. REMARK 290
  197. REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
  198. REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
  199. REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
  200. REMARK 290 RELATED MOLECULES.
  201. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
  202. REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
  203. REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
  204. REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
  205. REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
  206. REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.57750
  207. REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
  208. REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
  209. REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.57750
  210. REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
  211. REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
  212. REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
  213. REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 21.10250
  214. REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 22.30750
  215. REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
  216. REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.10250
  217. REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 22.30750
  218. REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 104.57750
  219. REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.10250
  220. REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 22.30750
  221. REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 104.57750
  222. REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.10250
  223. REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 22.30750
  224. REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
  225. REMARK 290
  226. REMARK 290 REMARK: NULL
  227. REMARK 300
  228. REMARK 300 BIOMOLECULE: 1, 2
  229. REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
  230. REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
  231. REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
  232. REMARK 300 BURIED SURFACE AREA.
  233. REMARK 350
  234. REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
  235. REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
  236. REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
  237. REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
  238. REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
  239. REMARK 350
  240. REMARK 350 BIOMOLECULE: 1
  241. REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
  242. REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
  243. REMARK 350 SOFTWARE USED: PISA
  244. REMARK 350 TOTAL BURIED SURFACE AREA: 2760 ANGSTROM**2
  245. REMARK 350 SURFACE AREA OF THE COMPLEX: 7460 ANGSTROM**2
  246. REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
  247. REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
  248. REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
  249. REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
  250. REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
  251. REMARK 350
  252. REMARK 350 BIOMOLECULE: 2
  253. REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
  254. REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
  255. REMARK 350 SOFTWARE USED: PISA
  256. REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2
  257. REMARK 350 SURFACE AREA OF THE COMPLEX: 7800 ANGSTROM**2
  258. REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
  259. REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
  260. REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
  261. REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
  262. REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
  263. REMARK 375
  264. REMARK 375 SPECIAL POSITION
  265. REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
  266. REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
  267. REMARK 375 POSITIONS.
  268. REMARK 375
  269. REMARK 375 ATOM RES CSSEQI
  270. REMARK 465
  271. REMARK 465 MISSING RESIDUES
  272. REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
  273. REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
  274. REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
  275. REMARK 465
  276. REMARK 465 M RES C SSSEQI
  277. REMARK 465 GLY A 432
  278. REMARK 465 ALA A 433
  279. REMARK 465 MSE A 434
  280. REMARK 470
  281. REMARK 470 MISSING ATOM
  282. REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
  283. REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
  284. REMARK 470 I=INSERTION CODE):
  285. REMARK 470 M RES CSSEQI ATOMS
  286. REMARK 470 LYS A 453 CD CE NZ
  287. REMARK 470 GLU A 462 CG CD OE1 OE2
  288. REMARK 470 GLU A 464 CD OE1 OE2
  289. REMARK 470 GLU A 465 CG CD OE1 OE2
  290. REMARK 470 LYS B 441 NZ
  291. REMARK 470 LYS B 453 NZ
  292. REMARK 470 GLN C 468 CG CD OE1 NE2
  293. REMARK 500
  294. REMARK 500 GEOMETRY AND STEREOCHEMISTRY
  295. REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
  296. REMARK 500
  297. REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
  298. REMARK 500
  299. REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
  300. REMARK 500 OE2 GLU A 460 O HOH A 524 2.11
  301. REMARK 500
  302. REMARK 500 REMARK: NULL
  303. REMARK 500
  304. REMARK 500 GEOMETRY AND STEREOCHEMISTRY
  305. REMARK 500 SUBTOPIC: CLOSE CONTACTS
  306. REMARK 500
  307. REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
  308. REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
  309. REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
  310. REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
  311. REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
  312. REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
  313. REMARK 500
  314. REMARK 500 DISTANCE CUTOFF:
  315. REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
  316. REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
  317. REMARK 500
  318. REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
  319. REMARK 500
  320. REMARK 500 REMARK: NULL
  321. REMARK 500
  322. REMARK 500 GEOMETRY AND STEREOCHEMISTRY
  323. REMARK 500 SUBTOPIC: TORSION ANGLES
  324. REMARK 500
  325. REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
  326. REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
  327. REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
  328. REMARK 500
  329. REMARK 500 STANDARD TABLE:
  330. REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
  331. REMARK 500
  332. REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
  333. REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
  334. REMARK 500
  335. REMARK 500 M RES CSSEQI PSI PHI
  336. REMARK 500 ASP A 436 -33.88 103.97
  337. REMARK 500
  338. REMARK 500 REMARK: NULL
  339. REMARK 500
  340. REMARK 500 GEOMETRY AND STEREOCHEMISTRY
  341. REMARK 500 SUBTOPIC: CHIRAL CENTERS
  342. REMARK 500
  343. REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
  344. REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
  345. REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
  346. REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
  347. REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
  348. REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
  349. REMARK 500
  350. REMARK 500 STANDARD TABLE:
  351. REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
  352. REMARK 500
  353. REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
  354. REMARK 500 ASP A 436 21.6 L L OUTSIDE RANGE
  355. REMARK 500
  356. REMARK 500 REMARK: NULL
  357. DBREF 4HKD A 436 484 UNP Q13188 STK3_HUMAN 436 484
  358. DBREF 4HKD B 436 484 UNP Q13188 STK3_HUMAN 436 484
  359. DBREF 4HKD C 436 484 UNP Q13188 STK3_HUMAN 436 484
  360. DBREF 4HKD D 436 484 UNP Q13188 STK3_HUMAN 436 484
  361. SEQADV 4HKD GLY A 432 UNP Q13188 EXPRESSION TAG
  362. SEQADV 4HKD ALA A 433 UNP Q13188 EXPRESSION TAG
  363. SEQADV 4HKD MSE A 434 UNP Q13188 EXPRESSION TAG
  364. SEQADV 4HKD ASP A 435 UNP Q13188 EXPRESSION TAG
  365. SEQADV 4HKD GLY B 432 UNP Q13188 EXPRESSION TAG
  366. SEQADV 4HKD ALA B 433 UNP Q13188 EXPRESSION TAG
  367. SEQADV 4HKD MSE B 434 UNP Q13188 EXPRESSION TAG
  368. SEQADV 4HKD ASP B 435 UNP Q13188 EXPRESSION TAG
  369. SEQADV 4HKD GLY C 432 UNP Q13188 EXPRESSION TAG
  370. SEQADV 4HKD ALA C 433 UNP Q13188 EXPRESSION TAG
  371. SEQADV 4HKD MSE C 434 UNP Q13188 EXPRESSION TAG
  372. SEQADV 4HKD ASP C 435 UNP Q13188 EXPRESSION TAG
  373. SEQADV 4HKD GLY D 432 UNP Q13188 EXPRESSION TAG
  374. SEQADV 4HKD ALA D 433 UNP Q13188 EXPRESSION TAG
  375. SEQADV 4HKD MSE D 434 UNP Q13188 EXPRESSION TAG
  376. SEQADV 4HKD ASP D 435 UNP Q13188 EXPRESSION TAG
  377. SEQRES 1 A 53 GLY ALA MSE ASP ASP PHE ASP PHE LEU LYS ASN LEU SER
  378. SEQRES 2 A 53 LEU GLU GLU LEU GLN MSE ARG LEU LYS ALA LEU ASP PRO
  379. SEQRES 3 A 53 MSE MSE GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR
  380. SEQRES 4 A 53 THR ALA LYS ARG GLN PRO ILE LEU ASP ALA MSE ASP ALA
  381. SEQRES 5 A 53 LYS
  382. SEQRES 1 B 53 GLY ALA MSE ASP ASP PHE ASP PHE LEU LYS ASN LEU SER
  383. SEQRES 2 B 53 LEU GLU GLU LEU GLN MSE ARG LEU LYS ALA LEU ASP PRO
  384. SEQRES 3 B 53 MSE MSE GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR
  385. SEQRES 4 B 53 THR ALA LYS ARG GLN PRO ILE LEU ASP ALA MSE ASP ALA
  386. SEQRES 5 B 53 LYS
  387. SEQRES 1 C 53 GLY ALA MSE ASP ASP PHE ASP PHE LEU LYS ASN LEU SER
  388. SEQRES 2 C 53 LEU GLU GLU LEU GLN MSE ARG LEU LYS ALA LEU ASP PRO
  389. SEQRES 3 C 53 MSE MSE GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR
  390. SEQRES 4 C 53 THR ALA LYS ARG GLN PRO ILE LEU ASP ALA MSE ASP ALA
  391. SEQRES 5 C 53 LYS
  392. SEQRES 1 D 53 GLY ALA MSE ASP ASP PHE ASP PHE LEU LYS ASN LEU SER
  393. SEQRES 2 D 53 LEU GLU GLU LEU GLN MSE ARG LEU LYS ALA LEU ASP PRO
  394. SEQRES 3 D 53 MSE MSE GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR
  395. SEQRES 4 D 53 THR ALA LYS ARG GLN PRO ILE LEU ASP ALA MSE ASP ALA
  396. SEQRES 5 D 53 LYS
  397. MODRES 4HKD MSE A 450 MET SELENOMETHIONINE
  398. MODRES 4HKD MSE A 458 MET SELENOMETHIONINE
  399. MODRES 4HKD MSE A 459 MET SELENOMETHIONINE
  400. MODRES 4HKD MSE A 481 MET SELENOMETHIONINE
  401. MODRES 4HKD MSE B 434 MET SELENOMETHIONINE
  402. MODRES 4HKD MSE B 450 MET SELENOMETHIONINE
  403. MODRES 4HKD MSE B 458 MET SELENOMETHIONINE
  404. MODRES 4HKD MSE B 459 MET SELENOMETHIONINE
  405. MODRES 4HKD MSE B 481 MET SELENOMETHIONINE
  406. MODRES 4HKD MSE C 434 MET SELENOMETHIONINE
  407. MODRES 4HKD MSE C 450 MET SELENOMETHIONINE
  408. MODRES 4HKD MSE C 458 MET SELENOMETHIONINE
  409. MODRES 4HKD MSE C 459 MET SELENOMETHIONINE
  410. MODRES 4HKD MSE C 481 MET SELENOMETHIONINE
  411. MODRES 4HKD MSE D 434 MET SELENOMETHIONINE
  412. MODRES 4HKD MSE D 450 MET SELENOMETHIONINE
  413. MODRES 4HKD MSE D 458 MET SELENOMETHIONINE
  414. MODRES 4HKD MSE D 459 MET SELENOMETHIONINE
  415. MODRES 4HKD MSE D 481 MET SELENOMETHIONINE
  416. HET MSE A 450 8
  417. HET MSE A 458 8
  418. HET MSE A 459 8
  419. HET MSE A 481 8
  420. HET MSE B 434 8
  421. HET MSE B 450 16
  422. HET MSE B 458 8
  423. HET MSE B 459 8
  424. HET MSE B 481 8
  425. HET MSE C 434 8
  426. HET MSE C 450 8
  427. HET MSE C 458 16
  428. HET MSE C 459 8
  429. HET MSE C 481 8
  430. HET MSE D 434 8
  431. HET MSE D 450 16
  432. HET MSE D 458 8
  433. HET MSE D 459 8
  434. HET MSE D 481 8
  435. HETNAM MSE SELENOMETHIONINE
  436. FORMUL 1 MSE 19(C5 H11 N O2 SE)
  437. FORMUL 5 HOH *239(H2 O)
  438. HELIX 1 1 ASP A 436 LYS A 441 1 6
  439. HELIX 2 2 SER A 444 LYS A 484 1 41
  440. HELIX 3 3 ALA B 433 ASN B 442 1 10
  441. HELIX 4 4 SER B 444 ASP B 482 1 39
  442. HELIX 5 5 ALA C 433 LYS C 441 1 9
  443. HELIX 6 6 SER C 444 ASP C 482 1 39
  444. HELIX 7 7 ALA C 483 LYS C 484 5 2
  445. HELIX 8 8 GLY D 432 ASP D 435 5 4
  446. HELIX 9 9 ASP D 436 LYS D 441 1 6
  447. HELIX 10 10 SER D 444 LYS D 484 1 41
  448. LINK C GLN A 449 N MSE A 450 1555 1555 1.32
  449. LINK C MSE A 450 N ARG A 451 1555 1555 1.32
  450. LINK C PRO A 457 N MSE A 458 1555 1555 1.33
  451. LINK C MSE A 458 N MSE A 459 1555 1555 1.33
  452. LINK C MSE A 459 N GLU A 460 1555 1555 1.33
  453. LINK C ALA A 480 N MSE A 481 1555 1555 1.33
  454. LINK C MSE A 481 N ASP A 482 1555 1555 1.33
  455. LINK C ALA B 433 N MSE B 434 1555 1555 1.33
  456. LINK C MSE B 434 N ASP B 435 1555 1555 1.33
  457. LINK C GLN B 449 N AMSE B 450 1555 1555 1.33
  458. LINK C GLN B 449 N BMSE B 450 1555 1555 1.33
  459. LINK C AMSE B 450 N ARG B 451 1555 1555 1.33
  460. LINK C BMSE B 450 N ARG B 451 1555 1555 1.33
  461. LINK C PRO B 457 N MSE B 458 1555 1555 1.33
  462. LINK C MSE B 458 N MSE B 459 1555 1555 1.33
  463. LINK C MSE B 459 N GLU B 460 1555 1555 1.33
  464. LINK C ALA B 480 N MSE B 481 1555 1555 1.33
  465. LINK C MSE B 481 N ASP B 482 1555 1555 1.33
  466. LINK C ALA C 433 N MSE C 434 1555 1555 1.33
  467. LINK C MSE C 434 N ASP C 435 1555 1555 1.33
  468. LINK C GLN C 449 N MSE C 450 1555 1555 1.33
  469. LINK C MSE C 450 N ARG C 451 1555 1555 1.33
  470. LINK C PRO C 457 N AMSE C 458 1555 1555 1.33
  471. LINK C PRO C 457 N BMSE C 458 1555 1555 1.33
  472. LINK C AMSE C 458 N MSE C 459 1555 1555 1.33
  473. LINK C BMSE C 458 N MSE C 459 1555 1555 1.33
  474. LINK C MSE C 459 N GLU C 460 1555 1555 1.33
  475. LINK C ALA C 480 N MSE C 481 1555 1555 1.33
  476. LINK C MSE C 481 N ASP C 482 1555 1555 1.33
  477. LINK C ALA D 433 N MSE D 434 1555 1555 1.33
  478. LINK C MSE D 434 N ASP D 435 1555 1555 1.33
  479. LINK C GLN D 449 N AMSE D 450 1555 1555 1.32
  480. LINK C GLN D 449 N BMSE D 450 1555 1555 1.33
  481. LINK C AMSE D 450 N ARG D 451 1555 1555 1.33
  482. LINK C BMSE D 450 N ARG D 451 1555 1555 1.34
  483. LINK C PRO D 457 N MSE D 458 1555 1555 1.33
  484. LINK C MSE D 458 N MSE D 459 1555 1555 1.33
  485. LINK C MSE D 459 N GLU D 460 1555 1555 1.33
  486. LINK C ALA D 480 N MSE D 481 1555 1555 1.33
  487. LINK C MSE D 481 N ASP D 482 1555 1555 1.33
  488. CISPEP 1 ASP A 435 ASP A 436 0 -8.81
  489. CRYST1 42.205 44.615 209.155 90.00 90.00 90.00 C 2 2 21 32
  490. ORIGX1 1.000000 0.000000 0.000000 0.00000
  491. ORIGX2 0.000000 1.000000 0.000000 0.00000
  492. ORIGX3 0.000000 0.000000 1.000000 0.00000
  493. SCALE1 0.023694 0.000000 0.000000 0.00000
  494. SCALE2 0.000000 0.022414 0.000000 0.00000
  495. SCALE3 0.000000 0.000000 0.004781 0.00000
  496. ATOM 1 N ASP A 435 7.397 28.376 121.784 1.00 34.35 N
  497. ATOM 2 CA ASP A 435 8.023 27.301 122.545 1.00 30.66 C
  498. ATOM 3 C ASP A 435 8.170 27.721 124.009 1.00 31.39 C
  499. ATOM 4 O ASP A 435 9.078 28.509 124.284 1.00 38.78 O
  500. ATOM 5 CB ASP A 435 9.401 26.976 121.961 1.00 27.46 C
  501. ATOM 6 CG ASP A 435 9.914 25.635 122.420 1.00 24.04 C
  502. ATOM 7 OD1 ASP A 435 9.199 24.998 123.211 1.00 24.18 O
  503. ATOM 8 OD2 ASP A 435 11.011 25.218 122.003 1.00 23.94 O
  504. ATOM 9 N ASP A 436 7.339 27.281 124.975 1.00 32.37 N
  505. ATOM 10 CA ASP A 436 6.060 26.501 124.940 1.00 25.92 C
  506. ATOM 11 C ASP A 436 6.063 24.996 125.322 1.00 16.49 C
  507. ATOM 12 O ASP A 436 5.077 24.496 125.896 1.00 14.09 O
  508. ATOM 13 CB ASP A 436 5.142 26.791 123.744 1.00 29.64 C
  509. ATOM 14 CG ASP A 436 3.699 26.819 124.135 1.00 28.48 C
  510. ATOM 15 OD1 ASP A 436 3.432 26.847 125.357 1.00 31.15 O
  511. ATOM 16 OD2 ASP A 436 2.833 26.829 123.231 1.00 33.93 O
  512. ATOM 17 N PHE A 437 7.151 24.297 125.003 1.00 15.81 N
  513. ATOM 18 CA PHE A 437 7.386 22.915 125.436 1.00 14.21 C
  514. ATOM 19 C PHE A 437 7.176 22.710 126.939 1.00 13.59 C
  515. ATOM 20 O PHE A 437 6.668 21.664 127.370 1.00 12.07 O
  516. ATOM 21 CB PHE A 437 8.813 22.492 125.052 1.00 11.84 C
  517. ATOM 22 CG PHE A 437 9.180 21.102 125.485 1.00 12.76 C
  518. ATOM 23 CD1 PHE A 437 9.808 20.889 126.695 1.00 12.93 C
  519. ATOM 24 CD2 PHE A 437 8.921 20.014 124.678 1.00 11.83 C
  520. ATOM 25 CE1 PHE A 437 10.168 19.627 127.098 1.00 13.67 C
  521. ATOM 26 CE2 PHE A 437 9.274 18.731 125.083 1.00 11.82 C
  522. ATOM 27 CZ PHE A 437 9.896 18.544 126.296 1.00 13.63 C
  523. ATOM 28 N ASP A 438 7.569 23.689 127.748 1.00 13.20 N
  524. ATOM 29 CA ASP A 438 7.497 23.504 129.190 1.00 12.53 C
  525. ATOM 30 C ASP A 438 6.055 23.281 129.660 1.00 12.88 C
  526. ATOM 31 O ASP A 438 5.821 22.634 130.680 1.00 13.48 O
  527. ATOM 32 CB ASP A 438 8.148 24.673 129.936 1.00 12.82 C
  528. ATOM 33 CG ASP A 438 8.283 24.407 131.412 1.00 17.18 C
  529. ATOM 34 OD1 ASP A 438 9.153 23.597 131.783 1.00 17.73 O
  530. ATOM 35 OD2 ASP A 438 7.530 25.009 132.208 1.00 18.39 O
  531. ATOM 36 N PHE A 439 5.102 23.813 128.903 1.00 12.35 N
  532. ATOM 37 CA PHE A 439 3.680 23.598 129.138 1.00 12.15 C
  533. ATOM 38 C PHE A 439 3.198 22.327 128.463 1.00 10.82 C
  534. ATOM 39 O PHE A 439 2.556 21.477 129.092 1.00 11.41 O
  535. ATOM 40 CB PHE A 439 2.898 24.793 128.577 1.00 12.00 C
  536. ATOM 41 CG PHE A 439 1.401 24.585 128.503 1.00 13.52 C
  537. ATOM 42 CD1 PHE A 439 0.630 24.556 129.653 1.00 14.61 C
  538. ATOM 43 CD2 PHE A 439 0.764 24.461 127.276 1.00 17.22 C
  539. ATOM 44 CE1 PHE A 439 -0.741 24.381 129.591 1.00 14.82 C
  540. ATOM 45 CE2 PHE A 439 -0.618 24.292 127.196 1.00 16.51 C
  541. ATOM 46 CZ PHE A 439 -1.377 24.254 128.362 1.00 16.11 C
  542. ATOM 47 N LEU A 440 3.527 22.201 127.181 1.00 12.77 N
  543. ATOM 48 CA LEU A 440 3.028 21.108 126.370 1.00 11.12 C
  544. ATOM 49 C LEU A 440 3.466 19.745 126.882 1.00 11.44 C
  545. ATOM 50 O LEU A 440 2.744 18.759 126.715 1.00 11.57 O
  546. ATOM 51 CB LEU A 440 3.491 21.284 124.924 1.00 11.71 C
  547. ATOM 52 CG LEU A 440 2.954 22.544 124.244 1.00 12.28 C
  548. ATOM 53 CD1 LEU A 440 3.776 22.778 122.985 1.00 15.91 C
  549. ATOM 54 CD2 LEU A 440 1.470 22.402 123.935 1.00 14.17 C
  550. ATOM 55 N LYS A 441 4.654 19.665 127.484 1.00 11.08 N
  551. ATOM 56 CA LYS A 441 5.150 18.385 127.971 1.00 11.59 C
  552. ATOM 57 C LYS A 441 4.278 17.784 129.070 1.00 12.32 C
  553. ATOM 58 O LYS A 441 4.397 16.596 129.362 1.00 17.08 O
  554. ATOM 59 CB LYS A 441 6.581 18.522 128.489 1.00 13.49 C
  555. ATOM 60 CG LYS A 441 6.663 19.273 129.800 1.00 13.47 C
  556. ATOM 61 CD LYS A 441 8.088 19.357 130.282 1.00 15.27 C
  557. ATOM 62 CE LYS A 441 8.153 20.120 131.571 1.00 15.43 C
  558. ATOM 63 NZ LYS A 441 9.508 20.078 132.143 1.00 18.04 N
  559. ATOM 64 N ASN A 442 3.455 18.609 129.710 1.00 11.43 N
  560. ATOM 65 CA ASN A 442 2.582 18.157 130.796 1.00 12.58 C
  561. ATOM 66 C ASN A 442 1.234 17.642 130.298 1.00 11.53 C
  562. ATOM 67 O ASN A 442 0.402 17.176 131.086 1.00 14.01 O
  563. ATOM 68 CB ASN A 442 2.311 19.299 131.782 1.00 13.55 C
  564. ATOM 69 CG ASN A 442 3.542 19.749 132.507 1.00 17.83 C
  565. ATOM 70 OD1 ASN A 442 4.403 18.949 132.824 1.00 18.24 O
  566. ATOM 71 ND2 ASN A 442 3.634 21.047 132.773 1.00 19.93 N
  567. ATOM 72 N LEU A 443 1.004 17.730 128.994 1.00 10.71 N
  568. ATOM 73 CA LEU A 443 -0.316 17.420 128.439 1.00 11.41 C
  569. ATOM 74 C LEU A 443 -0.403 15.977 127.965 1.00 10.11 C
  570. ATOM 75 O LEU A 443 0.618 15.348 127.695 1.00 12.03 O
  571. ATOM 76 CB LEU A 443 -0.652 18.370 127.290 1.00 11.98 C
  572. ATOM 77 CG LEU A 443 -0.499 19.867 127.580 1.00 12.95 C
  573. ATOM 78 CD1 LEU A 443 -0.993 20.713 126.391 1.00 15.86 C
  574. ATOM 79 CD2 LEU A 443 -1.198 20.263 128.882 1.00 13.38 C
  575. ATOM 80 N SER A 444 -1.619 15.453 127.847 1.00 10.97 N
  576. ATOM 81 CA SER A 444 -1.784 14.082 127.370 1.00 11.19 C
  577. ATOM 82 C SER A 444 -1.443 13.998 125.892 1.00 12.53 C
  578. ATOM 83 O SER A 444 -1.469 15.005 125.186 1.00 11.03 O
  579. ATOM 84 CB SER A 444 -3.221 13.602 127.574 1.00 11.34 C
  580. ATOM 85 OG SER A 444 -4.096 14.212 126.643 1.00 12.32 O
  581. ATOM 86 N LEU A 445 -1.126 12.802 125.416 1.00 11.98 N
  582. ATOM 87 CA LEU A 445 -0.960 12.601 123.981 1.00 13.18 C
  583. ATOM 88 C LEU A 445 -2.190 12.977 123.152 1.00 13.65 C
  584. ATOM 89 O LEU A 445 -2.057 13.528 122.069 1.00 13.61 O
  585. ATOM 90 CB LEU A 445 -0.536 11.171 123.681 1.00 14.38 C
  586. ATOM 91 CG LEU A 445 0.884 10.835 124.139 1.00 16.51 C
  587. ATOM 92 CD1 LEU A 445 1.148 9.343 124.030 1.00 18.18 C
  588. ATOM 93 CD2 LEU A 445 1.889 11.647 123.321 1.00 16.39 C
  589. ATOM 94 N GLU A 446 -3.385 12.704 123.653 1.00 14.82 N
  590. ATOM 95 CA GLU A 446 -4.590 13.094 122.914 1.00 14.99 C
  591. ATOM 96 C GLU A 446 -4.677 14.609 122.739 1.00 15.26 C
  592. ATOM 97 O GLU A 446 -5.031 15.111 121.673 1.00 15.52 O
  593. ATOM 98 CB GLU A 446 -5.864 12.544 123.574 1.00 18.31 C
  594. ATOM 99 CG GLU A 446 -7.106 12.667 122.681 1.00 25.63 C
  595. ATOM 100 CD GLU A 446 -8.258 13.422 123.327 1.00 32.85 C
  596. ATOM 101 OE1 GLU A 446 -9.054 12.780 124.049 1.00 34.27 O
  597. ATOM 102 OE2 GLU A 446 -8.390 14.651 123.089 1.00 32.51 O
  598. ATOM 103 N GLU A 447 -4.345 15.339 123.794 1.00 11.49 N
  599. ATOM 104 CA GLU A 447 -4.386 16.797 123.754 1.00 11.12 C
  600. ATOM 105 C GLU A 447 -3.336 17.330 122.784 1.00 12.00 C
  601. ATOM 106 O GLU A 447 -3.604 18.240 122.008 1.00 13.14 O
  602. ATOM 107 CB GLU A 447 -4.164 17.363 125.162 1.00 13.56 C
  603. ATOM 108 CG GLU A 447 -4.083 18.866 125.231 1.00 15.61 C
  604. ATOM 109 CD GLU A 447 -5.421 19.540 125.043 1.00 19.34 C
  605. ATOM 110 OE1 GLU A 447 -6.456 18.846 125.116 1.00 21.54 O
  606. ATOM 111 OE2 GLU A 447 -5.445 20.765 124.816 1.00 22.56 O
  607. ATOM 112 N LEU A 448 -2.137 16.754 122.829 1.00 12.65 N
  608. ATOM 113 CA LEU A 448 -1.077 17.121 121.889 1.00 11.66 C
  609. ATOM 114 C LEU A 448 -1.494 16.832 120.438 1.00 12.79 C
  610. ATOM 115 O LEU A 448 -1.234 17.643 119.537 1.00 12.40 O
  611. ATOM 116 CB LEU A 448 0.204 16.366 122.239 1.00 12.85 C
  612. ATOM 117 CG LEU A 448 0.787 16.782 123.592 1.00 12.64 C
  613. ATOM 118 CD1 LEU A 448 1.961 15.924 123.935 1.00 14.59 C
  614. ATOM 119 CD2 LEU A 448 1.196 18.252 123.580 1.00 13.08 C
  615. ATOM 120 N GLN A 449 -2.143 15.686 120.218 1.00 12.29 N
  616. ATOM 121 CA GLN A 449 -2.662 15.333 118.893 1.00 12.99 C
  617. ATOM 122 C GLN A 449 -3.657 16.372 118.392 1.00 15.07 C
  618. ATOM 123 O GLN A 449 -3.635 16.757 117.221 1.00 14.50 O
  619. ATOM 124 CB GLN A 449 -3.314 13.948 118.912 1.00 15.18 C
  620. ATOM 125 CG GLN A 449 -2.330 12.806 118.967 1.00 14.92 C
  621. ATOM 126 CD GLN A 449 -2.853 11.592 119.709 1.00 17.95 C
  622. ATOM 127 OE1 GLN A 449 -4.056 11.297 119.695 1.00 20.83 O
  623. ATOM 128 NE2 GLN A 449 -1.948 10.876 120.359 1.00 14.98 N
  624. HETATM 129 N MSE A 450 -4.523 16.830 119.280 1.00 14.88 N
  625. HETATM 130 CA MSE A 450 -5.537 17.804 118.911 1.00 15.65 C
  626. HETATM 131 C MSE A 450 -4.879 19.123 118.543 1.00 17.10 C
  627. HETATM 132 O MSE A 450 -5.236 19.759 117.559 1.00 17.40 O
  628. HETATM 133 CB MSE A 450 -6.526 17.998 120.062 1.00 18.59 C
  629. HETATM 134 CG MSE A 450 -7.603 19.027 119.787 1.00 24.54 C
  630. HETATM 135 SE MSE A 450 -8.866 19.181 121.271 1.00 55.26 SE
  631. HETATM 136 CE MSE A 450 -7.749 20.188 122.510 1.00 28.83 C
  632. ATOM 137 N ARG A 451 -3.902 19.530 119.337 1.00 15.80 N
  633. ATOM 138 CA ARG A 451 -3.228 20.800 119.118 1.00 15.54 C
  634. ATOM 139 C ARG A 451 -2.430 20.827 117.826 1.00 16.64 C
  635. ATOM 140 O ARG A 451 -2.451 21.822 117.096 1.00 17.30 O
  636. ATOM 141 CB ARG A 451 -2.336 21.130 120.309 1.00 15.83 C
  637. ATOM 142 CG ARG A 451 -3.141 21.590 121.497 1.00 15.15 C
  638. ATOM 143 CD ARG A 451 -2.299 21.760 122.729 1.00 17.39 C
  639. ATOM 144 NE ARG A 451 -3.129 22.157 123.859 1.00 20.75 N
  640. ATOM 145 CZ ARG A 451 -3.148 23.376 124.384 1.00 19.32 C
  641. ATOM 146 NH1 ARG A 451 -2.371 24.327 123.883 1.00 22.53 N
  642. ATOM 147 NH2 ARG A 451 -3.928 23.639 125.422 1.00 21.47 N
  643. ATOM 148 N LEU A 452 -1.715 19.745 117.560 1.00 16.86 N
  644. ATOM 149 CA LEU A 452 -0.962 19.630 116.327 1.00 16.65 C
  645. ATOM 150 C LEU A 452 -1.894 19.683 115.110 1.00 19.13 C
  646. ATOM 151 O LEU A 452 -1.623 20.399 114.141 1.00 21.33 O
  647. ATOM 152 CB LEU A 452 -0.165 18.338 116.330 1.00 17.67 C
  648. ATOM 153 CG LEU A 452 0.814 18.176 115.172 1.00 19.79 C
  649. ATOM 154 CD1 LEU A 452 1.817 19.317 115.176 1.00 19.51 C
  650. ATOM 155 CD2 LEU A 452 1.500 16.872 115.356 1.00 21.98 C
  651. ATOM 156 N LYS A 453 -3.006 18.954 115.175 1.00 18.70 N
  652. ATOM 157 CA LYS A 453 -3.981 18.939 114.076 1.00 19.31 C
  653. ATOM 158 C LYS A 453 -4.571 20.326 113.803 1.00 21.74 C
  654. ATOM 159 O LYS A 453 -4.799 20.697 112.646 1.00 18.14 O
  655. ATOM 160 CB LYS A 453 -5.104 17.940 114.372 1.00 19.15 C
  656. ATOM 161 CG LYS A 453 -5.851 17.464 113.145 1.00 26.37 C
  657. ATOM 162 N ALA A 454 -4.810 21.089 114.868 1.00 15.75 N
  658. ATOM 163 CA ALA A 454 -5.413 22.414 114.759 1.00 19.04 C
  659. ATOM 164 C ALA A 454 -4.561 23.361 113.929 1.00 21.40 C
  660. ATOM 165 O ALA A 454 -5.064 24.339 113.378 1.00 22.46 O
  661. ATOM 166 CB ALA A 454 -5.656 23.001 116.142 1.00 20.00 C
  662. ATOM 167 N LEU A 455 -3.267 23.075 113.843 1.00 18.20 N
  663. ATOM 168 CA LEU A 455 -2.353 23.947 113.122 1.00 20.81 C
  664. ATOM 169 C LEU A 455 -2.588 23.890 111.617 1.00 18.42 C
  665. ATOM 170 O LEU A 455 -2.281 24.845 110.918 1.00 20.87 O
  666. ATOM 171 CB LEU A 455 -0.894 23.606 113.445 1.00 17.95 C
  667. ATOM 172 CG LEU A 455 -0.470 23.867 114.892 1.00 18.03 C
  668. ATOM 173 CD1 LEU A 455 0.988 23.447 115.099 1.00 17.14 C
  669. ATOM 174 CD2 LEU A 455 -0.670 25.320 115.247 1.00 23.85 C
  670. ATOM 175 N ASP A 456 -3.130 22.780 111.125 1.00 18.57 N
  671. ATOM 176 CA ASP A 456 -3.341 22.628 109.682 1.00 18.12 C
  672. ATOM 177 C ASP A 456 -4.392 23.599 109.124 1.00 23.64 C
  673. ATOM 178 O ASP A 456 -4.072 24.394 108.237 1.00 19.50 O
  674. ATOM 179 CB ASP A 456 -3.651 21.171 109.302 1.00 20.25 C
  675. ATOM 180 CG ASP A 456 -2.446 20.266 109.418 1.00 22.19 C
  676. ATOM 181 OD1 ASP A 456 -1.390 20.728 109.897 1.00 20.22 O
  677. ATOM 182 OD2 ASP A 456 -2.552 19.086 109.025 1.00 26.07 O
  678. ATOM 183 N PRO A 457 -5.634 23.564 109.640 1.00 23.70 N
  679. ATOM 184 CA PRO A 457 -6.572 24.556 109.102 1.00 20.45 C
  680. ATOM 185 C PRO A 457 -6.172 25.995 109.397 1.00 21.53 C
  681. ATOM 186 O PRO A 457 -6.533 26.900 108.647 1.00 23.46 O
  682. ATOM 187 CB PRO A 457 -7.888 24.222 109.807 1.00 24.59 C
  683. ATOM 188 CG PRO A 457 -7.745 22.787 110.206 1.00 26.26 C
  684. ATOM 189 CD PRO A 457 -6.305 22.649 110.587 1.00 24.32 C
  685. HETATM 190 N MSE A 458 -5.438 26.206 110.481 1.00 20.67 N
  686. HETATM 191 CA MSE A 458 -4.929 27.525 110.795 1.00 21.41 C
  687. HETATM 192 C MSE A 458 -3.956 28.006 109.728 1.00 22.83 C
  688. HETATM 193 O MSE A 458 -4.013 29.158 109.293 1.00 20.89 O
  689. HETATM 194 CB MSE A 458 -4.233 27.515 112.149 1.00 22.50 C
  690. HETATM 195 CG MSE A 458 -3.768 28.885 112.581 1.00 26.80 C
  691. HETATM 196 SE MSE A 458 -2.809 28.782 114.261 1.00 43.47 SE
  692. HETATM 197 CE MSE A 458 -3.964 27.475 115.158 1.00 21.77 C
  693. HETATM 198 N MSE A 459 -3.047 27.127 109.323 1.00 20.53 N
  694. HETATM 199 CA MSE A 459 -2.091 27.472 108.290 1.00 18.81 C
  695. HETATM 200 C MSE A 459 -2.810 27.728 106.975 1.00 20.89 C
  696. HETATM 201 O MSE A 459 -2.492 28.681 106.267 1.00 19.36 O
  697. HETATM 202 CB MSE A 459 -1.055 26.367 108.101 1.00 17.24 C
  698. HETATM 203 CG MSE A 459 -0.040 26.705 107.035 1.00 15.43 C
  699. HETATM 204 SE MSE A 459 1.354 25.373 106.858 1.00 22.78 SE
  700. HETATM 205 CE MSE A 459 0.380 24.019 105.869 1.00 19.69 C
  701. ATOM 206 N GLU A 460 -3.778 26.875 106.662 1.00 18.47 N
  702. ATOM 207 CA GLU A 460 -4.543 27.004 105.420 1.00 18.74 C
  703. ATOM 208 C GLU A 460 -5.313 28.315 105.350 1.00 22.20 C
  704. ATOM 209 O GLU A 460 -5.397 28.925 104.291 1.00 20.62 O
  705. ATOM 210 CB GLU A 460 -5.482 25.815 105.215 1.00 21.04 C
  706. ATOM 211 CG GLU A 460 -4.778 24.542 104.792 1.00 25.44 C
  707. ATOM 212 CD GLU A 460 -3.981 24.697 103.497 1.00 24.38 C
  708. ATOM 213 OE1 GLU A 460 -4.368 25.504 102.621 1.00 29.37 O
  709. ATOM 214 OE2 GLU A 460 -2.959 24.000 103.360 1.00 32.19 O
  710. ATOM 215 N ARG A 461 -5.878 28.748 106.473 1.00 22.68 N
  711. ATOM 216 CA ARG A 461 -6.553 30.043 106.524 1.00 24.34 C
  712. ATOM 217 C ARG A 461 -5.583 31.176 106.219 1.00 22.42 C
  713. ATOM 218 O ARG A 461 -5.918 32.121 105.497 1.00 25.07 O
  714. ATOM 219 CB ARG A 461 -7.222 30.272 107.887 1.00 24.53 C
  715. ATOM 220 CG ARG A 461 -8.425 29.394 108.150 1.00 26.38 C
  716. ATOM 221 CD ARG A 461 -9.188 29.848 109.387 1.00 28.06 C
  717. ATOM 222 NE ARG A 461 -8.384 29.820 110.609 1.00 27.00 N
  718. ATOM 223 CZ ARG A 461 -8.352 28.804 111.460 1.00 24.90 C
  719. ATOM 224 NH1 ARG A 461 -9.065 27.713 111.215 1.00 24.66 N
  720. ATOM 225 NH2 ARG A 461 -7.598 28.873 112.551 1.00 24.85 N
  721. ATOM 226 N GLU A 462 -4.371 31.078 106.757 1.00 22.74 N
  722. ATOM 227 CA GLU A 462 -3.355 32.098 106.536 1.00 20.49 C
  723. ATOM 228 C GLU A 462 -2.902 32.141 105.070 1.00 21.58 C
  724. ATOM 229 O GLU A 462 -2.633 33.220 104.516 1.00 20.45 O
  725. ATOM 230 CB GLU A 462 -2.156 31.853 107.445 1.00 23.08 C
  726. ATOM 231 N ILE A 463 -2.794 30.962 104.467 1.00 17.57 N
  727. ATOM 232 CA ILE A 463 -2.415 30.841 103.059 1.00 16.35 C
  728. ATOM 233 C ILE A 463 -3.504 31.410 102.148 1.00 21.08 C
  729. ATOM 234 O ILE A 463 -3.207 32.130 101.192 1.00 21.02 O
  730. ATOM 235 CB ILE A 463 -2.119 29.367 102.685 1.00 15.26 C
  731. ATOM 236 CG1 ILE A 463 -0.845 28.882 103.374 1.00 16.79 C
  732. ATOM 237 CG2 ILE A 463 -1.932 29.214 101.181 1.00 18.69 C
  733. ATOM 238 CD1 ILE A 463 -0.512 27.438 103.100 1.00 18.47 C
  734. ATOM 239 N GLU A 464 -4.761 31.097 102.450 1.00 20.49 N
  735. ATOM 240 CA GLU A 464 -5.888 31.631 101.679 1.00 20.67 C
  736. ATOM 241 C GLU A 464 -5.976 33.149 101.760 1.00 24.29 C
  737. ATOM 242 O GLU A 464 -6.197 33.824 100.752 1.00 22.25 O
  738. ATOM 243 CB GLU A 464 -7.205 31.004 102.130 1.00 24.72 C
  739. ATOM 244 CG GLU A 464 -7.350 29.548 101.735 1.00 25.78 C
  740. ATOM 245 N GLU A 465 -5.804 33.688 102.960 1.00 22.84 N
  741. ATOM 246 CA GLU A 465 -5.789 35.136 103.128 1.00 23.40 C
  742. ATOM 247 C GLU A 465 -4.675 35.763 102.304 1.00 23.21 C
  743. ATOM 248 O GLU A 465 -4.815 36.880 101.792 1.00 24.38 O
  744. ATOM 249 CB GLU A 465 -5.650 35.508 104.607 1.00 25.87 C
  745. ATOM 250 N LEU A 466 -3.567 35.039 102.169 1.00 24.37 N
  746. ATOM 251 CA LEU A 466 -2.437 35.518 101.390 1.00 23.52 C
  747. ATOM 252 C LEU A 466 -2.790 35.527 99.900 1.00 20.32 C
  748. ATOM 253 O LEU A 466 -2.556 36.513 99.204 1.00 23.21 O
  749. ATOM 254 CB LEU A 466 -1.209 34.651 101.660 1.00 24.56 C
  750. ATOM 255 CG LEU A 466 0.150 35.306 101.487 1.00 24.16 C
  751. ATOM 256 CD1 LEU A 466 1.156 34.629 102.389 1.00 25.62 C
  752. ATOM 257 CD2 LEU A 466 0.566 35.166 100.042 1.00 26.90 C
  753. ATOM 258 N ARG A 467 -3.376 34.437 99.425 1.00 19.54 N
  754. ATOM 259 CA ARG A 467 -3.817 34.378 98.038 1.00 18.55 C
  755. ATOM 260 C ARG A 467 -4.809 35.497 97.748 1.00 21.40 C
  756. ATOM 261 O ARG A 467 -4.744 36.140 96.703 1.00 21.57 O
  757. ATOM 262 CB ARG A 467 -4.441 33.017 97.721 1.00 19.71 C
  758. ATOM 263 CG ARG A 467 -3.452 31.860 97.715 1.00 23.22 C
  759. ATOM 264 CD ARG A 467 -4.147 30.545 97.411 1.00 23.31 C
  760. ATOM 265 NE ARG A 467 -3.230 29.409 97.467 1.00 25.92 N
  761. ATOM 266 CZ ARG A 467 -3.426 28.316 98.200 1.00 23.36 C
  762. ATOM 267 NH1 ARG A 467 -4.519 28.189 98.948 1.00 26.17 N
  763. ATOM 268 NH2 ARG A 467 -2.529 27.341 98.177 1.00 26.21 N
  764. ATOM 269 N GLN A 468 -5.722 35.739 98.683 1.00 22.17 N
  765. ATOM 270 CA GLN A 468 -6.733 36.776 98.481 1.00 22.98 C
  766. ATOM 271 C GLN A 468 -6.082 38.161 98.425 1.00 22.44 C
  767. ATOM 272 O GLN A 468 -6.526 39.040 97.673 1.00 26.26 O
  768. ATOM 273 CB GLN A 468 -7.820 36.683 99.562 1.00 23.10 C
  769. ATOM 274 CG GLN A 468 -9.144 37.311 99.175 1.00 25.71 C
  770. ATOM 275 CD GLN A 468 -9.770 36.649 97.965 1.00 29.33 C
  771. ATOM 276 OE1 GLN A 468 -9.992 35.435 97.943 1.00 33.35 O
  772. ATOM 277 NE2 GLN A 468 -10.060 37.447 96.947 1.00 28.00 N
  773. ATOM 278 N ARG A 469 -5.015 38.343 99.199 1.00 22.59 N
  774. ATOM 279 CA ARG A 469 -4.238 39.582 99.207 1.00 22.68 C
  775. ATOM 280 C ARG A 469 -3.606 39.861 97.847 1.00 23.36 C
  776. ATOM 281 O ARG A 469 -3.504 41.011 97.412 1.00 24.70 O
  777. ATOM 282 CB ARG A 469 -3.121 39.514 100.254 1.00 26.59 C
  778. ATOM 283 CG ARG A 469 -3.351 40.341 101.512 1.00 28.77 C
  779. ATOM 284 CD ARG A 469 -2.087 41.136 101.884 1.00 31.58 C
  780. ATOM 285 NE ARG A 469 -0.881 40.305 101.952 1.00 34.22 N
  781. ATOM 286 CZ ARG A 469 0.309 40.668 101.477 1.00 31.17 C
  782. ATOM 287 NH1 ARG A 469 0.463 41.848 100.890 1.00 35.03 N
  783. ATOM 288 NH2 ARG A 469 1.351 39.851 101.585 1.00 34.39 N
  784. ATOM 289 N TYR A 470 -3.168 38.801 97.186 1.00 20.87 N
  785. ATOM 290 CA TYR A 470 -2.549 38.939 95.875 1.00 20.67 C
  786. ATOM 291 C TYR A 470 -3.574 39.088 94.758 1.00 19.32 C
  787. ATOM 292 O TYR A 470 -3.302 39.753 93.764 1.00 20.17 O
  788. ATOM 293 CB TYR A 470 -1.572 37.791 95.614 1.00 18.57 C
  789. ATOM 294 CG TYR A 470 -0.225 38.055 96.229 1.00 20.58 C
  790. ATOM 295 CD1 TYR A 470 0.764 38.707 95.509 1.00 19.17 C
  791. ATOM 296 CD2 TYR A 470 0.053 37.683 97.539 1.00 21.66 C
  792. ATOM 297 CE1 TYR A 470 1.993 38.970 96.054 1.00 23.17 C
  793. ATOM 298 CE2 TYR A 470 1.290 37.939 98.100 1.00 21.98 C
  794. ATOM 299 CZ TYR A 470 2.255 38.587 97.351 1.00 22.14 C
  795. ATOM 300 OH TYR A 470 3.496 38.851 97.880 1.00 29.59 O
  796. ATOM 301 N THR A 471 -4.741 38.477 94.928 1.00 18.43 N
  797. ATOM 302 CA THR A 471 -5.869 38.716 94.022 1.00 17.74 C
  798. ATOM 303 C THR A 471 -6.207 40.209 93.975 1.00 22.35 C
  799. ATOM 304 O THR A 471 -6.491 40.765 92.908 1.00 16.95 O
  800. ATOM 305 CB THR A 471 -7.099 37.874 94.413 1.00 21.02 C
  801. ATOM 306 OG1 THR A 471 -6.812 36.479 94.220 1.00 23.19 O
  802. ATOM 307 CG2 THR A 471 -8.289 38.240 93.554 1.00 21.09 C
  803. ATOM 308 N ALA A 472 -6.131 40.868 95.128 1.00 22.76 N
  804. ATOM 309 CA ALA A 472 -6.373 42.310 95.222 1.00 19.27 C
  805. ATOM 310 C ALA A 472 -5.315 43.155 94.523 1.00 20.36 C
  806. ATOM 311 O ALA A 472 -5.549 44.323 94.207 1.00 20.32 O
  807. ATOM 312 CB ALA A 472 -6.492 42.724 96.680 1.00 21.05 C
  808. ATOM 313 N LYS A 473 -4.141 42.573 94.300 1.00 18.74 N
  809. ATOM 314 CA LYS A 473 -3.064 43.246 93.578 1.00 17.74 C
  810. ATOM 315 C LYS A 473 -3.142 42.953 92.079 1.00 14.74 C
  811. ATOM 316 O LYS A 473 -2.853 43.808 91.237 1.00 19.92 O
  812. ATOM 317 CB LYS A 473 -1.698 42.779 94.096 1.00 19.69 C
  813. ATOM 318 CG LYS A 473 -1.368 43.199 95.515 1.00 22.18 C
  814. ATOM 319 CD LYS A 473 0.044 42.749 95.860 1.00 23.93 C
  815. ATOM 320 CE LYS A 473 0.596 43.460 97.082 1.00 28.08 C
  816. ATOM 321 NZ LYS A 473 1.997 43.024 97.354 1.00 30.70 N
  817. ATOM 322 N ARG A 474 -3.544 41.728 91.768 1.00 16.73 N
  818. ATOM 323 CA ARG A 474 -3.554 41.220 90.403 1.00 15.21 C
  819. ATOM 324 C ARG A 474 -4.666 41.798 89.546 1.00 17.79 C
  820. ATOM 325 O ARG A 474 -4.438 42.206 88.404 1.00 13.95 O
  821. ATOM 326 CB ARG A 474 -3.684 39.697 90.439 1.00 15.05 C
  822. ATOM 327 CG ARG A 474 -3.412 39.031 89.108 1.00 16.83 C
  823. ATOM 328 CD ARG A 474 -3.682 37.533 89.184 1.00 17.67 C
  824. ATOM 329 NE ARG A 474 -2.762 36.836 90.078 1.00 20.03 N
  825. ATOM 330 CZ ARG A 474 -3.106 36.303 91.252 1.00 17.83 C
  826. ATOM 331 NH1 ARG A 474 -4.364 36.384 91.677 1.00 17.56 N
  827. ATOM 332 NH2 ARG A 474 -2.194 35.678 91.987 1.00 19.46 N
  828. ATOM 333 N GLN A 475 -5.871 41.814 90.099 1.00 16.07 N
  829. ATOM 334 CA GLN A 475 -7.037 42.317 89.385 1.00 16.58 C
  830. ATOM 335 C GLN A 475 -6.843 43.741 88.859 1.00 14.33 C
  831. ATOM 336 O GLN A 475 -7.081 43.979 87.672 1.00 12.57 O
  832. ATOM 337 CB GLN A 475 -8.311 42.187 90.234 1.00 16.21 C
  833. ATOM 338 CG GLN A 475 -8.777 40.749 90.413 1.00 18.05 C
  834. ATOM 339 CD GLN A 475 -10.153 40.619 91.060 1.00 21.79 C
  835. ATOM 340 OE1 GLN A 475 -10.525 41.397 91.941 1.00 23.35 O
  836. ATOM 341 NE2 GLN A 475 -10.909 39.624 90.624 1.00 23.94 N
  837. ATOM 342 N PRO A 476 -6.386 44.682 89.702 1.00 13.38 N
  838. ATOM 343 CA PRO A 476 -6.233 46.031 89.136 1.00 12.52 C
  839. ATOM 344 C PRO A 476 -5.134 46.139 88.073 1.00 14.73 C
  840. ATOM 345 O PRO A 476 -5.208 47.011 87.209 1.00 13.84 O
  841. ATOM 346 CB PRO A 476 -5.916 46.910 90.353 1.00 17.80 C
  842. ATOM 347 CG PRO A 476 -5.473 45.967 91.412 1.00 22.20 C
  843. ATOM 348 CD PRO A 476 -6.219 44.689 91.172 1.00 15.35 C
  844. ATOM 349 N ILE A 477 -4.111 45.295 88.138 1.00 13.28 N
  845. ATOM 350 CA ILE A 477 -3.101 45.299 87.087 1.00 13.70 C
  846. ATOM 351 C ILE A 477 -3.719 44.813 85.774 1.00 12.78 C
  847. ATOM 352 O ILE A 477 -3.540 45.441 84.721 1.00 12.10 O
  848. ATOM 353 CB ILE A 477 -1.895 44.426 87.444 1.00 13.40 C
  849. ATOM 354 CG1 ILE A 477 -1.164 44.976 88.662 1.00 17.30 C
  850. ATOM 355 CG2 ILE A 477 -0.948 44.341 86.264 1.00 14.16 C
  851. ATOM 356 CD1 ILE A 477 -0.125 44.004 89.207 1.00 14.86 C
  852. ATOM 357 N LEU A 478 -4.453 43.711 85.837 1.00 11.56 N
  853. ATOM 358 CA LEU A 478 -5.117 43.175 84.651 1.00 11.38 C
  854. ATOM 359 C LEU A 478 -6.095 44.183 84.079 1.00 12.55 C
  855. ATOM 360 O LEU A 478 -6.151 44.390 82.868 1.00 12.82 O
  856. ATOM 361 CB LEU A 478 -5.825 41.856 84.961 1.00 12.53 C
  857. ATOM 362 CG LEU A 478 -4.826 40.718 85.164 1.00 14.60 C
  858. ATOM 363 CD1 LEU A 478 -5.520 39.506 85.743 1.00 18.07 C
  859. ATOM 364 CD2 LEU A 478 -4.095 40.368 83.852 1.00 13.53 C
  860. ATOM 365 N ASP A 479 -6.858 44.820 84.957 1.00 11.63 N
  861. ATOM 366 CA ASP A 479 -7.826 45.826 84.516 1.00 10.65 C
  862. ATOM 367 C ASP A 479 -7.143 47.038 83.864 1.00 12.50 C
  863. ATOM 368 O ASP A 479 -7.610 47.540 82.845 1.00 11.81 O
  864. ATOM 369 CB ASP A 479 -8.753 46.250 85.674 1.00 11.37 C
  865. ATOM 370 CG ASP A 479 -9.575 45.082 86.237 1.00 13.02 C
  866. ATOM 371 OD1 ASP A 479 -9.570 43.977 85.660 1.00 14.76 O
  867. ATOM 372 OD2 ASP A 479 -10.259 45.283 87.267 1.00 16.15 O
  868. ATOM 373 N ALA A 480 -6.039 47.502 84.456 1.00 11.09 N
  869. ATOM 374 CA ALA A 480 -5.274 48.617 83.904 1.00 12.53 C
  870. ATOM 375 C ALA A 480 -4.757 48.297 82.499 1.00 13.80 C
  871. ATOM 376 O ALA A 480 -4.764 49.151 81.609 1.00 15.55 O
  872. ATOM 377 CB ALA A 480 -4.123 48.983 84.832 1.00 14.52 C
  873. HETATM 378 N MSE A 481 -4.311 47.064 82.302 1.00 11.80 N
  874. HETATM 379 CA MSE A 481 -3.835 46.641 80.994 1.00 13.25 C
  875. HETATM 380 C MSE A 481 -4.965 46.643 79.972 1.00 13.84 C
  876. HETATM 381 O MSE A 481 -4.793 47.100 78.833 1.00 13.49 O
  877. HETATM 382 CB MSE A 481 -3.203 45.258 81.074 1.00 9.50 C
  878. HETATM 383 CG MSE A 481 -1.937 45.229 81.914 1.00 9.58 C
  879. HETATM 384 SE MSE A 481 -0.958 43.547 81.786 1.00 18.77 SE
  880. HETATM 385 CE MSE A 481 -0.263 43.735 79.991 1.00 16.62 C
  881. ATOM 386 N ASP A 482 -6.129 46.161 80.390 1.00 10.93 N
  882. ATOM 387 CA ASP A 482 -7.284 46.069 79.515 1.00 12.38 C
  883. ATOM 388 C ASP A 482 -7.977 47.421 79.309 1.00 12.53 C
  884. ATOM 389 O ASP A 482 -8.819 47.559 78.416 1.00 14.05 O
  885. ATOM 390 CB ASP A 482 -8.288 45.050 80.071 1.00 12.02 C
  886. ATOM 391 CG ASP A 482 -9.316 44.625 79.044 1.00 12.47 C
  887. ATOM 392 OD1 ASP A 482 -8.927 44.250 77.923 1.00 14.90 O
  888. ATOM 393 OD2 ASP A 482 -10.528 44.683 79.332 1.00 16.25 O
  889. ATOM 394 N ALA A 483 -7.616 48.407 80.123 1.00 14.48 N
  890. ATOM 395 CA ALA A 483 -8.224 49.734 80.064 1.00 16.63 C
  891. ATOM 396 C ALA A 483 -7.563 50.639 79.035 1.00 18.40 C
  892. ATOM 397 O ALA A 483 -8.113 51.680 78.677 1.00 21.77 O
  893. ATOM 398 CB ALA A 483 -8.189 50.404 81.438 1.00 15.82 C
  894. ATOM 399 N LYS A 484 -6.379 50.267 78.572 1.00 17.56 N
  895. ATOM 400 CA LYS A 484 -5.706 51.081 77.568 1.00 19.53 C
  896. ATOM 401 C LYS A 484 -6.298 50.873 76.181 1.00 21.46 C
  897. ATOM 402 O LYS A 484 -6.813 49.799 75.862 1.00 21.43 O
  898. ATOM 403 CB LYS A 484 -4.213 50.788 77.560 1.00 20.53 C
  899. ATOM 404 CG LYS A 484 -3.552 51.105 78.858 1.00 21.77 C
  900. ATOM 405 CD LYS A 484 -2.123 51.487 78.632 1.00 24.72 C
  901. ATOM 406 CE LYS A 484 -1.416 51.621 79.940 1.00 21.37 C
  902. ATOM 407 NZ LYS A 484 -1.976 52.712 80.776 1.00 24.13 N
  903. ATOM 408 OXT LYS A 484 -6.290 51.786 75.346 1.00 28.50 O
  904. TER 409 LYS A 484
  905. HETATM 1756 O HOH A 501 -0.923 10.560 127.393 1.00 16.58 O
  906. HETATM 1757 O HOH A 502 9.272 22.148 134.167 1.00 15.08 O
  907. HETATM 1758 O HOH A 503 0.109 20.243 112.094 1.00 20.74 O
  908. HETATM 1759 O HOH A 504 -3.930 10.522 125.779 1.00 20.79 O
  909. HETATM 1760 O HOH A 505 -0.759 36.323 88.018 1.00 17.42 O
  910. HETATM 1761 O HOH A 506 -4.645 51.936 81.852 1.00 21.43 O
  911. HETATM 1762 O HOH A 507 -3.900 17.103 128.596 1.00 14.08 O
  912. HETATM 1763 O HOH A 508 6.834 21.053 135.062 1.00 16.98 O
  913. HETATM 1764 O HOH A 509 -1.709 8.163 126.388 1.00 21.28 O
  914. HETATM 1765 O HOH A 510 -6.178 53.926 80.841 1.00 22.51 O
  915. HETATM 1766 O HOH A 511 -3.874 34.920 94.206 1.00 19.34 O
  916. HETATM 1767 O HOH A 512 -2.271 14.925 115.464 1.00 20.03 O
  917. HETATM 1768 O HOH A 513 -4.246 31.998 93.867 1.00 22.43 O
  918. HETATM 1769 O HOH A 514 -8.028 54.104 78.963 1.00 23.92 O
  919. HETATM 1770 O HOH A 515 -8.633 26.494 106.913 1.00 26.07 O
  920. HETATM 1771 O HOH A 516 -0.590 28.861 96.048 1.00 24.28 O
  921. HETATM 1772 O HOH A 517 -2.720 24.283 118.285 1.00 25.45 O
  922. HETATM 1773 O HOH A 518 9.282 26.082 126.906 1.00 24.09 O
  923. HETATM 1774 O HOH A 519 6.015 26.868 128.250 1.00 24.80 O
  924. HETATM 1775 O HOH A 520 -1.450 35.660 105.568 1.00 31.08 O
  925. HETATM 1776 O HOH A 521 -9.113 42.329 83.139 1.00 25.68 O
  926. HETATM 1777 O HOH A 522 -7.853 19.549 116.416 1.00 25.49 O
  927. HETATM 1778 O HOH A 523 -6.915 21.942 106.809 1.00 28.30 O
  928. HETATM 1779 O HOH A 524 -1.085 23.498 102.526 1.00 24.33 O
  929. HETATM 1780 O HOH A 525 7.386 14.818 129.490 1.00 25.48 O
  930. HETATM 1781 O HOH A 526 -2.313 36.927 85.735 1.00 22.53 O
  931. HETATM 1782 O HOH A 527 -1.420 45.858 92.153 1.00 25.98 O
  932. HETATM 1783 O HOH A 528 -7.683 34.918 91.688 1.00 30.35 O
  933. HETATM 1784 O HOH A 529 5.798 23.023 133.475 1.00 25.95 O
  934. HETATM 1785 O HOH A 530 1.230 28.143 125.792 1.00 31.35 O
  935. HETATM 1786 O HOH A 531 -5.628 54.301 75.787 1.00 30.74 O
  936. HETATM 1787 O HOH A 532 -7.095 36.790 90.323 1.00 28.32 O
  937. HETATM 1788 O HOH A 533 -5.920 51.354 72.921 1.00 24.51 O
  938. HETATM 1789 O HOH A 534 -10.366 49.727 77.141 1.00 22.50 O
  939. HETATM 1790 O HOH A 535 -8.952 31.894 104.884 1.00 28.60 O
  940. HETATM 1791 O HOH A 536 -3.767 43.250 98.715 1.00 27.86 O
  941. HETATM 1792 O HOH A 537 -8.460 20.657 113.837 1.00 26.68 O
  942. HETATM 1793 O HOH A 538 -5.843 42.804 100.332 1.00 31.69 O
  943. HETATM 1794 O HOH A 539 -0.894 24.556 121.485 1.00 28.68 O
  944. HETATM 1795 O HOH A 540 -6.066 9.602 121.168 1.00 24.72 O
  945. HETATM 1796 O HOH A 541 -8.745 23.492 106.175 1.00 30.52 O
  946. HETATM 1797 O HOH A 542 -6.197 11.291 126.842 1.00 28.41 O
  947. HETATM 1798 O HOH A 543 -10.381 55.071 77.667 1.00 32.81 O
  948. HETATM 1799 O HOH A 544 -7.509 25.382 113.808 1.00 27.21 O
  949. HETATM 1800 O HOH A 545 1.541 17.743 111.417 1.00 23.03 O
  950. HETATM 1801 O HOH A 546 0.787 26.274 124.180 1.00 28.89 O
  951. HETATM 1802 O HOH A 547 -6.866 34.595 107.456 1.00 32.21 O
  952. HETATM 1803 O HOH A 548 -9.429 34.843 103.190 1.00 31.83 O
  953. HETATM 1804 O HOH A 549 7.152 15.964 131.671 1.00 27.75 O
  954. HETATM 1805 O HOH A 550 9.576 15.601 130.061 1.00 28.72 O
  955. HETATM 1806 O HOH A 551 -5.027 8.954 123.822 1.00 28.70 O
  956. HETATM 1807 O HOH A 552 -4.470 25.803 126.775 1.00 28.65 O
  957. CONECT 122 129
  958. CONECT 129 122 130
  959. CONECT 130 129 131 133
  960. CONECT 131 130 132 137
  961. CONECT 132 131
  962. CONECT 133 130 134
  963. CONECT 134 133 135
  964. CONECT 135 134 136
  965. CONECT 136 135
  966. CONECT 137 131
  967. CONECT 185 190
  968. CONECT 190 185 191
  969. CONECT 191 190 192 194
  970. CONECT 192 191 193 198
  971. CONECT 193 192
  972. CONECT 194 191 195
  973. CONECT 195 194 196
  974. CONECT 196 195 197
  975. CONECT 197 196
  976. CONECT 198 192 199
  977. CONECT 199 198 200 202
  978. CONECT 200 199 201 206
  979. CONECT 201 200
  980. CONECT 202 199 203
  981. CONECT 203 202 204
  982. CONECT 204 203 205
  983. CONECT 205 204
  984. CONECT 206 200
  985. CONECT 375 378
  986. CONECT 378 375 379
  987. CONECT 379 378 380 382
  988. CONECT 380 379 381 386
  989. CONECT 381 380
  990. CONECT 382 379 383
  991. CONECT 383 382 384
  992. CONECT 384 383 385
  993. CONECT 385 384
  994. CONECT 386 380
  995. CONECT 416 419
  996. CONECT 419 416 420
  997. CONECT 420 419 421 423
  998. CONECT 421 420 422 427
  999. CONECT 422 421
  1000. CONECT 423 420 424
  1001. CONECT 424 423 425
  1002. CONECT 425 424 426
  1003. CONECT 426 425
  1004. CONECT 427 421
  1005. CONECT 547 554 555
  1006. CONECT 554 547 556
  1007. CONECT 555 547 557
  1008. CONECT 556 554 558 562
  1009. CONECT 557 555 559 563
  1010. CONECT 558 556 560 570
  1011. CONECT 559 557 561 570
  1012. CONECT 560 558
  1013. CONECT 561 559
  1014. CONECT 562 556 564
  1015. CONECT 563 557 565
  1016. CONECT 564 562 566
  1017. CONECT 565 563 567
  1018. CONECT 566 564 568
  1019. CONECT 567 565 569
  1020. CONECT 568 566
  1021. CONECT 569 567
  1022. CONECT 570 558 559
  1023. CONECT 620 625
  1024. CONECT 625 620 626
  1025. CONECT 626 625 627 629
  1026. CONECT 627 626 628 633
  1027. CONECT 628 627
  1028. CONECT 629 626 630
  1029. CONECT 630 629 631
  1030. CONECT 631 630 632
  1031. CONECT 632 631
  1032. CONECT 633 627 634
  1033. CONECT 634 633 635 637
  1034. CONECT 635 634 636 641
  1035. CONECT 636 635
  1036. CONECT 637 634 638
  1037. CONECT 638 637 639
  1038. CONECT 639 638 640
  1039. CONECT 640 639
  1040. CONECT 641 635
  1041. CONECT 821 824
  1042. CONECT 824 821 825
  1043. CONECT 825 824 826 828
  1044. CONECT 826 825 827 832
  1045. CONECT 827 826
  1046. CONECT 828 825 829
  1047. CONECT 829 828 830
  1048. CONECT 830 829 831
  1049. CONECT 831 830
  1050. CONECT 832 826
  1051. CONECT 862 865
  1052. CONECT 865 862 866
  1053. CONECT 866 865 867 869
  1054. CONECT 867 866 868 873
  1055. CONECT 868 867
  1056. CONECT 869 866 870
  1057. CONECT 870 869 871
  1058. CONECT 871 870 872
  1059. CONECT 872 871
  1060. CONECT 873 867
  1061. CONECT 994 1001
  1062. CONECT 1001 994 1002
  1063. CONECT 1002 1001 1003 1005
  1064. CONECT 1003 1002 1004 1009
  1065. CONECT 1004 1003
  1066. CONECT 1005 1002 1006
  1067. CONECT 1006 1005 1007
  1068. CONECT 1007 1006 1008
  1069. CONECT 1008 1007
  1070. CONECT 1009 1003
  1071. CONECT 1060 1065 1066
  1072. CONECT 1065 1060 1067
  1073. CONECT 1066 1060 1068
  1074. CONECT 1067 1065 1069 1073
  1075. CONECT 1068 1066 1070 1074
  1076. CONECT 1069 1067 1071 1081
  1077. CONECT 1070 1068 1072 1081
  1078. CONECT 1071 1069
  1079. CONECT 1072 1070
  1080. CONECT 1073 1067 1075
  1081. CONECT 1074 1068 1076
  1082. CONECT 1075 1073 1077
  1083. CONECT 1076 1074 1078
  1084. CONECT 1077 1075 1079
  1085. CONECT 1078 1076 1080
  1086. CONECT 1079 1077
  1087. CONECT 1080 1078
  1088. CONECT 1081 1069 1070 1082
  1089. CONECT 1082 1081 1083 1085
  1090. CONECT 1083 1082 1084 1089
  1091. CONECT 1084 1083
  1092. CONECT 1085 1082 1086
  1093. CONECT 1086 1085 1087
  1094. CONECT 1087 1086 1088
  1095. CONECT 1088 1087
  1096. CONECT 1089 1083
  1097. CONECT 1273 1276
  1098. CONECT 1276 1273 1277
  1099. CONECT 1277 1276 1278 1280
  1100. CONECT 1278 1277 1279 1284
  1101. CONECT 1279 1278
  1102. CONECT 1280 1277 1281
  1103. CONECT 1281 1280 1282
  1104. CONECT 1282 1281 1283
  1105. CONECT 1283 1282
  1106. CONECT 1284 1278
  1107. CONECT 1314 1317
  1108. CONECT 1317 1314 1318
  1109. CONECT 1318 1317 1319 1321
  1110. CONECT 1319 1318 1320 1325
  1111. CONECT 1320 1319
  1112. CONECT 1321 1318 1322
  1113. CONECT 1322 1321 1323
  1114. CONECT 1323 1322 1324
  1115. CONECT 1324 1323
  1116. CONECT 1325 1319
  1117. CONECT 1446 1453 1454
  1118. CONECT 1453 1446 1455
  1119. CONECT 1454 1446 1456
  1120. CONECT 1455 1453 1457 1461
  1121. CONECT 1456 1454 1458 1462
  1122. CONECT 1457 1455 1459 1469
  1123. CONECT 1458 1456 1460 1469
  1124. CONECT 1459 1457
  1125. CONECT 1460 1458
  1126. CONECT 1461 1455 1463
  1127. CONECT 1462 1456 1464
  1128. CONECT 1463 1461 1465
  1129. CONECT 1464 1462 1466
  1130. CONECT 1465 1463 1467
  1131. CONECT 1466 1464 1468
  1132. CONECT 1467 1465
  1133. CONECT 1468 1466
  1134. CONECT 1469 1457 1458
  1135. CONECT 1520 1525
  1136. CONECT 1525 1520 1526
  1137. CONECT 1526 1525 1527 1529
  1138. CONECT 1527 1526 1528 1533
  1139. CONECT 1528 1527
  1140. CONECT 1529 1526 1530
  1141. CONECT 1530 1529 1531
  1142. CONECT 1531 1530 1532
  1143. CONECT 1532 1531
  1144. CONECT 1533 1527 1534
  1145. CONECT 1534 1533 1535 1537
  1146. CONECT 1535 1534 1536 1541
  1147. CONECT 1536 1535
  1148. CONECT 1537 1534 1538
  1149. CONECT 1538 1537 1539
  1150. CONECT 1539 1538 1540
  1151. CONECT 1540 1539
  1152. CONECT 1541 1535
  1153. CONECT 1721 1724
  1154. CONECT 1724 1721 1725
  1155. CONECT 1725 1724 1726 1728
  1156. CONECT 1726 1725 1727 1732
  1157. CONECT 1727 1726
  1158. CONECT 1728 1725 1729
  1159. CONECT 1729 1728 1730
  1160. CONECT 1730 1729 1731
  1161. CONECT 1731 1730
  1162. CONECT 1732 1726
  1163. MASTER 334 0 19 10 0 0 0 6 1958 4 206 20
  1164. END
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