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