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PDBsum entry 1zkf

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Top Page protein ligands Protein-protein interface(s) links
Isomerase/isomerase substrate PDB id
1zkf
Jmol
Contents
Protein chains
165 a.a.
Ligands
SIN-ALA-GLY-PRO-
PHE-NIT
×2
Waters ×90
HEADER    ISOMERASE/ISOMERASE SUBSTRATE           02-MAY-05   1ZKF
TITLE     CYRSTAL STRUCTURE OF HUMAN CYCLOPHILIN-A IN COMPLEX WITH SUC-AGPF-PNA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: PPIASE, ROTAMASE, CYCLOPHILIN A, CYCLOSPORIN A-BINDING
COMPND   5 PROTEIN;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: SUC-ALA-GLY-PRO-PHE-PNA;
COMPND  10 CHAIN: C, D;
COMPND  11 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: PPIA, CYPA;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE  11 MOL_ID: 2;
SOURCE  12 SYNTHETIC: YES;
SOURCE  13 OTHER_DETAILS: THE PEPTIDE SUBSTRATE WAS PURCHASED FROM BACHEM (KING
SOURCE  14 OF PRUSSIA, PA).
KEYWDS    CYPA, CYCLOPHILIN-A, CYCLOPHILIN, PPIASE, PROLYL-ISOMERASE,
KEYWDS   2 ISOMERASE, ISOMERASE-ISOMERASE SUBSTRATE COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.Z.EISENMESSER,V.THAI,E.POZHARSKI,D.KERN
REVDAT   3   13-JUL-11 1ZKF    1       VERSN
REVDAT   2   24-FEB-09 1ZKF    1       VERSN
REVDAT   1   11-APR-06 1ZKF    0
JRNL        AUTH   E.Z.EISENMESSER,V.THAI,E.POZHARSKI,D.KERN
JRNL        TITL   MECHANISTIC INSIGHTS OF CYCLOPHILIN-A FROM X-RAY
JRNL        TITL 2 CYRSTALLOGRAPHIC AND NUCLEAR MAGNET RESONANCE INVESTIGATIONS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 10.200
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 15797
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.168
REMARK   3   FREE R VALUE                     : 0.210
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 769
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2612
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 90
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) : 0.35200
REMARK   3    B22 (A**2) : -3.95100
REMARK   3    B33 (A**2) : 3.59900
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : LIGAND.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1ZKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-05.
REMARK 100 THE RCSB ID CODE IS RCSB032819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-03
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 8.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15797
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.14400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RMH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 32.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS-HCL, SODIUM
REMARK 280  AZIDE, DIMETHYL SULFOXIDE, GLYCEROL, PH 8.2, VAPOR DIFFUSION,
REMARK 280  TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   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       17.87850
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.36300
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.41000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.36300
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.87850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.41000
REMARK 290   SMTRY3   4  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 APPLY THE FOLLOWING TO CHAINS: A, C
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 APPLY THE FOLLOWING TO CHAINS: B, 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 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     MET B     1
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    PHE A  60      -75.27   -124.13
REMARK 500    ASN A  71       19.81   -145.40
REMARK 500    ALA A 117      166.43    178.53
REMARK 500    LEU B  17      -80.79    -92.70
REMARK 500    PHE B  60      -77.02   -129.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF SUC-ALA-GLY-PRO-PHE-
REMARK 800  PNA
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF SUC-ALA-GLY-PRO-PHE-
REMARK 800  PNA
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RMH   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN IN COMPLEX WITH SUC-
REMARK 900 AAPF-PNA
DBREF  1ZKF A    1   165  UNP    P62937   PPIA_HUMAN       1    165
DBREF  1ZKF B    1   165  UNP    P62937   PPIA_HUMAN       1    165
DBREF  1ZKF C    1     6  PDB    1ZKF     1ZKF             1      6
DBREF  1ZKF D    1     6  PDB    1ZKF     1ZKF             1      6
SEQRES   1 A  165  MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP
SEQRES   2 A  165  GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA
SEQRES   3 A  165  ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES   4 A  165  SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS
SEQRES   5 A  165  PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY
SEQRES   6 A  165  ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES   7 A  165  TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS
SEQRES   8 A  165  HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY
SEQRES   9 A  165  PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA
SEQRES  10 A  165  LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES  11 A  165  LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU
SEQRES  12 A  165  ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE
SEQRES  13 A  165  THR ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES   1 B  165  MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP
SEQRES   2 B  165  GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA
SEQRES   3 B  165  ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES   4 B  165  SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS
SEQRES   5 B  165  PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY
SEQRES   6 B  165  ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES   7 B  165  TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS
SEQRES   8 B  165  HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY
SEQRES   9 B  165  PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA
SEQRES  10 B  165  LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES  11 B  165  LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU
SEQRES  12 B  165  ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE
SEQRES  13 B  165  THR ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES   1 C    6  SIN ALA GLY PRO PHE NIT
SEQRES   1 D    6  SIN ALA GLY PRO PHE NIT
HET    SIN  C   1       7
HET    NIT  C   6      10
HET    SIN  D   1       7
HET    NIT  D   6      10
HETNAM     SIN SUCCINIC ACID
HETNAM     NIT 4-NITROANILINE
HETSYN     NIT PARANITROANILINE
FORMUL   3  SIN    2(C4 H6 O4)
FORMUL   3  NIT    2(C6 H6 N2 O2)
FORMUL   5  HOH   *90(H2 O)
HELIX    1   1 VAL A   29  GLY A   42  1                                  14
HELIX    2   2 THR A  119  ASP A  123  5                                   5
HELIX    3   3 GLY A  135  ARG A  144  1                                  10
HELIX    4   4 VAL B   29  GLY B   42  1                                  14
HELIX    5   5 THR B  119  ASP B  123  5                                   5
HELIX    6   6 GLY B  135  ARG B  144  1                                  10
SHEET    1   A 8 ARG A  55  ILE A  57  0
SHEET    2   A 8 MET A  61  GLY A  64 -1  O  GLN A  63   N  ARG A  55
SHEET    3   A 8 PHE A 112  CYS A 115 -1  O  ILE A 114   N  CYS A  62
SHEET    4   A 8 ILE A  97  MET A 100 -1  N  ILE A  97   O  CYS A 115
SHEET    5   A 8 VAL A 128  GLU A 134 -1  O  GLY A 130   N  LEU A  98
SHEET    6   A 8 GLU A  15  LEU A  24 -1  N  SER A  21   O  LYS A 133
SHEET    7   A 8 THR A   5  VAL A  12 -1  N  ILE A  10   O  LEU A  17
SHEET    8   A 8 ILE A 156  GLN A 163 -1  O  ASP A 160   N  ASP A   9
SHEET    1   B 8 ARG B  55  ILE B  57  0
SHEET    2   B 8 MET B  61  GLY B  64 -1  O  GLN B  63   N  ARG B  55
SHEET    3   B 8 PHE B 112  CYS B 115 -1  O  PHE B 112   N  GLY B  64
SHEET    4   B 8 ILE B  97  MET B 100 -1  N  SER B  99   O  PHE B 113
SHEET    5   B 8 VAL B 128  GLU B 134 -1  O  GLY B 130   N  LEU B  98
SHEET    6   B 8 GLU B  15  LEU B  24 -1  N  SER B  21   O  LYS B 133
SHEET    7   B 8 THR B   5  VAL B  12 -1  N  VAL B   6   O  PHE B  22
SHEET    8   B 8 ILE B 156  GLN B 163 -1  O  ASP B 160   N  ASP B   9
LINK         C4  SIN C   1                 N   ALA C   2     1555   1555  1.32
LINK         C   PHE C   5                 N1  NIT C   6     1555   1555  1.34
LINK         C4  SIN D   1                 N   ALA D   2     1555   1555  1.33
LINK         C   PHE D   5                 N1  NIT D   6     1555   1555  1.34
CISPEP   1 GLY C    3    PRO C    4          0         0.45
CISPEP   2 GLY D    3    PRO D    4          0         0.44
SITE     1 AC1 17 ARG A  55  ILE A  57  PHE A  60  GLN A  63
SITE     2 AC1 17 GLY A  72  ALA A 101  ASN A 102  PHE A 113
SITE     3 AC1 17 TRP A 121  LEU A 122  HIS A 126  HOH A 176
SITE     4 AC1 17 TRP B 121  LYS B 125  HOH C  36  HOH C  85
SITE     5 AC1 17 PHE D   5
SITE     1 AC2 17 TRP A 121  LYS A 125  ARG B  55  PHE B  60
SITE     2 AC2 17 GLN B  63  GLY B  72  THR B  73  ALA B 101
SITE     3 AC2 17 ASN B 102  GLN B 111  PHE B 113  TRP B 121
SITE     4 AC2 17 LEU B 122  HIS B 126  HOH B 190  PHE C   5
SITE     5 AC2 17 HOH D  63
CRYST1   35.757  108.820  118.726  90.00  90.00  90.00 P 21 21 21    8
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      0.027967  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009189  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008423        0.00000
      
PROCHECK
Go to PROCHECK summary
 References