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PDBsum entry 1zyy

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Oxidoreductase/electron transport PDB id
1zyy
Jmol
Contents
Protein chains
529 a.a.
252 a.a.
100 a.a.
Ligands
HEC
Metals
CU1 ×2
HEADER    OXIDOREDUCTASE/ELECTRON TRANSPORT       13-JUN-05   1ZYY
TITLE     STRUCTURAL MODEL FOR THE ADDUCT BETWEEN CYTOCHROME C AND
TITLE    2 CYTOCHROME C OXIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE I-BETA;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 17-545;
COMPND   5 SYNONYM: CYTOCHROME AA3 SUBUNIT 1-BETA;
COMPND   6 EC: 1.9.3.1;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE II PRECURSOR;
COMPND   9 CHAIN: B;
COMPND  10 FRAGMENT: RESIDUES 30-281;
COMPND  11 SYNONYM: CYTOCHROME AA3 SUBUNIT 2, OXIDASE AA3, SUBUNIT 2;
COMPND  12 EC: 1.9.3.1;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: CYTOCHROME C-552;
COMPND  15 CHAIN: C;
COMPND  16 FRAGMENT: RESIDUES 78-176;
COMPND  17 SYNONYM: CYTOCHROME C552
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE   3 ORGANISM_COMMON: BACTERIA;
SOURCE   4 MOL_ID: 2;
SOURCE   5 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE   6 ORGANISM_COMMON: BACTERIA;
SOURCE   7 MOL_ID: 3;
SOURCE   8 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE   9 ORGANISM_COMMON: BACTERIA
KEYWDS    PROTEIN-PROTEIN COMPLEX
EXPDTA    THEORETICAL MODEL
AUTHOR    I.BERTINI,G.CAVALLARO,A.ROSATO
REVDAT   1   13-DEC-05 1ZYY    0
JRNL        AUTH   I.BERTINI,G.CAVALLARO,A.ROSATO
JRNL        TITL   A STRUCTURAL MODEL FOR THE ADDUCT BETWEEN
JRNL        TITL 2 CYTOCHROME C AND CYTOCHROME C OXIDASE.
JRNL        REF    J.BIOL.INORG.CHEM.            V.  10   613 2005
JRNL        REFN   ASTM JJBCFA  GW ISSN 0949-8257
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : HADDOCK 1.3
REMARK   3   AUTHORS     : BONVIN
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: THIS MODEL WAS PRODUCED BY HADDOCK
REMARK   3  1.3 STARTING FROM PDB STRUCTURES ID 1AR1 AND 1I6D. IT INCLUDES
REMARK   3  4 CLUSTERS COMPOSED OF 5 STRUCTURES EACH. MODELS 1-5 BELONG TO
REMARK   3  CLUSTER 1, MODELS 6-10 BELONG TO CLUSTER 2, MODELS 11-15
REMARK   3  BELONG TO CLUSTER 3, AND MODELS 16-20 BELONG TO CLUSTER 4.
REMARK   4
REMARK   4 1ZYY COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-2005.
REMARK 100 THE RCSB ID CODE IS RCSB033284.
REMARK 220
REMARK 220 EXPERIMENTAL DETAILS
REMARK 220  EXPERIMENT TYPE                : THEORETICAL MODELLING
REMARK 220
REMARK 220 REMARK: NULL
REMARK 225
REMARK 225 THEORETICAL MODEL
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 225 RECORDS ARE MEANINGLESS.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI
REMARK 500   O    GLU B   218    CU    CU1 B   255              1.68
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500  2 PHE C  44   CE1   PHE C  44   CZ     2.907
REMARK 500  2 PHE C  44   CZ    PHE C  44   CE2    1.450
REMARK 500  9 SER B  24   CB    SER B  24   OG    -0.174
REMARK 500  9 PHE C  44   CE1   PHE C  44   CZ     1.921
REMARK 500  9 PHE C  44   CZ    PHE C  44   CE2    0.179
REMARK 500 13 PHE C  44   CE1   PHE C  44   CZ     1.599
REMARK 500 13 PHE C  44   CZ    PHE C  44   CE2    0.721
REMARK 500 14 SER B  24   CB    SER B  24   OG     0.448
REMARK 500 14 PHE C  44   CE1   PHE C  44   CZ     1.661
REMARK 500 14 PHE C  44   CZ    PHE C  44   CE2    0.388
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500  2 PHE C  44   CB  -  CG  -  CD2 ANGL. DEV. = 12.1 DEGREES
REMARK 500  2 PHE C  44   CB  -  CG  -  CD1 ANGL. DEV. =-71.9 DEGREES
REMARK 500  2 PHE C  44   CD1 -  CE1 -  CZ  ANGL. DEV. =-58.2 DEGREES
REMARK 500  2 PHE C  44   CE1 -  CZ  -  CE2 ANGL. DEV. =-88.5 DEGREES
REMARK 500  2 PHE C  44   CZ  -  CE2 -  CD2 ANGL. DEV. =-75.5 DEGREES
REMARK 500  7 ASP B   6   CB  -  CG  -  OD1 ANGL. DEV. =-59.2 DEGREES
REMARK 500  9 ASP B   6   CB  -  CG  -  OD1 ANGL. DEV. =-29.7 DEGREES
REMARK 500  9 ASP B   6   CB  -  CG  -  OD2 ANGL. DEV. =-60.9 DEGREES
REMARK 500  9 SER B  24   CA  -  CB  -  OG  ANGL. DEV. =-71.5 DEGREES
REMARK 500  9 ASP C  24   CB  -  CG  -  OD1 ANGL. DEV. =-13.2 DEGREES
REMARK 500  9 ASP C  24   CB  -  CG  -  OD2 ANGL. DEV. = 14.0 DEGREES
REMARK 500  9 PHE C  44   CB  -  CG  -  CD2 ANGL. DEV. = 27.0 DEGREES
REMARK 500  9 PHE C  44   CB  -  CG  -  CD1 ANGL. DEV. =-45.2 DEGREES
REMARK 500  9 PHE C  44   CD1 -  CE1 -  CZ  ANGL. DEV. =-38.0 DEGREES
REMARK 500  9 PHE C  44   CE1 -  CZ  -  CE2 ANGL. DEV. =-77.8 DEGREES
REMARK 500  9 PHE C  44   CZ  -  CE2 -  CD2 ANGL. DEV. =-46.8 DEGREES
REMARK 500 13 PHE C  44   CB  -  CG  -  CD2 ANGL. DEV. =  5.3 DEGREES
REMARK 500 13 PHE C  44   CB  -  CG  -  CD1 ANGL. DEV. =-30.0 DEGREES
REMARK 500 13 PHE C  44   CD1 -  CE1 -  CZ  ANGL. DEV. =-38.6 DEGREES
REMARK 500 13 PHE C  44   CE1 -  CZ  -  CE2 ANGL. DEV. =-67.2 DEGREES
REMARK 500 13 PHE C  44   CZ  -  CE2 -  CD2 ANGL. DEV. =-42.3 DEGREES
REMARK 500 14 ASP B   6   CB  -  CG  -  OD1 ANGL. DEV. =-62.4 DEGREES
REMARK 500 14 ASP B   6   CB  -  CG  -  OD2 ANGL. DEV. =-37.1 DEGREES
REMARK 500 14 SER B  24   CA  -  CB  -  OG  ANGL. DEV. = 15.2 DEGREES
REMARK 500 14 ASP C  24   CB  -  CG  -  OD1 ANGL. DEV. =-30.3 DEGREES
REMARK 500 14 ASP C  24   CB  -  CG  -  OD2 ANGL. DEV. =-83.0 DEGREES
REMARK 500 14 PHE C  44   CB  -  CG  -  CD2 ANGL. DEV. = 14.8 DEGREES
REMARK 500 14 PHE C  44   CB  -  CG  -  CD1 ANGL. DEV. =-35.1 DEGREES
REMARK 500 14 PHE C  44   CD1 -  CE1 -  CZ  ANGL. DEV. =-36.4 DEGREES
REMARK 500 14 PHE C  44   CE1 -  CZ  -  CE2 ANGL. DEV. =-68.4 DEGREES
REMARK 500 14 PHE C  44   CZ  -  CE2 -  CD2 ANGL. DEV. =-40.9 DEGREES
REMARK 500 18 ASP B   6   CB  -  CG  -  OD1 ANGL. DEV. =-36.1 DEGREES
REMARK 500 18 ASP B   6   CB  -  CG  -  OD2 ANGL. DEV. =-78.1 DEGREES
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  M RES CSSEQI        PSI       PHI
REMARK 500  1 TRP B 121      -31.83     77.32
REMARK 500  2 GLU B 218      148.14     71.13
REMARK 500  3 GLU B 218      144.76     67.31
REMARK 500  6 GLU B 218      143.48     68.99
REMARK 500  8 TRP B 121      -48.74     72.05
REMARK 500 11 GLU B 218      140.25     68.34
REMARK 500 12 GLU B 218      137.07     70.68
REMARK 500 13 TRP B 121      -34.82     71.27
REMARK 500 13 GLU B 218      142.50     71.57
REMARK 500 14 LEU C  20      -62.77     71.98
REMARK 500 15 GLU B 218      136.56     69.82
REMARK 500 20 TRP B 121      -68.63     76.07
DBREF  1ZYY A   17   545  UNP    P98002   COX1B_PARDE     17    545
DBREF  1ZYY B    1   252  UNP    P08306   COX2_PARDE      30    281
DBREF  1ZYY C    2   100  UNP    P54820   CY552_PARDE     78    176
SEQADV 1ZYY MET C    1  UNP  P54820              CLONING ARTIFACT
SEQRES   1 A  529  GLY PHE PHE THR ARG TRP PHE MET SER THR ASN HIS LYS
SEQRES   2 A  529  ASP ILE GLY ILE LEU TYR LEU PHE THR ALA GLY ILE VAL
SEQRES   3 A  529  GLY LEU ILE SER VAL CYS PHE THR VAL TYR MET ARG MET
SEQRES   4 A  529  GLU LEU GLN HIS PRO GLY VAL GLN TYR MET CYS LEU GLU
SEQRES   5 A  529  GLY ALA ARG LEU ILE ALA ASP ALA SER ALA GLU CYS THR
SEQRES   6 A  529  PRO ASN GLY HIS LEU TRP ASN VAL MET ILE THR TYR HIS
SEQRES   7 A  529  GLY VAL LEU MET MET PHE PHE VAL VAL ILE PRO ALA LEU
SEQRES   8 A  529  PHE GLY GLY PHE GLY ASN TYR PHE MET PRO LEU HIS ILE
SEQRES   9 A  529  GLY ALA PRO ASP MET ALA PHE PRO ARG LEU ASN ASN LEU
SEQRES  10 A  529  SER TYR TRP MET TYR VAL CYS GLY VAL ALA LEU GLY VAL
SEQRES  11 A  529  ALA SER LEU LEU ALA PRO GLY GLY ASN ASP GLN MET GLY
SEQRES  12 A  529  SER GLY VAL GLY TRP VAL LEU TYR PRO PRO LEU SER THR
SEQRES  13 A  529  THR GLU ALA GLY TYR SER MET ASP LEU ALA ILE PHE ALA
SEQRES  14 A  529  VAL HIS VAL SER GLY ALA SER SER ILE LEU GLY ALA ILE
SEQRES  15 A  529  ASN ILE ILE THR THR PHE LEU ASN MET ARG ALA PRO GLY
SEQRES  16 A  529  MET THR LEU PHE LYS VAL PRO LEU PHE ALA TRP SER VAL
SEQRES  17 A  529  PHE ILE THR ALA TRP LEU ILE LEU LEU SER LEU PRO VAL
SEQRES  18 A  529  LEU ALA GLY ALA ILE THR MET LEU LEU MET ASP ARG ASN
SEQRES  19 A  529  PHE GLY THR GLN PHE PHE ASP PRO ALA GLY GLY GLY ASP
SEQRES  20 A  529  PRO VAL LEU TYR GLN HIS ILE LEU TRP PHE PHE GLY HIS
SEQRES  21 A  529  PRO GLU VAL TYR ILE ILE ILE LEU PRO GLY PHE GLY ILE
SEQRES  22 A  529  ILE SER HIS VAL ILE SER THR PHE ALA LYS LYS PRO ILE
SEQRES  23 A  529  PHE GLY TYR LEU PRO MET VAL LEU ALA MET ALA ALA ILE
SEQRES  24 A  529  GLY ILE LEU GLY PHE VAL VAL TRP ALA HIS HIS MET TYR
SEQRES  25 A  529  THR ALA GLY MET SER LEU THR GLN GLN ALA TYR PHE MET
SEQRES  26 A  529  LEU ALA THR MET THR ILE ALA VAL PRO THR GLY ILE LYS
SEQRES  27 A  529  VAL PHE SER TRP ILE ALA THR MET TRP GLY GLY SER ILE
SEQRES  28 A  529  GLU PHE LYS THR PRO MET LEU TRP ALA PHE GLY PHE LEU
SEQRES  29 A  529  PHE LEU PHE THR VAL GLY GLY VAL THR GLY VAL VAL LEU
SEQRES  30 A  529  SER GLN ALA PRO LEU ASP ARG VAL TYR HIS ASP THR TYR
SEQRES  31 A  529  TYR VAL VAL ALA HIS PHE HIS TYR VAL MET SER LEU GLY
SEQRES  32 A  529  ALA VAL PHE GLY ILE PHE ALA GLY VAL TYR TYR TRP ILE
SEQRES  33 A  529  GLY LYS MET SER GLY ARG GLN TYR PRO GLU TRP ALA GLY
SEQRES  34 A  529  GLN LEU HIS PHE TRP MET MET PHE ILE GLY SER ASN LEU
SEQRES  35 A  529  ILE PHE PHE PRO GLN HIS PHE LEU GLY ARG GLN GLY MET
SEQRES  36 A  529  PRO ARG ARG TYR ILE ASP TYR PRO VAL GLU PHE ALA TYR
SEQRES  37 A  529  TRP ASN ASN ILE SER SER ILE GLY ALA TYR ILE SER PHE
SEQRES  38 A  529  ALA SER PHE LEU PHE PHE ILE GLY ILE VAL PHE TYR THR
SEQRES  39 A  529  LEU PHE ALA GLY LYS ARG VAL ASN VAL PRO ASN TYR TRP
SEQRES  40 A  529  ASN GLU HIS ALA ASP THR LEU GLU TRP THR LEU PRO SER
SEQRES  41 A  529  PRO PRO PRO GLU HIS THR PHE GLU THR
SEQRES   1 B  252  GLN ASP VAL LEU GLY ASP LEU PRO VAL ILE GLY LYS PRO
SEQRES   2 B  252  VAL ASN GLY GLY MET ASN PHE GLN PRO ALA SER SER PRO
SEQRES   3 B  252  LEU ALA HIS ASP GLN GLN TRP LEU ASP HIS PHE VAL LEU
SEQRES   4 B  252  TYR ILE ILE THR ALA VAL THR ILE PHE VAL CYS LEU LEU
SEQRES   5 B  252  LEU LEU ILE CYS ILE VAL ARG PHE ASN ARG ARG ALA ASN
SEQRES   6 B  252  PRO VAL PRO ALA ARG PHE THR HIS ASN THR PRO ILE GLU
SEQRES   7 B  252  VAL ILE TRP THR LEU VAL PRO VAL LEU ILE LEU VAL ALA
SEQRES   8 B  252  ILE GLY ALA PHE SER LEU PRO ILE LEU PHE ARG SER GLN
SEQRES   9 B  252  GLU MET PRO ASN ASP PRO ASP LEU VAL ILE LYS ALA ILE
SEQRES  10 B  252  GLY HIS GLN TRP TYR TRP SER TYR GLU TYR PRO ASN ASP
SEQRES  11 B  252  GLY VAL ALA PHE ASP ALA LEU MET LEU GLU LYS GLU ALA
SEQRES  12 B  252  LEU ALA ASP ALA GLY TYR SER GLU ASP GLU TYR LEU LEU
SEQRES  13 B  252  ALA THR ASP ASN PRO VAL VAL VAL PRO VAL GLY LYS LYS
SEQRES  14 B  252  VAL LEU VAL GLN VAL THR ALA THR ASP VAL ILE HIS ALA
SEQRES  15 B  252  TRP THR ILE PRO ALA PHE ALA VAL LYS GLN ASP ALA VAL
SEQRES  16 B  252  PRO GLY ARG ILE ALA GLN LEU TRP PHE SER VAL ASP GLN
SEQRES  17 B  252  GLU GLY VAL TYR PHE GLY GLN CYS SER GLU LEU CYS GLY
SEQRES  18 B  252  ILE ASN HIS ALA TYR MET PRO ILE VAL VAL LYS ALA VAL
SEQRES  19 B  252  SER GLN GLU LYS TYR GLU ALA TRP LEU ALA GLY ALA LYS
SEQRES  20 B  252  GLU GLU PHE ALA ALA
SEQRES   1 C  100  MET ALA ASP PRO ALA ALA GLY GLU LYS VAL PHE GLY LYS
SEQRES   2 C  100  CYS LYS ALA CYS HIS LYS LEU ASP GLY ASN ASP GLY VAL
SEQRES   3 C  100  GLY PRO HIS LEU ASN GLY VAL VAL GLY ARG THR VAL ALA
SEQRES   4 C  100  GLY VAL ASP GLY PHE ASN TYR SER ASP PRO MET LYS ALA
SEQRES   5 C  100  HIS GLY GLY ASP TRP THR PRO GLU ALA LEU GLN GLU PHE
SEQRES   6 C  100  LEU THR ASN PRO LYS ALA VAL VAL LYS GLY THR LYS MET
SEQRES   7 C  100  ALA PHE ALA GLY LEU PRO LYS ILE GLU ASP ARG ALA ASN
SEQRES   8 C  100  LEU ILE ALA TYR LEU GLU GLY GLN GLN
HET    CU1  B 255       1
HET    CU1  B 256       1
HET    HEC  C 101      75
HETNAM     CU1 COPPER (I) ION
HETNAM     HEC HEME C
FORMUL   4  CU1    2(CU 1+)
FORMUL   6  HEC    C34 H34 FE N4 O4
HELIX    1   1 PHE A   18  PHE A   23  1                                   6
HELIX    2   2 ASN A   27  LEU A   57  1                                  31
HELIX    3   3 ASN A   83  PHE A  101  1                                  19
HELIX    4   4 VAL A  102  PHE A  108  1                                   7
HELIX    5   5 GLY A  110  GLY A  121  1                                  12
HELIX    6   6 PHE A  127  LEU A  150  1                                  24
HELIX    7   7 PRO A  169  GLU A  174  1                                   6
HELIX    8   8 TYR A  177  LEU A  205  1                                  29
HELIX    9   9 THR A  213  VAL A  217  5                                   5
HELIX   10  10 PRO A  218  ARG A  249  1                                  32
HELIX   11  11 ASP A  263  ALA A  298  1                                  36
HELIX   12  12 GLY A  304  LEU A  318  1                                  15
HELIX   13  13 GLY A  319  VAL A  321  5                                   3
HELIX   14  14 SER A  333  THR A  346  1                                  14
HELIX   15  15 ILE A  347  TRP A  363  1                                  17
HELIX   16  16 LYS A  370  GLN A  395  1                                  26
HELIX   17  17 GLN A  395  HIS A  403  1                                   9
HELIX   18  18 THR A  405  MET A  416  1                                  12
HELIX   19  19 GLY A  419  SER A  436  1                                  18
HELIX   20  20 PRO A  441  GLY A  470  1                                  30
HELIX   21  21 PRO A  479  GLU A  481  5                                   3
HELIX   22  22 PHE A  482  GLY A  514  1                                  33
HELIX   23  23 THR A  529  THR A  533  5                                   5
HELIX   24  24 SER B   25  ARG B   59  1                                  35
HELIX   25  25 ASN B   74  GLU B  105  1                                  32
HELIX   26  26 ALA B  143  GLY B  148  1                                   6
HELIX   27  27 SER B  150  ALA B  157  5                                   8
HELIX   28  28 SER B  235  PHE B  250  1                                  16
HELIX   29  29 ALA C    5  PHE C   11  1                                   7
HELIX   30  30 GLY C   12  CYS C   14  5                                   3
HELIX   31  31 SER C   47  ALA C   52  1                                   6
HELIX   32  32 THR C   58  LEU C   66  1                                   9
HELIX   33  33 ASN C   68  VAL C   73  1                                   6
HELIX   34  34 LYS C   85  GLY C   98  1                                  14
SHEET    1   A 2 PRO A 152  GLY A 153  0
SHEET    2   A 2 GLN A 157  MET A 158 -1  O  GLN A 157   N  GLY A 153
SHEET    1   B 2 ARG A 438  GLN A 439  0
SHEET    2   B 2 LYS A 515  ARG A 516 -1  O  LYS A 515   N  GLN A 439
SHEET    1   C 4 VAL B   9  GLY B  11  0
SHEET    2   C 4 GLY B 210  GLY B 214  1  O  VAL B 211   N  GLY B  11
SHEET    3   C 4 ILE B 229  VAL B 234 -1  O  ALA B 233   N  GLY B 210
SHEET    4   C 4 VAL B 162  PRO B 165  1  N  VAL B 162   O  LYS B 232
SHEET    1   D 5 ALA B 133  ALA B 136  0
SHEET    2   D 5 TRP B 123  GLU B 126 -1  N  TYR B 125   O  PHE B 134
SHEET    3   D 5 LEU B 112  GLY B 118 -1  N  LYS B 115   O  GLU B 126
SHEET    4   D 5 LYS B 169  ALA B 176  1  O  LEU B 171   N  LEU B 112
SHEET    5   D 5 ALA B 200  SER B 205 -1  O  LEU B 202   N  VAL B 172
SHEET    1   E 2 HIS B 181  ILE B 185  0
SHEET    2   E 2 VAL B 190  ALA B 194 -1  O  GLN B 192   N  TRP B 183
SSBOND   1 CYS A   66    CYS A   80
SSBOND   2 CYS B  216    CYS B  220
LINK        CU   CU1 B 255                 SG  CYS B 216
LINK        CU   CU1 B 255                 SG  CYS B 220
LINK        CU   CU1 B 255                 ND1 HIS B 224
LINK        CU   CU1 B 256                 ND1 HIS B 181
LINK        CU   CU1 B 256                 SG  CYS B 216
LINK        CU   CU1 B 256                 SG  CYS B 220
LINK         NE2 HIS C  18                FE   HEC C 101
LINK         SG  CYS C  14                 CAB HEC C 101
LINK         SG  CYS C  17                 CAC HEC C 101
LINK         SD  MET C  78                FE   HEC C 101
CISPEP   1 PRO A  168    PRO A  169          1         0.00
CISPEP   2 SER A  536    PRO A  537          1        -0.21
CISPEP   3 PRO A  168    PRO A  169          2         0.05
CISPEP   4 SER A  536    PRO A  537          2        -0.27
CISPEP   5 PRO A  168    PRO A  169          3         0.33
CISPEP   6 SER A  536    PRO A  537          3        -0.38
CISPEP   7 PRO A  168    PRO A  169          4         0.32
CISPEP   8 SER A  536    PRO A  537          4        -0.26
CISPEP   9 PRO A  168    PRO A  169          5         0.59
CISPEP  10 SER A  536    PRO A  537          5        -0.71
CISPEP  11 PRO A  168    PRO A  169          6         0.13
CISPEP  12 SER A  536    PRO A  537          6        -0.17
CISPEP  13 PRO A  168    PRO A  169          7         0.11
CISPEP  14 SER A  536    PRO A  537          7        -0.59
CISPEP  15 PRO A  168    PRO A  169          8         0.21
CISPEP  16 SER A  536    PRO A  537          8        -0.41
CISPEP  17 PRO A  168    PRO A  169          9         0.50
CISPEP  18 SER A  536    PRO A  537          9        -0.31
CISPEP  19 PRO A  168    PRO A  169         10        -0.36
CISPEP  20 SER A  536    PRO A  537         10        -0.54
CISPEP  21 PRO A  168    PRO A  169         11        -0.06
CISPEP  22 SER A  536    PRO A  537         11        -0.45
CISPEP  23 PRO A  168    PRO A  169         12        -0.02
CISPEP  24 SER A  536    PRO A  537         12        -0.49
CISPEP  25 PRO A  168    PRO A  169         13         0.12
CISPEP  26 SER A  536    PRO A  537         13        -0.79
CISPEP  27 PRO A  168    PRO A  169         14         0.09
CISPEP  28 SER A  536    PRO A  537         14        -0.85
CISPEP  29 PRO A  168    PRO A  169         15         0.00
CISPEP  30 SER A  536    PRO A  537         15        -0.62
CISPEP  31 PRO A  168    PRO A  169         16         0.07
CISPEP  32 SER A  536    PRO A  537         16        -0.97
CISPEP  33 PRO A  168    PRO A  169         17         0.30
CISPEP  34 SER A  536    PRO A  537         17        -0.60
CISPEP  35 PRO A  168    PRO A  169         18         0.07
CISPEP  36 SER A  536    PRO A  537         18        -0.50
CISPEP  37 PRO A  168    PRO A  169         19        -0.02
CISPEP  38 SER A  536    PRO A  537         19        -0.64
CISPEP  39 PRO A  168    PRO A  169         20        -0.13
CISPEP  40 SER A  536    PRO A  537         20        -1.17
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
Go to PROCHECK summary
 References