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PDBsum entry 1a85

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Hydrolase/hydrolase inhibitor PDB id
1a85
Jmol
Contents
Protein chain
158 a.a. *
Ligands
0DY
Metals
_CA ×2
_ZN ×2
* Residue conservation analysis
HEADER    HYDROLASE/HYDROLASE INHIBITOR           03-APR-98   1A85
TITLE     MMP8 WITH MALONIC AND ASPARAGINE BASED INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MMP-8;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MATRIX METALLOPROTEINASE-8;
COMPND   5 EC: 3.4.24.34
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    COLLAGENASE, MATRIX METALLOPROTEINASE, MALONIC ACID, MMP8, HYDROLASE-
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.BRANDSTETTER,E.G.V.ROEDERN,F.GRAMS,R.A.ENGH
REVDAT   3   13-JUL-11 1A85    1       VERSN
REVDAT   2   24-FEB-09 1A85    1       VERSN
REVDAT   1   27-APR-99 1A85    0
JRNL        AUTH   H.BRANDSTETTER,R.A.ENGH,E.G.VON ROEDERN,L.MORODER,R.HUBER,
JRNL        AUTH 2 W.BODE,F.GRAMS
JRNL        TITL   STRUCTURE OF MALONIC ACID-BASED INHIBITORS BOUND TO HUMAN
JRNL        TITL 2 NEUTROPHIL COLLAGENASE. A NEW BINDING MODE EXPLAINS
JRNL        TITL 3 APPARENTLY ANOMALOUS DATA.
JRNL        REF    PROTEIN SCI.                  V.   7  1303 1998
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   9655333
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 1247
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 32
REMARK   3   SOLVENT ATOMS            : 0
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  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  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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1A85 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : DEC-95
REMARK 200  TEMPERATURE           (KELVIN) : 283
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       16.57000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.31000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.71500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.31000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.57000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.71500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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     GLY A 242    O
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     MET A  215   CE
REMARK 480     ARG A  222   CD   NE   CZ   NH1  NH2
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   H    GLN A   144     OE1  GLN A   238     3656     1.47
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A 146   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES
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    ARG A 145     -117.88     32.78
REMARK 500    HIS A 147       37.51   -145.38
REMARK 500    ASN A 157     -160.42     63.41
REMARK 500    THR A 185     -160.64   -117.98
REMARK 500    TYR A 241     -129.16   -107.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615   M RES C SSEQI
REMARK 615     0DY A    1
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 996  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 137   O
REMARK 620 2 GLY A 169   O   160.9
REMARK 620 3 GLY A 171   O   106.1  92.9
REMARK 620 4 ASP A 173   OD1  87.4  96.0  81.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 997  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 154   OD1
REMARK 620 2 GLY A 155   O    93.4
REMARK 620 3 ASN A 157   O    94.1  91.7
REMARK 620 4 ASP A 177   OD2  94.1  90.6 171.3
REMARK 620 5 GLU A 180   OE2 171.5  94.7  88.0  83.4
REMARK 620 6 ILE A 159   O    86.2 173.9  94.4  83.4  85.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 998  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 147   NE2
REMARK 620 2 ASP A 149   OD2 106.9
REMARK 620 3 HIS A 162   NE2 116.1 110.7
REMARK 620 4 HIS A 175   ND1 107.8  96.3 116.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 999  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 197   NE2
REMARK 620 2 HIS A 201   NE2 100.2
REMARK 620 3 HIS A 207   NE2 111.8  97.9
REMARK 620 4 0DY A   1   OH   94.0  89.6 151.3
REMARK 620 5 0DY A   1   O1  109.9 146.5  84.8  74.2
REMARK 620 N                    1     2     3     4
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: N~1~-(3-AMINOBENZYL)-N~2~-[(2R)-2-
REMARK 630 (HYDROXYCARBAMOYL)-4-METHYLPENTANOYL]-L-ASPARTAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630   M RES C SSSEQI
REMARK 630     0DY A     1
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP:    HMI ASN DBP
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 996
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0DY A 1
DBREF  1A85 A   85   242  UNP    P22894   MM08_HUMAN     105    262
SEQRES   1 A  158  ASN PRO LYS TRP GLU ARG THR ASN LEU THR TYR ARG ILE
SEQRES   2 A  158  ARG ASN TYR THR PRO GLN LEU SER GLU ALA GLU VAL GLU
SEQRES   3 A  158  ARG ALA ILE LYS ASP ALA PHE GLU LEU TRP SER VAL ALA
SEQRES   4 A  158  SER PRO LEU ILE PHE THR ARG ILE SER GLN GLY GLU ALA
SEQRES   5 A  158  ASP ILE ASN ILE ALA PHE TYR GLN ARG ASP HIS GLY ASP
SEQRES   6 A  158  ASN SER PRO PHE ASP GLY PRO ASN GLY ILE LEU ALA HIS
SEQRES   7 A  158  ALA PHE GLN PRO GLY GLN GLY ILE GLY GLY ASP ALA HIS
SEQRES   8 A  158  PHE ASP ALA GLU GLU THR TRP THR ASN THR SER ALA ASN
SEQRES   9 A  158  TYR ASN LEU PHE LEU VAL ALA ALA HIS GLU PHE GLY HIS
SEQRES  10 A  158  SER LEU GLY LEU ALA HIS SER SER ASP PRO GLY ALA LEU
SEQRES  11 A  158  MET TYR PRO ASN TYR ALA PHE ARG GLU THR SER ASN TYR
SEQRES  12 A  158  SER LEU PRO GLN ASP ASP ILE ASP GLY ILE GLN ALA ILE
SEQRES  13 A  158  TYR GLY
HET     CA  A 996       1
HET     CA  A 997       1
HET     ZN  A 998       1
HET     ZN  A 999       1
HET    0DY  A   1      36
HETNAM      CA CALCIUM ION
HETNAM      ZN ZINC ION
HETNAM     0DY N~1~-(3-AMINOBENZYL)-N~2~-[(2R)-2-(HYDROXYCARBAMOYL)-4-
HETNAM   2 0DY  METHYLPENTANOYL]-L-ASPARTAMIDE
HETSYN     0DY HONH-IBM-ASN-NHBN(M-NH2)
FORMUL   2   CA    2(CA 2+)
FORMUL   4   ZN    2(ZN 2+)
FORMUL   6  0DY    C18 H27 N5 O5
HELIX    1   1 GLU A  106  ALA A  123  1                                  18
HELIX    2   2 LEU A  191  LEU A  203  1                                  13
HELIX    3   3 GLN A  231  GLN A  238  1                                   8
SHEET    1   A 5 ILE A 127  ARG A 130  0
SHEET    2   A 5 ASN A  92  ILE A  97  1  N  LEU A  93   O  ILE A 127
SHEET    3   A 5 ILE A 138  TYR A 143  1  N  ILE A 138   O  ARG A  96
SHEET    4   A 5 ALA A 174  ASP A 177  1  N  ALA A 174   O  ALA A 141
SHEET    5   A 5 ALA A 161  ALA A 163 -1  N  HIS A 162   O  HIS A 175
LINK        CA    CA A 996                 O   ASP A 137     1555   1555  2.09
LINK        CA    CA A 996                 O   GLY A 169     1555   1555  2.35
LINK        CA    CA A 996                 O   GLY A 171     1555   1555  2.22
LINK        CA    CA A 996                 OD1 ASP A 173     1555   1555  2.39
LINK        CA    CA A 997                 OD1 ASP A 154     1555   1555  2.18
LINK        CA    CA A 997                 O   GLY A 155     1555   1555  2.17
LINK        CA    CA A 997                 O   ASN A 157     1555   1555  2.13
LINK        CA    CA A 997                 OD2 ASP A 177     1555   1555  2.40
LINK        CA    CA A 997                 OE2 GLU A 180     1555   1555  2.29
LINK        ZN    ZN A 998                 NE2 HIS A 147     1555   1555  2.03
LINK        ZN    ZN A 998                 OD2 ASP A 149     1555   1555  1.91
LINK        ZN    ZN A 998                 NE2 HIS A 162     1555   1555  2.08
LINK        ZN    ZN A 998                 ND1 HIS A 175     1555   1555  2.03
LINK        ZN    ZN A 999                 NE2 HIS A 197     1555   1555  1.99
LINK        ZN    ZN A 999                 NE2 HIS A 201     1555   1555  2.17
LINK        ZN    ZN A 999                 NE2 HIS A 207     1555   1555  1.99
LINK        CA    CA A 997                 O   ILE A 159     1555   1555  2.48
LINK        ZN    ZN A 999                 OH  0DY A   1     1555   1555  2.16
LINK        ZN    ZN A 999                 O1  0DY A   1     1555   1555  2.35
CISPEP   1 ASN A  188    TYR A  189          0         2.73
SITE     1 AC1  4 ASP A 137  GLY A 169  GLY A 171  ASP A 173
SITE     1 AC2  6 ASP A 154  GLY A 155  ASN A 157  ILE A 159
SITE     2 AC2  6 ASP A 177  GLU A 180
SITE     1 AC3  4 HIS A 147  ASP A 149  HIS A 162  HIS A 175
SITE     1 AC4  4 0DY A   1  HIS A 197  HIS A 201  HIS A 207
SITE     1 AC5 16 THR A 129  GLY A 158  ILE A 159  LEU A 160
SITE     2 AC5 16 ALA A 161  LEU A 193  HIS A 197  GLU A 198
SITE     3 AC5 16 HIS A 201  HIS A 207  LEU A 214  TYR A 216
SITE     4 AC5 16 PRO A 217  ASN A 218  TYR A 219   ZN A 999
CRYST1   33.140   69.430   72.620  90.00  90.00  90.00 P 21 21 21    4
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      0.030175  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014403  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013770        0.00000
      
PROCHECK
Go to PROCHECK summary
 References