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PDBsum entry 1cpa

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Hydrolase (c-terminal peptidase) PDB id
1cpa
Jmol
Contents
Protein chain
307 a.a.
Ligands
GLY-TYR
Metals
_ZN
HEADER    HYDROLASE (C-TERMINAL PEPTIDASE)        01-FEB-73   1CPA
OBSLTE     29-JUL-82 1CPA      3CPA
TITLE     CARBOXYPEPTIDASE A,A PROTEIN AND AN ENZYME
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE:;
COMPND   3 CHAIN: NULL;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE:;
COMPND   7 CHAIN: S;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 MOL_ID: 2
KEYWDS    HYDROLASE (C-TERMINAL PEPTIDASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    F.A.QUIOCHO,W.N.LIPSCOMB
REVDAT   1             1CPA    0
JRNL        AUTH   F.A.QUIOCHO,W.N.LIPSCOMB
JRNL        TITL   CARBOXYPEPTIDASE A,A PROTEIN AND AN ENZYME
JRNL        REF    ADV.PROTEIN CHEM.             V.  25     1 1971
JRNL        REFN   ASTM APCHA2  US ISSN 0065-3233
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   D.C.REES,W.N.LIPSCOMB
REMARK   1  TITL   BINDING OF LIGANDS TO THE ACTIVE SITE OF
REMARK   1  TITL 2 CARBOXYPEPTIDASE A
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  78  5455 1981
REMARK   1  REFN   ASTM PNASA6  US ISSN 0027-8424
REMARK   1 REFERENCE 2
REMARK   1  AUTH   D.C.REES,M.LEWIS,R.B.HONZATKO,W.N.LIPSCOMB,
REMARK   1  AUTH 2 K.D.HARDMAN
REMARK   1  TITL   ZINC ENVIRONMENT AND CIS PEPTIDE BONDS IN
REMARK   1  TITL 2 CARBOXYPEPTIDASE A AT 1.75-ANGSTROMS RESOLUTION
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  78  3408 1981
REMARK   1  REFN   ASTM PNASA6  US ISSN 0027-8424
REMARK   1 REFERENCE 3
REMARK   1  AUTH   W.N.LIPSCOMB
REMARK   1  TITL   CARBOXYPEPTIDASE A MECHANISMS
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  77  3875 1980
REMARK   1  REFN   ASTM PNASA6  US ISSN 0027-8424
REMARK   1 REFERENCE 4
REMARK   1  AUTH   W.N.LIPSCOMB,J.A.HARTSUCK,G.N.REEKEJUNIOR,
REMARK   1  AUTH 2 F.A.QUIOCHO,P.H.BETHGE,M.L.LUDWIG,T.A.STEITZ,
REMARK   1  AUTH 3 H.MUIRHEAD,J.C.COPPOLA
REMARK   1  TITL   THE STRUCTURE OF CARBOXYPEPTIDASE A, VII.THE
REMARK   1  TITL 2 2.0-ANGSTROMS RESOLUTION STUDIES OF THE ENZYME AND
REMARK   1  TITL 3 OF ITS COMPLEX WITH GLYCYLTYROSINE,AND MECHANISTIC
REMARK   1  TITL 4 DEDUCTIONS
REMARK   1  REF    BROOKHAVEN SYMPOSIA IN        V.  21    24 1969
REMARK   1  REF  2 BIOLOGY,STRUCTURE,FUNCTION,
REMARK   1  REF  3 AND EVOLUTION IN PROTEINS
REMARK   1  PUBL   NATIONAL TECHNICAL INFORMATION SERVICE,
REMARK   1  PUBL 2 SPRINGFIELD,VA. (BNL 50116(C-53)VOL.1)
REMARK   1  REFN
REMARK   1 REFERENCE 5
REMARK   1  AUTH   W.N.LIPSCOMB
REMARK   1  TITL   STRUCTURE AND MECHANISM IN THE ENZYMATIC ACTIVITY
REMARK   1  TITL 2 OF CARBOXYPEPTIDASE A AND RELATIONS TO CHEMICAL
REMARK   1  TITL 3 SEQUENCE
REMARK   1  REF    ACC.CHEM.RES.                 V.   3    81 1970
REMARK   1  REFN   ASTM ACHRE4  US ISSN 0001-4842
REMARK   1 REFERENCE 6
REMARK   1  EDIT   R.J.FELDMANN
REMARK   1  REF    ATLAS OF MACROMOLECULAR                289 1976
REMARK   1  REF  2 STRUCTURE ON MICROFICHE
REMARK   1  PUBL   TRACOR JITCO,INC.,ROCKVILLE,MD.
REMARK   1  REFN                   ISBN 0-917934-01-6
REMARK   1 REFERENCE 7
REMARK   1  EDIT   M.O.DAYHOFF
REMARK   1  REF    ATLAS OF PROTEIN SEQUENCE     V.   5   126 1972
REMARK   1  REF  2 AND STRUCTURE (DATA SECTION)
REMARK   1  PUBL   NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER
REMARK   1  PUBL 2 SPRING,MD.
REMARK   1  REFN                   ISBN 0-912466-02-2
REMARK   2
REMARK   2 RESOLUTION. NULL ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : NULL
REMARK   3   AUTHORS     : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : NULL
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            : 2452
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
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 1CPA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK   5
REMARK   5 1CPA CORRECTION. INSERT MISSING CONECT RECORD. 03-JAN-77.
REMARK   5 1CPA
REMARK   6
REMARK   6 1CPA CORRECTION. CORRECT ATOM NAMES AND ORDERING FOR ALL
REMARK   6 TRP 1CPA RESIDUES, REVERSING CD1 WITH CD2, CE2 WITH CE3,
REMARK   6 CZ2 WITH 1CPA CZ3. 23-AUG-77. 1CPA
REMARK   7
REMARK   7 1CPA CORRECTION. REFORMAT HEADER INFORMATION TO MEET NEW
REMARK   7 1CPA SPECIFICATIONS. 1CPA ADD FORMUL RECORDS. 1CPA ADD
REMARK   7 SSBOND RECORDS. 1CPA 01-NOV-77. 1CPA
REMARK   8
REMARK   8 1CPA CORRECTION. CORRECT FORMAT OF HET RECORD. 05-FEB-79.
REMARK   8 1CPA
REMARK   9
REMARK   9 1CPA CORRECTION. STANDARDIZE NOMENCLATURE TO FOLLOW IUPAC-
REMARK   9 IUB 1CPA RECOMMENDATIONS. INTERCHANGE CD1 AND CD2 FOR
REMARK   9 LEUCINES 1CPA 15, 24, 25, 32, 36, 50, 66, 100, 107, 125,
REMARK   9 137, 193, 201, 1CPA 202, 203, 219, 230, 233, 271, 280, 281,
REMARK   9 295, 298. 1CPA INTERCHANGE CG1 AND CG2 FOR VALINES 26, 33,
REMARK   9 49, 80, 110, 1CPA 132, 139, 141, 174, 176, 180, 183, 222,
REMARK   9 227, 297, 305. 1CPA 07-APR-80. 1CPA
REMARK  10
REMARK  10 1CPA CORRECTION. INSERT NEW PUBLICATION AS REFERENCE 1 AND
REMARK  10 1CPA RENUMBER ALL OTHERS. 09-SEP-80. 1CPA
REMARK  11
REMARK  11 1CPA CORRECTION. STANDARDIZE FORMAT OF REMARKS 2 AND 3.
REMARK  11 1CPA 31-DEC-80. 1CPA
REMARK  12
REMARK  12 1CPA CORRECTION. CHANGE RESIDUE 72 FROM GLN TO GLU ON 1CPA
REMARK  12 DEPOSITORS INSTRUCTIONS. 20-APR-81. 1CPA
REMARK  13
REMARK  13 1CPA CORRECTION. INSERT NEW PUBLICATION AS REFERENCE 1 AND
REMARK  13 1CPA RENUMBER ALL OTHERS. INSERT REMARKS 14, 15, 16, 17 AND
REMARK  13 1CPA FTNOTES 2, 3. ADD FTNOTE 2 TO RESIDUES 197-198 AND
REMARK  13 1CPA FTNOTE 3 TO RESIDUES 205-206 AND 272-273. 14-SEP-81.
REMARK  13 1CPA
REMARK  14
REMARK  14 1CPA THE COORDINATES GIVEN BELOW ARE FOR THE NATIVE 1CPA
REMARK  14 (UNCOMPLEXED) FORM OF THE ENZYME AND FOR THE INHIBITOR AS
REMARK  14 1CPA FOUND IN THE INHIBITOR-ENZYME COMPLEX. THE COMPLEXED
REMARK  14 FORM 1CPA OF THE ENZYME SHOWS CONFORMATIONAL CHANGES.
REMARK  14 COORDINATES 1CPA FOR THE COMPLEX WILL BE DEPOSITED IN THE
REMARK  14 PROTEIN DATA BANK 1CPA AT A FUTURE DATE. 1CPA
REMARK  15
REMARK  15 1CPA THE PEPTIDE LINKAGE SER 197 - TYR 198 HAS BEEN FOUND
REMARK  15 TO BE 1CPA IN CIS-CONFORMATION AFTER LEAST-SQUARES
REMARK  15 REFINEMENT. THE 1CPA TORSION ANGLE ABOUT THIS BOND HAS BEEN
REMARK  15 SET TO 90 DEGREES 1CPA IN THIS ENTRY. 1CPA
REMARK  16
REMARK  16 1CPA THE PEPTIDE LINKAGES PRO 205 - TYR 206 AND ARG 272 -
REMARK  16 ASP 1CPA 273 HAVE BEEN FOUND TO BE IN CIS-CONFORMATION
REMARK  16 AFTER 1CPA LEAST-SQUARES REFINEMENT. THESE LINKAGES ARE IN
REMARK  16 1CPA TRANS-CONFORMATION IN THIS ENTRY. 1CPA
REMARK  17
REMARK  17 1CPA IN THE REFINED STRUCTURE OF CARBOXYPEPTIDASE A BOTH
REMARK  17 OXYGENS 1CPA OF THE GLU 72 CARBOXYLATE GROUP ARE
REMARK  17 COORDINATED TO THE ZN. 1CPA
REMARK  18
REMARK  18 1CPA CORRECTION. INSERT NEW PUBLICATION AS REFERENCE 1 AND
REMARK  18 1CPA RENUMBER ALL OTHERS. ASSIGN NEW CODEN TO REFERENCE 4.
REMARK  18 1CPA CORRECT JOURNAL NAME FOR JRNL REFERENCE. 03-DEC-81.
REMARK  18 1CPA
REMARK  19
REMARK  19 1CPA CORRECTION. CORRECT SCALE TRANSFORMATION. 06-JAN-82.
REMARK  19 1CPA
REMARK  20
REMARK  20 1CPA CORRECTION. FIX FORMAT OF DATE IN REMARK 5. 15-JAN-82.
REMARK  20 1CPA
REMARK  21
REMARK  21 1CPA CORRECTION. THIS ENTRY IS OBSOLETE. 14-FEB-84. 1CPA
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
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) : NULL
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   (%): 40.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,1/2+Y,-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       29.94500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: S
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     ALA     1    N
REMARK 470     ASN     5    OD1   ND2
REMARK 470     ASN     8    OD1   ND2
REMARK 470     GLN    28    OE1   NE2
REMARK 470     GLN    37    OE1   NE2
REMARK 470     ASN    58    OD1   ND2
REMARK 470     GLN    76    OE1   NE2
REMARK 470     ASN    89    OD1   ND2
REMARK 470     GLN    92    OE1   NE2
REMARK 470     ASN    93    OD1   ND2
REMARK 470     ASN   112    OD1   ND2
REMARK 470     ASN   114    OD1   ND2
REMARK 470     ASN   123    OD1   ND2
REMARK 470     ASN   144    OD1   ND2
REMARK 470     ASN   146    OD1   ND2
REMARK 470     ASN   171    OD1   ND2
REMARK 470     ASN   185    OD1   ND2
REMARK 470     ASN   188    OD1   ND2
REMARK 470     GLN   200    OE1   NE2
REMARK 470     GLN   211    OE1   NE2
REMARK 470     ASN   220    OD1   ND2
REMARK 470     GLN   221    OE1   NE2
REMARK 470     GLN   249    OE1   NE2
REMARK 470     ASN   260    OD1   ND2
REMARK 470     GLN   261    OE1   NE2
REMARK 470     GLN   285    OE1   NE2
REMARK 470     GLN   291    OE1   NE2
REMARK 470     MET   301    CE
REMARK 470     ASN   306    OD1   ND2
REMARK 470     ASN   307    OD1   ND2
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
REMARK 500   OE2  GLU      72     O    SER     197              1.70
REMARK 500   OH   TYR      12     O    LEU     281              1.71
REMARK 500   OG1  THR       4    AE1   GLN      28              1.85
REMARK 500   NH2  ARG     272     OE2  GLU     292              1.85
REMARK 500   N    PHE     192     O    TYR     265              1.95
REMARK 500   O    ASN     171     NZ   LYS     177              1.97
REMARK 500   O    GLY     207     N    ALA     250              2.00
REMARK 500   C    GLY      55     NH1  ARG      59              2.03
REMARK 500   O    LYS      84     OG1  THR      87              2.04
REMARK 500   OH   TYR     234    AE1   GLN     291              2.06
REMARK 500   CG   PRO     214     OH   TYR     259              2.08
REMARK 500   OG   SER      95     OE2  GLU     302              2.10
REMARK 500   O    SER     242     CB   THR     245              2.10
REMARK 500   O    GLY     207     O    ALA     250              2.12
REMARK 500   OG1  THR      14     CG   GLU      17              2.16
REMARK 500   O    PHE     116     OG1  THR     119              2.16
REMARK 500   O    THR       4     OH   TYR       9              2.18
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    ILE    62   N     ILE    62   CA    -0.171
REMARK 500    SER   197   C     TYR   198   N     -0.189
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    ILE    62   C   -  N   -  CA  ANGL. DEV. = 20.5 DEGREES
REMARK 500    TYR   198   C   -  N   -  CA  ANGL. DEV. = 26.4 DEGREES
REMARK 500    TYR   206   CB  -  CA  -  C   ANGL. DEV. = 19.3 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    THR   133      150.03     83.23
REMARK 500    SER   134     -167.13    115.44
REMARK 500    SER   199       -4.72    140.49
REMARK 500    ASP   273      127.17     80.18
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 SER    197    TYR    198                   88.31
SEQRES   1    307  ALA ARG SER THR ASN THR PHE ASN TYR ALA THR TYR HIS
SEQRES   2    307  THR LEU ASP GLU ILE TYR ASP PHE MET ASP LEU LEU VAL
SEQRES   3    307  ALA GLN HIS PRO GLU LEU VAL SER LYS LEU GLN ILE GLY
SEQRES   4    307  ARG SER TYR GLU GLY ARG PRO ILE TYR VAL LEU LYS PHE
SEQRES   5    307  SER THR GLY GLY SER ASN ARG PRO ALA ILE TRP ILE ASP
SEQRES   6    307  LEU GLY ILE HIS SER ARG GLU TRP ILE THR GLN ALA THR
SEQRES   7    307  GLY VAL TRP PHE ALA LYS LYS PHE THR GLU ASN TYR GLY
SEQRES   8    307  GLN ASN PRO SER PHE THR ALA ILE LEU ASP SER MET ASP
SEQRES   9    307  ILE PHE LEU GLU ILE VAL THR ASN PRO ASN GLY PHE ALA
SEQRES  10    307  PHE THR HIS SER GLU ASN ARG LEU TRP ARG LYS THR ARG
SEQRES  11    307  SER VAL THR SER SER SER LEU CYS VAL GLY VAL ASP ALA
SEQRES  12    307  ASN ARG ASN TRP ASP ALA GLY PHE GLY LYS ALA GLY ALA
SEQRES  13    307  SER SER SER PRO CYS SER GLU THR TYR HIS GLY LYS TYR
SEQRES  14    307  ALA ASN SER GLU VAL GLU VAL LYS SER ILE VAL ASP PHE
SEQRES  15    307  VAL LYS ASN HIS GLY ASN PHE LYS ALA PHE LEU SER ILE
SEQRES  16    307  HIS SER TYR SER GLN LEU LEU LEU TYR PRO TYR GLY TYR
SEQRES  17    307  THR THR GLN SER ILE PRO ASP LYS THR GLU LEU ASN GLN
SEQRES  18    307  VAL ALA LYS SER ALA VAL ALA ALA LEU LYS SER LEU TYR
SEQRES  19    307  GLY THR SER TYR LYS TYR GLY SER ILE ILE THR THR ILE
SEQRES  20    307  TYR GLN ALA SER GLY GLY SER ILE ASP TRP SER TYR ASN
SEQRES  21    307  GLN GLY ILE LYS TYR SER PHE THR PHE GLU LEU ARG ASP
SEQRES  22    307  THR GLY ARG TYR GLY PHE LEU LEU PRO ALA SER GLN ILE
SEQRES  23    307  ILE PRO THR ALA GLN GLU THR TRP LEU GLY VAL LEU THR
SEQRES  24    307  ILE MET GLU HIS THR VAL ASN ASN
FTNOTE   1 GLYCYL-TYROSINE PSEUDO-SUBSTRATE
FTNOTE   2 SEE REMARK 15.
FTNOTE   3 SEE REMARK 16.
HET     ZN    501       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    ZN 2+
HELIX    1  H1 THR     14  GLN     28  1AA 26-28 FORM ALPHA(II) HELIX     15
HELIX    2  H2 GLU     72  GLU     88  1                                  17
HELIX    3  H3 PRO     94  MET    103  1AA 100-103 FORM ALPHA(II) HLX     10
HELIX    4  H4 ASN    112  GLU    122  1CONTAINS ONLY 1-2 H-BONDS.        11
HELIX    5  H5 GLU    173  GLY    187  1                                  15
HELIX    6  H6 ASP    215  LYS    231  1                                  17
HELIX    7  H7 SER    254  GLY    262  1AA 260-262 FORM ALPHA(II) HLX      9
HELIX    8  H8 GLN    285  ASN    306  1                                  22
SHEET    1  S1 8 LEU    32  LEU    36  0
SHEET    2  S1 8 VAL    49  SER    53 -1  N  LYS    51   O  SER    34
SHEET    3  S1 8 ASP   104  ILE   109 -1  N  LEU   107   O  LEU    50
SHEET    4  S1 8 PRO    60  LEU    66  1  N  ILE    64   O  PHE   106
SHEET    5  S1 8 LYS   190  HIS   196  1  N  LEU   193   O  TRP    63
SHEET    6  S1 8 TYR   265  LEU   271  1  N  PHE   269   O  SER   194
SHEET    7  S1 8 GLN   200  TYR   204 -1  N  LEU   203   O  THR   268
SHEET    8  S1 8 LYS   239  GLY   241  1  N  GLY   241   O  LEU   202
TURN     1  T1 SER     3  THR     6     NR-III
TURN     2  T2 THR     4  PHE     7     NR-I
TURN     3  T3 HIS    29  LEU    32     RT-I
TURN     4  T4 SER    41  GLY    44     RT-I
TURN     5  T5 GLY    56  ARG    59     NR-(I)
TURN     6  T6 GLY    67  SER    70     O-(I)
TURN     7  T7 GLU    72  THR    75     NR-III
TURN     8  T8 LYS    85  GLU    88     RT-I
TURN     9  T9 ASN    89  GLN    92     O-(II)
TURN    10 T10 ILE    99  SER   102     RT-I
TURN    11 T11 VAL   110  PRO   113     O-(I)
TURN    12 T12 PRO   113  PHE   116     NR-(I)
TURN    13 T13 ALA   117  HIS   120     RT-III
TURN    14 T14 ASN   123  TRP   126     RT-I
TURN    15 T15 ASP   142  ARG   145     O-(I)
TURN    16 T16 ASP   148  PHE   151     O-(II)
TURN    17 T17 GLY   150  LYS   153     NR-II
TURN    18 T18 SER   159  SER   162     RT-III
TURN    19 T19 SER   162  TYR   165     NR-I
TURN    20 T20 TYR   169  SER   172     NR-II
TURN    21 T21 TYR   206  THR   209     O-(III)
TURN    22 T22 ILE   213  LYS   216     O-(I)
TURN    23 T23 ALA   229  SER   232     RT-I
TURN    24 T24 SER   232  GLY   235     O
TURN    25 T25 SER   242  THR   245     NR-(I)
TURN    26 T26 ILE   244  ILE   247     O-(I)
TURN    27 T27 SER   258  GLN   261     RT-I
TURN    28 T28 TYR   259  GLY   262     RT-III
TURN    29 T29 ASP   273  ARG   276     O
TURN    30 T30 GLY   275  GLY   278     O-(I)
TURN    31 T31 TYR   277  LEU   280     NR-II
TURN    32 T32 ALA   283  ILE   286     NR-(I)
SSBOND   1 CYS    138    CYS    161
CRYST1   51.410   59.890   47.190  90.00  97.58  90.00 P 1 21 1      2
ORIGX1      0.787402  0.000000  0.000000        0.00000
ORIGX2      0.000000  0.787402  0.000000        0.00000
ORIGX3      0.000000  0.000000  0.787402        0.00000
SCALE1      0.019451  0.000000  0.002588        0.00000
SCALE2      0.000000  0.016697  0.000000        0.00000
SCALE3      0.000000  0.000000  0.021378        0.00000
      
PROCHECK
Go to PROCHECK summary
 References