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PDBsum entry 4tln

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Hydrolase (metalloproteinase) PDB id
4tln
Jmol
Contents
Protein chain
316 a.a.
Ligands
LNO
Metals
_CA ×4
_ZN
Waters ×150
HEADER    HYDROLASE (METALLOPROTEINASE)           08-FEB-82   4TLN
TITLE     BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE THERMOLYSIN
TITLE    2 SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN CATALYSIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOLYSIN;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.4.24.27;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE   3 ORGANISM_TAXID: 1427
KEYWDS    HYDROLASE (METALLOPROTEINASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.W.MATTHEWS,M.A.HOLMES
REVDAT   9   13-JUL-11 4TLN    1       VERSN
REVDAT   8   14-JUL-09 4TLN    1       REMARK
REVDAT   7   24-FEB-09 4TLN    1       VERSN
REVDAT   6   08-MAR-95 4TLN    1       COMPND
REVDAT   5   31-JAN-84 4TLN    1       JRNL   REMARK
REVDAT   4   30-SEP-83 4TLN    1       REVDAT
REVDAT   3   03-DEC-82 4TLN    1       REMARK
REVDAT   2   30-AUG-82 4TLN    1       REMARK
REVDAT   1   26-MAY-82 4TLN    0
JRNL        AUTH   M.A.HOLMES,B.W.MATTHEWS
JRNL        TITL   BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE
JRNL        TITL 2 THERMOLYSIN SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN
JRNL        TITL 3 CATALYSIS.
JRNL        REF    BIOCHEMISTRY                  V.  20  6912 1981
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   7317361
JRNL        DOI    10.1021/BI00527A026
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.A.HOLMES,B.W.MATTHEWS
REMARK   1  TITL   STRUCTURE OF THERMOLYSIN REFINED AT 1.6 ANGSTROMS RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 160   623 1982
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 2
REMARK   1  AUTH   A.F.MONZINGO,B.W.MATTHEWS
REMARK   1  TITL   STRUCTURE OF A MERCAPTAN-THERMOLYSIN COMPLEX ILLUSTRATES
REMARK   1  TITL 2 MODE OF INHIBITION OF ZINC PROTEASES BY SUBSTRATE-ANALOGUE
REMARK   1  TITL 3 MERCAPTANS
REMARK   1  REF    BIOCHEMISTRY                  V.  21  3390 1982
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 3
REMARK   1  AUTH   M.C.BOLOGNESI,B.W.MATTHEWS
REMARK   1  TITL   BINDING OF THE BIPRODUCT ANALOG L-BENZYLSUCCINIC ACID TO
REMARK   1  TITL 2 THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY
REMARK   1  REF    J.BIOL.CHEM.                  V. 254   634 1979
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 4
REMARK   1  AUTH   W.R.KESTER,B.W.MATTHEWS
REMARK   1  TITL   COMPARISON OF THE STRUCTURES OF CARBOXYPEPTIDASE A AND
REMARK   1  TITL 2 THERMOLYSIN
REMARK   1  REF    J.BIOL.CHEM.                  V. 252  7704 1977
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 5
REMARK   1  AUTH   L.H.WEAVER,W.R.KESTER,B.W.MATTHEWS
REMARK   1  TITL   A CRYSTALLOGRAPHIC STUDY OF THE COMPLEX OF PHOSPHORAMIDON
REMARK   1  TITL 2 WITH THERMOLYSIN. A MODEL FOR THE PRESUMED CATALYTIC
REMARK   1  TITL 3 TRANSITION STATE AND FOR THE BINDING OF EXTENDED SUBSTRATES
REMARK   1  REF    J.MOL.BIOL.                   V. 114   119 1977
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 6
REMARK   1  AUTH   W.R.KESTER,B.W.MATTHEWS
REMARK   1  TITL   CRYSTALLOGRAPHIC STUDY OF THE BINDING OF DIPEPTIDE
REMARK   1  TITL 2 INHIBITORS TO THERMOLYSIN. IMPLICATIONS FOR THE MECHANISM OF
REMARK   1  TITL 3 CATALYSIS
REMARK   1  REF    BIOCHEMISTRY                  V.  16  2506 1977
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 7
REMARK   1  AUTH   F.W.DAHLQUIST,J.W.LONG,W.L.BIGBEE
REMARK   1  TITL   ROLE OF CALCIUM IN THE THERMAL STABILITY OF THERMOLYSIN
REMARK   1  REF    BIOCHEMISTRY                  V.  15  1103 1976
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 8
REMARK   1  AUTH   P.L.LEVY,M.K.PANGBURN,Y.BURSTEIN,L.H.ERICSSON,H.NEURATH,
REMARK   1  AUTH 2 K.A.WALSH
REMARK   1  TITL   EVIDENCE OF HOMOLOGOUS RELATIONSHIP BETWEEN THERMOLYSIN AND
REMARK   1  TITL 2 NEUTRAL PROTEASE A OF BACILLUS SUBTILIS
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  72  4341 1975
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1 REFERENCE 9
REMARK   1  AUTH   B.W.MATTHEWS,L.H.WEAVER,W.R.KESTER
REMARK   1  TITL   THE CONFORMATION OF THERMOLYSIN
REMARK   1  REF    J.BIOL.CHEM.                  V. 249  8030 1974
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 10
REMARK   1  AUTH   B.W.MATTHEWS,L.H.WEAVER
REMARK   1  TITL   BINDING OF LANTHANIDE IONS TO THERMOLYSIN
REMARK   1  REF    BIOCHEMISTRY                  V.  13  1719 1974
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 11
REMARK   1  AUTH   P.M.COLMAN,J.N.JANSONIUS,B.W.MATTHEWS
REMARK   1  TITL   THE STRUCTURE OF THERMOLYSIN,AN ELECTRON DENSITY MAP AT 2.3
REMARK   1  TITL 2 ANGSTROMS RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V.  70   701 1972
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 12
REMARK   1  AUTH   K.TITANI,M.A.HERMODSON,L.H.ERICSSON,K.A.WALSH,H.NEURATH
REMARK   1  TITL   AMINO-ACID SEQUENCE OF THERMOLYSIN
REMARK   1  REF    NATURE NEW BIOL.              V. 238    35 1972
REMARK   1  REFN                   ISSN 0369-4887
REMARK   1 REFERENCE 13
REMARK   1  AUTH   B.W.MATTHEWS,J.N.JANSONIUS,P.M.COLMAN,B.P.SCHOENBORN,
REMARK   1  AUTH 2 D.DUPORQUE
REMARK   1  TITL   THREE DIMENSIONAL STRUCTURE OF THERMOLYSIN
REMARK   1  REF    NATURE NEW BIOL.              V. 238    37 1972
REMARK   1  REFN                   ISSN 0369-4887
REMARK   1 REFERENCE 14
REMARK   1  AUTH   B.W.MATTHEWS,P.M.COLMAN,J.N.JANSONIUS,K.TITANI,K.A.WALSH,
REMARK   1  AUTH 2 H.NEURATH
REMARK   1  TITL   STRUCTURE OF THERMOLYSIN
REMARK   1  REF    NATURE NEW BIOL.              V. 238    41 1972
REMARK   1  REFN                   ISSN 0369-4887
REMARK   1 REFERENCE 15
REMARK   1  EDIT   M.O.DAYHOFF
REMARK   1  REF    ATLAS OF PROTEIN SEQUENCE     V.   5    98 1976
REMARK   1  REF  2 AND STRUCTURE,SUPPLEMENT 2
REMARK   1  PUBL   NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK   1  REFN                   ISSN 0-912466-05-7
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 11854
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NONE
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169
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
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1690
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 11854
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2432
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 15
REMARK   3   SOLVENT ATOMS            : 150
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : 0.045 ; NULL  ; 2500
REMARK   3   BOND ANGLES            (DEGREES) : 5.900 ; NULL  ; 3395
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; 0.000 ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; 0.000 ; 0
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.007 ; NULL  ; 66
REMARK   3   GENERAL PLANES               (A) : 0.012 ; NULL  ; 375
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; 0.000 ; 0
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NONE
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : TNT PROTGEO VERSION 1.0
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: ATOM 2448 IN HET GROUP *LNO* IS AN
REMARK   3  OXYGEN ATOM AND IS IDENTIFIED IN THIS ENTRY AS * ON2*. IN THE
REMARK   3  PAPER CITED IN THE JRNL RECORDS ABOVE IT IS IDENTIFIED AS * N2O*.
REMARK   4
REMARK   4 4TLN 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        : 1980
REMARK 200  TEMPERATURE           (KELVIN) : 285
REMARK 200  PH                             : 7.2
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          : ELLIOTT GX-3
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NICKEL FILTER
REMARK 200  OPTICS                         : ADJUSTABLE COLLIMATOR SLIT
REMARK 200
REMARK 200  DETECTOR TYPE                  : FILM
REMARK 200  DETECTOR MANUFACTURER          : KODAK
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : VENUS
REMARK 200  DATA SCALING SOFTWARE          : ODPROC
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12029
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.600
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.02600
REMARK 200  R SYM                      (I) : 0.06300
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 CRYSTAL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR SUBSTATUTION
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: DATA COLLECTED WITH PRECESSION PHOTOGRAPHY
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.2
REMARK 285
REMARK 285 THE ENTRY COORDINATES
REMARK 285 ARE NOT PRESENTED IN THE STANDARD CRYSTAL FRAME.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
REMARK 290       7555   Y,X,-Z+1/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+2/3
REMARK 290      10555   -Y,-X,-Z+5/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+1/6
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 -0.500000 -0.866047  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866004 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.80201
REMARK 290   SMTRY1   3 -0.500000  0.866047  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866004 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       87.60403
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       65.70302
REMARK 290   SMTRY1   5  0.500000  0.866047  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866004  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      109.50504
REMARK 290   SMTRY1   6  0.500000 -0.866047  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866004  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.90101
REMARK 290   SMTRY1   7  0.500000  0.866047  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866004 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.80201
REMARK 290   SMTRY1   8  0.500000 -0.866047  0.000000        0.00000
REMARK 290   SMTRY2   8 -0.866004 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       87.60403
REMARK 290   SMTRY1  10 -0.500000 -0.866047  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866004  0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      109.50504
REMARK 290   SMTRY1  11 -0.500000  0.866047  0.000000        0.00000
REMARK 290   SMTRY2  11  0.866004  0.500000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       65.70302
REMARK 290   SMTRY1  12  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       21.90101
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 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 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   N    PHE A    62     O    HOH A   421              0.82
REMARK 500   C    GLN A    61     O    HOH A   421              1.05
REMARK 500   CB   VAL A   230     O    HOH A   440              1.27
REMARK 500   C    GLY A   228     O    HOH A   382              1.56
REMARK 500   N    SER A   118     O    HOH A   442              1.78
REMARK 500   OD1  ASN A   116     O    HOH A   442              1.78
REMARK 500   CG1  VAL A   230     O    HOH A   440              1.79
REMARK 500   ND1  HIS A   216     O    HOH A   435              1.88
REMARK 500   N    GLY A   229     O    HOH A   382              1.92
REMARK 500   CA   PHE A    62     O    HOH A   421              1.94
REMARK 500   OE1  GLU A   119     O    HOH A   447              1.97
REMARK 500   CA   GLY A   228     O    HOH A   382              2.03
REMARK 500   OG   SER A    92     O    HOH A   451              2.04
REMARK 500   O    GLN A    61     O    HOH A   421              2.04
REMARK 500   O    HOH A   410     O    HOH A   492              2.09
REMARK 500   CA   GLN A    61     O    HOH A   421              2.12
REMARK 500   OE1  GLU A   187     O    HOH A   411              2.16
REMARK 500   O    GLY A   228     O    HOH A   382              2.16
REMARK 500   NH1  ARG A   269     OD2  ASP A   294              2.18
REMARK 500   OG   SER A   102     O    HOH A   408              2.18
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   O    HOH A   372     O    HOH A   409     5564     0.93
REMARK 500   O    HOH A   407     O    HOH A   369     6655     1.42
REMARK 500   O    HOH A   333     O    HOH A   337    10664     1.74
REMARK 500   O    HOH A   418     O    HOH A   418    12565     1.75
REMARK 500   O    HOH A   332     O    HOH A   336    10664     1.75
REMARK 500   O    HOH A   485     O    HOH A   485     7555     1.80
REMARK 500   O    HOH A   379     O    HOH A   396    10664     2.01
REMARK 500   CB   THR A     6     O    HOH A   473    12565     2.03
REMARK 500   O    ASN A   116     O    HOH A   336    10664     2.11
REMARK 500   O    HOH A   463     O    HOH A   372     6655     2.14
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    THR A   4   C     THR A   4   O       0.117
REMARK 500    SER A   5   CB    SER A   5   OG      0.091
REMARK 500    GLY A   8   N     GLY A   8   CA      0.140
REMARK 500    ARG A  11   NE    ARG A  11   CZ      0.101
REMARK 500    ILE A  20   C     ILE A  20   O       0.117
REMARK 500    SER A  25   CB    SER A  25   OG      0.148
REMARK 500    ARG A  35   C     GLY A  36   N      -0.183
REMARK 500    GLY A  52   C     GLY A  52   O       0.106
REMARK 500    SER A  53   CA    SER A  53   CB      0.163
REMARK 500    ALA A  77   C     ALA A  77   O      -0.119
REMARK 500    SER A  92   CB    SER A  92   OG      0.089
REMARK 500    GLY A  95   C     GLY A  95   O       0.112
REMARK 500    ARG A 101   CG    ARG A 101   CD      0.303
REMARK 500    ARG A 101   NE    ARG A 101   CZ     -0.094
REMARK 500    ARG A 101   CZ    ARG A 101   NH2     0.091
REMARK 500    SER A 102   CA    SER A 102   CB      0.105
REMARK 500    HIS A 105   CG    HIS A 105   CD2     0.067
REMARK 500    GLN A 108   C     GLN A 108   O       0.135
REMARK 500    SER A 118   CB    SER A 118   OG     -0.090
REMARK 500    GLU A 119   CB    GLU A 119   CG     -0.135
REMARK 500    GLU A 119   CD    GLU A 119   OE1    -0.133
REMARK 500    GLY A 123   CA    GLY A 123   C       0.098
REMARK 500    GLU A 143   CD    GLU A 143   OE1    -0.077
REMARK 500    GLU A 160   CD    GLU A 160   OE2    -0.085
REMARK 500    GLY A 162   C     GLY A 162   O       0.107
REMARK 500    GLU A 166   CD    GLU A 166   OE1    -0.128
REMARK 500    GLY A 173   CA    GLY A 173   C      -0.111
REMARK 500    LYS A 182   CE    LYS A 182   NZ      0.154
REMARK 500    TRP A 186   CG    TRP A 186   CD2     0.126
REMARK 500    GLU A 190   CD    GLU A 190   OE1    -0.076
REMARK 500    THR A 194   CB    THR A 194   OG1     0.135
REMARK 500    ASP A 213   CG    ASP A 213   OD2     0.141
REMARK 500    HIS A 216   CG    HIS A 216   ND1    -0.103
REMARK 500    SER A 218   CB    SER A 218   OG     -0.088
REMARK 500    GLY A 235   C     GLY A 235   O       0.115
REMARK 500    GLY A 252   C     GLY A 252   O       0.102
REMARK 500    VAL A 256   N     VAL A 256   CA      0.142
REMARK 500    ARG A 260   C     ASP A 261   N      -0.182
REMARK 500    LYS A 265   CA    LYS A 265   CB     -0.145
REMARK 500    LYS A 265   CE    LYS A 265   NZ      0.204
REMARK 500    PHE A 267   C     PHE A 267   O       0.129
REMARK 500    THR A 278   CB    THR A 278   OG1     0.143
REMARK 500    LYS A 316   C     LYS A 316   OXT     0.139
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    SER A   5   N   -  CA  -  CB  ANGL. DEV. =  10.7 DEGREES
REMARK 500    VAL A   9   CB  -  CA  -  C   ANGL. DEV. = -14.8 DEGREES
REMARK 500    GLY A   8   O   -  C   -  N   ANGL. DEV. = -10.9 DEGREES
REMARK 500    VAL A   9   CA  -  C   -  N   ANGL. DEV. =  12.3 DEGREES
REMARK 500    ARG A  11   CD  -  NE  -  CZ  ANGL. DEV. = -16.1 DEGREES
REMARK 500    ARG A  11   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.9 DEGREES
REMARK 500    ARG A  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ASP A  16   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    LYS A  18   CG  -  CD  -  CE  ANGL. DEV. =  18.9 DEGREES
REMARK 500    LYS A  18   O   -  C   -  N   ANGL. DEV. =  11.9 DEGREES
REMARK 500    TYR A  24   CB  -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    TYR A  24   CG  -  CD1 -  CE1 ANGL. DEV. =   8.2 DEGREES
REMARK 500    TYR A  27   CB  -  CG  -  CD2 ANGL. DEV. =  -9.7 DEGREES
REMARK 500    TYR A  27   CB  -  CG  -  CD1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    TYR A  27   CZ  -  CE2 -  CD2 ANGL. DEV. = -11.2 DEGREES
REMARK 500    TYR A  29   CB  -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    TYR A  29   CB  -  CG  -  CD1 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ASP A  32   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG A  35   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ARG A  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ASP A  37   CB  -  CG  -  OD2 ANGL. DEV. =  11.3 DEGREES
REMARK 500    GLY A  38   CA  -  C   -  O   ANGL. DEV. = -13.2 DEGREES
REMARK 500    GLY A  38   C   -  N   -  CA  ANGL. DEV. =  19.5 DEGREES
REMARK 500    ILE A  39   CB  -  CG1 -  CD1 ANGL. DEV. =  20.0 DEGREES
REMARK 500    GLY A  38   O   -  C   -  N   ANGL. DEV. =  10.8 DEGREES
REMARK 500    PHE A  40   C   -  N   -  CA  ANGL. DEV. =  16.4 DEGREES
REMARK 500    TYR A  42   CG  -  CD1 -  CE1 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    TYR A  42   CZ  -  CE2 -  CD2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    LYS A  45   CB  -  CA  -  C   ANGL. DEV. = -13.1 DEGREES
REMARK 500    LYS A  45   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES
REMARK 500    LYS A  45   O   -  C   -  N   ANGL. DEV. =  10.4 DEGREES
REMARK 500    ARG A  47   CD  -  NE  -  CZ  ANGL. DEV. =  31.9 DEGREES
REMARK 500    ARG A  47   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ARG A  47   NE  -  CZ  -  NH1 ANGL. DEV. =  12.3 DEGREES
REMARK 500    ARG A  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    THR A  49   CA  -  CB  -  OG1 ANGL. DEV. = -12.7 DEGREES
REMARK 500    THR A  49   O   -  C   -  N   ANGL. DEV. =  11.7 DEGREES
REMARK 500    SER A  53   CB  -  CA  -  C   ANGL. DEV. = -13.8 DEGREES
REMARK 500    SER A  53   CA  -  C   -  N   ANGL. DEV. =  13.3 DEGREES
REMARK 500    ALA A  56   CA  -  C   -  O   ANGL. DEV. =  16.2 DEGREES
REMARK 500    ALA A  56   O   -  C   -  N   ANGL. DEV. = -11.4 DEGREES
REMARK 500    ASP A  59   CB  -  CG  -  OD2 ANGL. DEV. =   9.0 DEGREES
REMARK 500    GLN A  61   O   -  C   -  N   ANGL. DEV. =  12.1 DEGREES
REMARK 500    SER A  65   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES
REMARK 500    TYR A  66   CG  -  CD2 -  CE2 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ASP A  67   OD1 -  CG  -  OD2 ANGL. DEV. = -12.0 DEGREES
REMARK 500    ASP A  67   CB  -  CG  -  OD1 ANGL. DEV. =  13.7 DEGREES
REMARK 500    ASP A  67   C   -  N   -  CA  ANGL. DEV. =  20.4 DEGREES
REMARK 500    ALA A  70   CA  -  C   -  O   ANGL. DEV. =  13.0 DEGREES
REMARK 500    ALA A  70   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     190 ANGLE DEVIATIONS.
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    SER A  25       84.05   -163.27
REMARK 500    THR A  26      -47.94     67.27
REMARK 500    PHE A  62       59.47   -113.29
REMARK 500    SER A  92      177.54     66.82
REMARK 500    SER A 107     -168.00     60.77
REMARK 500    ASN A 112      173.51    174.28
REMARK 500    SER A 118       -1.77   -148.78
REMARK 500    GLN A 128      -42.75   -136.85
REMARK 500    THR A 152      -99.44   -113.05
REMARK 500    TYR A 157       45.09    -76.54
REMARK 500    ASN A 159     -142.50     62.10
REMARK 500    THR A 194       84.19     29.10
REMARK 500    ILE A 232      -61.85    -99.74
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    ARG A 101        49.0      L          L   OUTSIDE RANGE
REMARK 500    ARG A 260        22.8      L          L   OUTSIDE RANGE
REMARK 500    ASP A 261        45.5      L          L   OUTSIDE RANGE
REMARK 500    PHE A 267        25.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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 317  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 190   OE1
REMARK 620 2 GLU A 177   OE2 124.7
REMARK 620 3 HOH A 346   O   146.9  82.2
REMARK 620 4 ASP A 185   OD2  85.2  81.0  80.4
REMARK 620 5 GLU A 177   OE1 134.2  45.3  77.7 123.9
REMARK 620 6 ASP A 138   OD1  81.9 124.1  99.1 154.8  80.0
REMARK 620 7 GLU A 190   OE2  50.5  75.5 156.1  87.6  92.4 100.5
REMARK 620 8 GLU A 187   O    75.0 151.1  73.3  79.9 138.3  75.9 124.9
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 318  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 183   O
REMARK 620 2 GLU A 177   OE2  86.0
REMARK 620 3 GLU A 190   OE2 167.0  88.7
REMARK 620 4 HOH A 353   O    86.9  87.4 104.7
REMARK 620 5 HOH A 475   O    88.7 174.5  96.1  93.9
REMARK 620 6 ASP A 185   OD1  91.1  89.2  76.9 176.1  89.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 319  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 482   O
REMARK 620 2 GLN A  61   O    86.8
REMARK 620 3 ASP A  59   OD1  73.2  80.3
REMARK 620 4 ASP A  57   OD2 146.5  86.3  73.3
REMARK 620 5 ASP A  57   OD1 160.8  94.7 125.9  52.7
REMARK 620 6 HOH A 419   O    74.9  85.1 145.5 136.9  86.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 320  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 480   O
REMARK 620 2 HOH A 354   O    78.8
REMARK 620 3 ASP A 200   OD1 136.0  77.5
REMARK 620 4 ILE A 197   O    64.1 117.5  95.6
REMARK 620 5 THR A 194   OG1 149.6 127.8  71.1 106.3
REMARK 620 6 TYR A 193   O    89.5  84.9 124.3 138.5  80.0
REMARK 620 7 THR A 194   O    86.4 150.4 128.9  77.1  63.2  69.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 321  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LNO A 322   O
REMARK 620 2 LNO A 322   ON2  69.4
REMARK 620 3 HIS A 146   NE2 138.3  72.5
REMARK 620 4 HIS A 142   NE2 109.6 101.4  93.7
REMARK 620 5 GLU A 166   OE1  92.5 135.1 102.9 123.5
REMARK 620 N                    1     2     3     4
REMARK 700
REMARK 700 SHEET
REMARK 700 THE *ACTIVE-SITE* SHEET SUBSTRUCTURE OF THIS MOLECULE HAS
REMARK 700 ONE EDGE-STRAND COMPRISED OF TWO DISTINCT SEQUENCES OF THE
REMARK 700 POLYPEPTIDE CHAIN. TO REPRESENT THIS FEATURE AN EXTRA SHEET
REMARK 700 IS DEFINED.  STRANDS 2,3,4,5 OF S1 ARE IDENTICAL TO STRANDS
REMARK 700 2,3,4,5 OF S2.
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 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNO A 322
DBREF  4TLN A    1   316  UNP    P00800   THER_BACTH       1    316
SEQRES   1 A  316  ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES   2 A  316  LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES   3 A  316  TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASP GLY ILE
SEQRES   4 A  316  PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES   5 A  316  SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES   6 A  316  TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES   7 A  316  VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES   8 A  316  SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES   9 A  316  HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES  10 A  316  SER GLU MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES  11 A  316  ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES  12 A  316  LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES  13 A  316  TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES  14 A  316  ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES  15 A  316  ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES  16 A  316  GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES  17 A  316  ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES  18 A  316  THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES  19 A  316  GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES  20 A  316  GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES  21 A  316  ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES  22 A  316  TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES  23 A  316  ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES  24 A  316  SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES  25 A  316  VAL GLY VAL LYS
HET     CA  A 317       1
HET     CA  A 318       1
HET     CA  A 319       1
HET     CA  A 320       1
HET     ZN  A 321       1
HET    LNO  A 322      10
HETNAM      CA CALCIUM ION
HETNAM      ZN ZINC ION
HETNAM     LNO L-LEUCYL-HYDROXYLAMINE
FORMUL   2   CA    4(CA 2+)
FORMUL   6   ZN    ZN 2+
FORMUL   7  LNO    C6 H14 N2 O2
FORMUL   8  HOH   *150(H2 O)
HELIX    1  H1 SER A   65  VAL A   87  165,66 3/10 OR ALPHA-II CONFN      23
HELIX    2  H2 LEU A  133  GLY A  135  5                                   3
HELIX    3  H3 ILE A  137  ASP A  150  1151 IN ALPHA-II CONFORMATION      14
HELIX    4  H4 GLU A  160  ALA A  180  1180 IN 3/10 CONFORMATION          21
HELIX    5  H5 GLU A  190  VAL A  192  1192 IN 3/10 OR ALPHA-II CONFN      3
HELIX    6  H6 PRO A  208  TYR A  211  5                                   4
HELIX    7  H7 TYR A  217  LYS A  219  5                                   3
HELIX    8  H8 ASP A  226  GLY A  229  6LEFT-HAND ALPHA HELIX              4
HELIX    9  H9 ASN A  233  GLN A  246  1233,234 IN 3/10 CONFORMATION      14
HELIX   10 H10 ARG A  260  TYR A  274  1262 IN ALPHA-II CONFORMATION      15
HELIX   11 H11 PHE A  281  TYR A  296  1                                  16
HELIX   12 H12 GLN A  301  VAL A  313  1313 IN 3/10 CONFORMATION          13
SHEET    1  S1 5 GLN A  31  ASP A  32  0
SHEET    2  S1 5 ILE A  39  ASP A  43 -1  N  ILE A  39   O  ASP A  32
SHEET    3  S1 5 ILE A 100  TYR A 106  1  N  SER A 102   O  PHE A  40
SHEET    4  S1 5 GLU A 119  TYR A 122  1  N  TYR A 122   O  SER A 103
SHEET    5  S1 5 ASN A 112  TRP A 115 -1  N  PHE A 114   O  VAL A 121
SHEET    1  S2 5 GLY A  52  LEU A  54  0
SHEET    2  S2 5 ILE A  39  ASP A  43 -1  N  ASP A  43   O  SER A  53
SHEET    3  S2 5 ILE A 100  TYR A 106  1  N  SER A 102   O  PHE A  40
SHEET    4  S2 5 GLU A 119  TYR A 122  1  N  TYR A 122   O  SER A 103
SHEET    5  S2 5 ASN A 112  TRP A 115 -1  N  PHE A 114   O  VAL A 121
SHEET    1  S3 5 TRP A  55  ASP A  57  0
SHEET    2  S3 5 TYR A  27  TYR A  29 -1  O  TYR A  28   N  ASP A  57
SHEET    3  S3 5 ASP A  16  SER A  25 -1  O  THR A  23   N  TYR A  29
SHEET    4  S3 5 THR A   2  ARG A  11 -1  O  THR A   6   N  THR A  22
SHEET    5  S3 5 GLN A  61  PHE A  62  1  O  VAL A   9   N  PHE A  62
LINK        CA    CA A 317                 OE1 GLU A 190     1555   1555  2.67
LINK        CA    CA A 317                 OE2 GLU A 177     1555   1555  2.83
LINK        CA    CA A 317                 O   HOH A 346     1555   1555  2.74
LINK        CA    CA A 317                 OD2 ASP A 185     1555   1555  2.51
LINK        CA    CA A 317                 OE1 GLU A 177     1555   1555  2.69
LINK        CA    CA A 317                 OD1 ASP A 138     1555   1555  2.58
LINK        CA    CA A 317                 OE2 GLU A 190     1555   1555  2.52
LINK        CA    CA A 317                 O   GLU A 187     1555   1555  2.35
LINK        CA    CA A 318                 O   ASN A 183     1555   1555  2.40
LINK        CA    CA A 318                 OE2 GLU A 177     1555   1555  2.32
LINK        CA    CA A 318                 OE2 GLU A 190     1555   1555  2.37
LINK        CA    CA A 318                 O   HOH A 353     1555   1555  2.37
LINK        CA    CA A 318                 O   HOH A 475     1555   1555  2.00
LINK        CA    CA A 318                 OD1 ASP A 185     1555   1555  2.65
LINK        CA    CA A 319                 O   HOH A 482     1555   1555  2.51
LINK        CA    CA A 319                 O   GLN A  61     1555   1555  2.03
LINK        CA    CA A 319                 OD1 ASP A  59     1555   1555  2.39
LINK        CA    CA A 319                 OD2 ASP A  57     1555   1555  2.51
LINK        CA    CA A 319                 OD1 ASP A  57     1555   1555  2.29
LINK        CA    CA A 319                 O   HOH A 419     1555   1555  2.15
LINK        CA    CA A 320                 O   HOH A 480     1555   1555  2.04
LINK        CA    CA A 320                 O   HOH A 354     1555   1555  2.44
LINK        CA    CA A 320                 OD1 ASP A 200     1555   1555  2.13
LINK        CA    CA A 320                 O   ILE A 197     1555   1555  2.75
LINK        CA    CA A 320                 OG1 THR A 194     1555   1555  2.41
LINK        CA    CA A 320                 O   TYR A 193     1555   1555  2.57
LINK        CA    CA A 320                 O   THR A 194     1555   1555  2.45
LINK        ZN    ZN A 321                 O   LNO A 322     1555   1555  2.00
LINK        ZN    ZN A 321                 ON2 LNO A 322     1555   1555  2.10
LINK        ZN    ZN A 321                 NE2 HIS A 146     1555   1555  1.99
LINK        ZN    ZN A 321                 NE2 HIS A 142     1555   1555  2.27
LINK        ZN    ZN A 321                 OE1 GLU A 166     1555   1555  1.98
CISPEP   1 LEU A   50    PRO A   51          0        -0.15
SITE     1 AC1  6 ASP A 138  GLU A 177  ASP A 185  GLU A 187
SITE     2 AC1  6 GLU A 190  HOH A 346
SITE     1 AC2  6 GLU A 177  ASN A 183  ASP A 185  GLU A 190
SITE     2 AC2  6 HOH A 353  HOH A 475
SITE     1 AC3  5 ASP A  57  ASP A  59  GLN A  61  HOH A 419
SITE     2 AC3  5 HOH A 482
SITE     1 AC4  6 TYR A 193  THR A 194  ILE A 197  ASP A 200
SITE     2 AC4  6 HOH A 354  HOH A 480
SITE     1 AC5  5 HIS A 142  HIS A 146  TYR A 157  GLU A 166
SITE     2 AC5  5 LNO A 322
SITE     1 AC6 11 ASN A 112  ALA A 113  HIS A 142  GLU A 143
SITE     2 AC6 11 HIS A 146  TYR A 157  GLU A 166  ARG A 203
SITE     3 AC6 11 HIS A 231   ZN A 321  HOH A 497
CRYST1   94.200   94.200  131.400  90.00  90.00 120.00 P 61 2 2     12
ORIGX1      1.154699  0.000000  0.000000        0.00000
ORIGX2      0.577350  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.012258  0.000000  0.000000        0.00000
SCALE2      0.006129  0.010616  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007610        0.00000
      
PROCHECK
Go to PROCHECK summary
 References