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PDBsum entry 1lnd

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Hydrolase (metalloprotease) PDB id
1lnd
Jmol
Contents
Protein chain
316 a.a. *
Ligands
VAL-LYS
DMS
Metals
_ZN ×2
_CA ×4
Waters ×156
* Residue conservation analysis
HEADER    HYDROLASE (METALLOPROTEASE)             13-MAY-94   1LND
TITLE     A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOLYSIN;
COMPND   3 CHAIN: E;
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 (METALLOPROTEASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.R.HOLLAND,A.C.HAUSRATH,D.JUERS,B.W.MATTHEWS
REVDAT   6   18-JUL-12 1LND    1       REMARK
REVDAT   5   13-JUN-12 1LND    1       REMARK VERSN
REVDAT   4   25-AUG-09 1LND    1       SOURCE
REVDAT   3   14-JUL-09 1LND    1       REMARK
REVDAT   2   24-FEB-09 1LND    1       VERSN
REVDAT   1   08-MAY-95 1LND    0
JRNL        AUTH   D.R.HOLLAND,A.C.HAUSRATH,D.JUERS,B.W.MATTHEWS
JRNL        TITL   STRUCTURAL ANALYSIS OF ZINC SUBSTITUTIONS IN THE ACTIVE SITE
JRNL        TITL 2 OF THERMOLYSIN.
JRNL        REF    PROTEIN SCI.                  V.   4  1955 1995
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   8535232
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   D.R.HOLLAND,D.E.TRONRUD,H.W.PLEY,K.M.FLAHERTY,W.STARK,
REMARK   1  AUTH 2 J.N.JANSONIUS,D.B.MCKAY,B.W.MATTHEWS
REMARK   1  TITL   STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED
REMARK   1  TITL 2 NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING
REMARK   1  TITL 3 CATALYSIS
REMARK   1  REF    BIOCHEMISTRY                  V.  31 11310 1992
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 2
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 3
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 4
REMARK   1  AUTH   M.A.HOLMES,B.W.MATTHEWS
REMARK   1  TITL   BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE
REMARK   1  TITL 2 THERMOLYSIN SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN
REMARK   1  TITL 3 CATALYSIS
REMARK   1  REF    BIOCHEMISTRY                  V.  20  6912 1981
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 5
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 6
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 7
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 8
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 9
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 10
REMARK   1  EDIT   M.O.DAYHOFF
REMARK   1  REF    ATLAS OF PROTEIN SEQUENCE     V.   5    98 1976
REMARK   1  REF  2 AND STRUCTURE (DATA SECTION)
REMARK   1  PUBL   NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK   1  REFN
REMARK   1 REFERENCE 11
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 12
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 13
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 14
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 15
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 16
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 17
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   2
REMARK   2 RESOLUTION.    1.70 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) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 36524
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157
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) : NULL
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) : NULL
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          : 27
REMARK   3   SOLVENT ATOMS            : 156
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) : 0.014 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 1.900 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
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 : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : NULL
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1LND 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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 298.0
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU 200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : MULTIWIRE AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : XUONG-HAMLIN
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN (HOWARD, NIELSEN, XUONG)
REMARK 200  DATA SCALING SOFTWARE          : XENGEN (HOWARD, NIELSEN, XUONG)
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: SINGLE CRYSTAL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR SUBSTITUTION
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   (%): 48.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.2
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 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.77400
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       87.54800
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       65.66100
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      109.43500
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.88700
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.77400
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       87.54800
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      109.43500
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       65.66100
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       21.88700
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: E
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: 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    GLU E 177   CD    GLU E 177   OE2     0.080
REMARK 500    GLU E 187   CD    GLU E 187   OE1     0.084
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 E  16   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASP E  16   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ASP E  37   CB  -  CG  -  OD1 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ASP E  59   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ASP E  72   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ASP E  72   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASP E 150   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ASP E 185   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP E 200   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ASP E 200   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES
REMARK 500    ARG E 203   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP E 207   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP E 207   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ASP E 213   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ASP E 215   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG E 220   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP E 226   CB  -  CG  -  OD1 ANGL. DEV. =   8.4 DEGREES
REMARK 500    ASP E 226   CB  -  CG  -  OD2 ANGL. DEV. =  -7.7 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    SER E  25       81.40   -159.55
REMARK 500    THR E  26      -62.88     80.47
REMARK 500    SER E  92     -170.74     64.56
REMARK 500    SER E 107     -162.66     60.87
REMARK 500    ASN E 111       50.83    -90.58
REMARK 500    THR E 152      -99.76   -117.19
REMARK 500    ASN E 159     -144.58     57.63
REMARK 500    THR E 194       72.03     36.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH E 994        DISTANCE =  5.51 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 RESIDUES 1321 AND 1322 FORM A DIPEPTIDE (VAL-LYS) BOUND IN THE
REMARK 600 ACTIVE SITE OF THE MOLECULE. IT IS PRESUMED THAT THE ORIGIN OF THIS
REMARK 600 DIPEPTIDE IS THE C-TERMINAL TWO RESIDUES OF THE PROTEIN. SINCE THE
REMARK 600 C-TERMINUS APPEARS AT FULL OCCUPANCY, MOLECULES NOT INCORPORATED
REMARK 600 INTO THE CRYSTAL MUST HAVE BEEN SACRIFICED. ONE ZINC ION IS THE
REMARK 600 NATIVE ZINC AND IS BOUND TO HOH 673, HIS 142, HIS 146, AND GLU 166.
REMARK 600 A SECOND (PARTIALLY-OCCUPIED) ZINC IS BOUND TO HIS 231, TYR 157,
REMARK 600 GLU 166, AND HOH 673.
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                              ZN E 800  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 142   NE2
REMARK 620 2 HIS E 146   NE2 105.0
REMARK 620 3 GLU E 166   OE2 147.0  86.8
REMARK 620 4 HOH E 910   O   115.3 117.2  84.2
REMARK 620 5 GLU E 166   OE1  95.1 111.5  52.1 110.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN E 801  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR E 157   OH
REMARK 620 2 GLU E 166   OE2  73.5
REMARK 620 3 HOH E 910   O   121.5  84.2
REMARK 620 4 HIS E 231   NE2 126.8  87.7 104.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 901  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 138   OD2
REMARK 620 2 GLU E 190   OE1  82.4
REMARK 620 3 GLU E 177   OE1  77.3 127.1
REMARK 620 4 GLU E 177   OE2 125.5 119.2  49.2
REMARK 620 5 GLU E 187   O    85.1  77.6 146.3 144.8
REMARK 620 6 GLU E 190   OE2  99.4  53.2  82.7  68.4 128.9
REMARK 620 7 HOH E 924   O   100.9 154.1  78.3  80.0  77.1 148.3
REMARK 620 8 ASP E 185   OD1 159.3  84.2 123.4  74.9  76.7  84.9  84.6
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 902  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 185   OD2
REMARK 620 2 GLU E 190   OE2  85.9
REMARK 620 3 ASN E 183   O    92.4 177.0
REMARK 620 4 HOH E 905   O   176.3  91.6  89.9
REMARK 620 5 HOH E 906   O   100.5  93.9  88.9  82.5
REMARK 620 6 GLU E 177   OE2  90.4  89.1  88.4  86.8 168.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 903  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E  59   OD1
REMARK 620 2 HOH E 909   O    88.6
REMARK 620 3 ASP E  57   OD1 118.8  84.2
REMARK 620 4 GLN E  61   O    88.7 177.3  96.9
REMARK 620 5 HOH E 908   O    81.8  85.1 156.5  94.7
REMARK 620 6 HOH E 963   O   158.4  98.7  82.3  83.8  78.7
REMARK 620 7 ASP E  57   OD2  66.3  88.9  52.9  89.9 147.6 133.7
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 904  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 194   O
REMARK 620 2 THR E 194   OG1  68.2
REMARK 620 3 HOH E 907   O    81.8 147.8
REMARK 620 4 HOH E 931   O   154.5 125.4  78.7
REMARK 620 5 ILE E 197   O    80.3 103.4  81.9 112.7
REMARK 620 6 ASP E 200   OD1 131.0  75.1 136.3  74.3  77.8
REMARK 620 7 TYR E 193   O    78.7  78.4  84.8  83.3 156.6 124.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL E 1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS E 1322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS E 320
DBREF  1LND E    1   316  UNP    P00800   THER_BACTH       1    316
SEQRES   1 E  316  ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES   2 E  316  LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES   3 E  316  TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASP GLY ILE
SEQRES   4 E  316  PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES   5 E  316  SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES   6 E  316  TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES   7 E  316  VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES   8 E  316  SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES   9 E  316  HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES  10 E  316  SER GLU MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES  11 E  316  ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES  12 E  316  LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES  13 E  316  TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES  14 E  316  ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES  15 E  316  ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES  16 E  316  GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES  17 E  316  ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES  18 E  316  THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES  19 E  316  GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES  20 E  316  GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES  21 E  316  ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES  22 E  316  TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES  23 E  316  ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES  24 E  316  SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES  25 E  316  VAL GLY VAL LYS
HET    VAL  E1321       7
HET    LYS  E1322      10
HET     ZN  E 800       1
HET     ZN  E 801       1
HET     CA  E 901       1
HET     CA  E 902       1
HET     CA  E 903       1
HET     CA  E 904       1
HET    DMS  E 320       4
HETNAM     VAL VALINE
HETNAM     LYS LYSINE
HETNAM      ZN ZINC ION
HETNAM      CA CALCIUM ION
HETNAM     DMS DIMETHYL SULFOXIDE
FORMUL   2  VAL    C5 H11 N O2
FORMUL   3  LYS    C6 H15 N2 O2 1+
FORMUL   4   ZN    2(ZN 2+)
FORMUL   6   CA    4(CA 2+)
FORMUL  10  DMS    C2 H6 O S
FORMUL  11  HOH   *156(H2 O)
HELIX    1  H1 SER E   65  VAL E   87  165,66 3/10 OR ALPHA-II CONFN      23
HELIX    2  H2 LEU E  133  GLY E  135  5                                   3
HELIX    3  H3 ILE E  137  ASP E  150  1151 IN ALPHA-II CONFORMATION      14
HELIX    4  H4 GLU E  160  ALA E  180  1180 IN 3/10 CONFORMATION          21
HELIX    5  H5 GLU E  190  VAL E  192  1192 IN 3/10 OR ALPHA-II CONFN      3
HELIX    6  H6 PRO E  208  TYR E  211  5                                   4
HELIX    7  H7 TYR E  217  LYS E  219  5                                   3
HELIX    8  H8 ASP E  226  GLY E  229  6LEFT-HAND ALPHA HELIX              4
HELIX    9  H9 ASN E  233  GLN E  246  1233,234 IN 3/10 CONFORMATION      14
HELIX   10 H10 ARG E  260  TYR E  274  1262 IN ALPHA-II CONFORMATION      15
HELIX   11 H11 PHE E  281  TYR E  296  1                                  16
HELIX   12 H12 GLN E  301  VAL E  313  1313 IN 3/10 CONFORMATION          13
SHEET    1  S1 5 GLN E  31  ASP E  32  0
SHEET    2  S1 5 ILE E  39  ASP E  43 -1  N  ILE E  39   O  ASP E  32
SHEET    3  S1 5 ILE E 100  TYR E 106  1  N  SER E 102   O  PHE E  40
SHEET    4  S1 5 GLU E 119  TYR E 122  1  N  TYR E 122   O  SER E 103
SHEET    5  S1 5 ASN E 112  TRP E 115 -1  N  PHE E 114   O  VAL E 121
SHEET    1  S2 5 GLY E  52  LEU E  54  0
SHEET    2  S2 5 ILE E  39  ASP E  43 -1  N  ASP E  43   O  SER E  53
SHEET    3  S2 5 ILE E 100  TYR E 106  1  N  SER E 102   O  PHE E  40
SHEET    4  S2 5 GLU E 119  TYR E 122  1  N  TYR E 122   O  SER E 103
SHEET    5  S2 5 ASN E 112  TRP E 115 -1  N  PHE E 114   O  VAL E 121
SHEET    1  S3 5 TRP E  55  ASP E  57  0
SHEET    2  S3 5 TYR E  27  TYR E  29 -1  O  TYR E  28   N  ASP E  57
SHEET    3  S3 5 ASP E  16  SER E  25 -1  O  THR E  23   N  TYR E  29
SHEET    4  S3 5 THR E   2  ARG E  11 -1  O  THR E   6   N  THR E  22
SHEET    5  S3 5 GLN E  61  PHE E  62  1  N  PHE E  62   O  VAL E   9
LINK        ZN    ZN E 800                 NE2 HIS E 142     1555   1555  1.91
LINK        ZN    ZN E 800                 NE2 HIS E 146     1555   1555  2.01
LINK        ZN    ZN E 800                 OE2 GLU E 166     1555   1555  2.68
LINK        ZN    ZN E 800                 O   HOH E 910     1555   1555  1.83
LINK        ZN    ZN E 800                 OE1 GLU E 166     1555   1555  2.08
LINK        ZN    ZN E 801                 OH  TYR E 157     1555   1555  1.82
LINK        ZN    ZN E 801                 OE2 GLU E 166     1555   1555  2.59
LINK        ZN    ZN E 801                 O   HOH E 910     1555   1555  1.96
LINK        ZN    ZN E 801                 NE2 HIS E 231     1555   1555  2.31
LINK        CA    CA E 901                 OD2 ASP E 138     1555   1555  2.30
LINK        CA    CA E 901                 OE1 GLU E 190     1555   1555  2.47
LINK        CA    CA E 901                 OE1 GLU E 177     1555   1555  2.49
LINK        CA    CA E 901                 OE2 GLU E 177     1555   1555  2.85
LINK        CA    CA E 901                 O   GLU E 187     1555   1555  2.20
LINK        CA    CA E 901                 OE2 GLU E 190     1555   1555  2.55
LINK        CA    CA E 901                 O   HOH E 924     1555   1555  2.53
LINK        CA    CA E 901                 OD1 ASP E 185     1555   1555  2.44
LINK        CA    CA E 902                 OD2 ASP E 185     1555   1555  2.19
LINK        CA    CA E 902                 OE2 GLU E 190     1555   1555  2.13
LINK        CA    CA E 902                 O   ASN E 183     1555   1555  2.39
LINK        CA    CA E 902                 O   HOH E 905     1555   1555  2.24
LINK        CA    CA E 902                 O   HOH E 906     1555   1555  2.14
LINK        CA    CA E 902                 OE2 GLU E 177     1555   1555  2.21
LINK        CA    CA E 903                 OD1 ASP E  59     1555   1555  2.35
LINK        CA    CA E 903                 O   HOH E 909     1555   1555  2.34
LINK        CA    CA E 903                 OD1 ASP E  57     1555   1555  2.41
LINK        CA    CA E 903                 O   GLN E  61     1555   1555  2.28
LINK        CA    CA E 903                 O   HOH E 908     1555   1555  2.35
LINK        CA    CA E 903                 O   HOH E 963     1555   1555  2.45
LINK        CA    CA E 903                 OD2 ASP E  57     1555   1555  2.58
LINK        CA    CA E 904                 O   THR E 194     1555   1555  2.34
LINK        CA    CA E 904                 OG1 THR E 194     1555   1555  2.26
LINK        CA    CA E 904                 O   HOH E 907     1555   1555  2.21
LINK        CA    CA E 904                 O   HOH E 931     1555   1555  2.49
LINK        CA    CA E 904                 O   ILE E 197     1555   1555  2.22
LINK        CA    CA E 904                 OD1 ASP E 200     1555   1555  2.24
LINK        CA    CA E 904                 O   TYR E 193     1555   1555  2.36
LINK         C   VAL E1321                 N   LYS E1322     1555   1555  1.33
CISPEP   1 LEU E   50    PRO E   51          0         3.51
SITE     1 ZN1  4 GLU E 166  HIS E 142  HIS E 146  HOH E 910
SITE     1 ZN2  3 TYR E 157  HIS E 231  HOH E 910
SITE     1 AC1  6 ASN E 112  ALA E 113  GLU E 143  ARG E 203
SITE     2 AC1  6 HIS E 231  LYS E1322
SITE     1 AC2  5 ASN E 111  ASN E 112  HIS E 231  HOH E 604
SITE     2 AC2  5 VAL E1321
SITE     1 AC3  6 HIS E 142  GLU E 143  HIS E 146  GLU E 166
SITE     2 AC3  6  ZN E 801  HOH E 910
SITE     1 AC4  5 TYR E 157  GLU E 166  HIS E 231   ZN E 800
SITE     2 AC4  5 HOH E 910
SITE     1 AC5  7 ASP E 138  GLU E 177  ASP E 185  GLU E 187
SITE     2 AC5  7 GLU E 190   CA E 902  HOH E 924
SITE     1 AC6  7 GLU E 177  ASN E 183  ASP E 185  GLU E 190
SITE     2 AC6  7  CA E 901  HOH E 905  HOH E 906
SITE     1 AC7  6 ASP E  57  ASP E  59  GLN E  61  HOH E 908
SITE     2 AC7  6 HOH E 909  HOH E 963
SITE     1 AC8  6 TYR E 193  THR E 194  ILE E 197  ASP E 200
SITE     2 AC8  6 HOH E 907  HOH E 931
SITE     1 AC9  3 SER E 218  TYR E 251  HOH E 997
CRYST1   93.852   93.852  131.322  90.00  90.00 120.00 P 61 2 2     12
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      0.010655  0.006152  0.000000        0.00000
SCALE2      0.000000  0.012303  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007615        0.00000
      
PROCHECK
Go to PROCHECK summary
 References