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PDBsum entry 1ton

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Hydrolase(serine proteinase) PDB id
1ton
Jmol
Contents
Protein chain
228 a.a.
Metals
_ZN
Waters ×149
HEADER    HYDROLASE(SERINE PROTEINASE)            03-JUN-87   1TON
TITLE     RAT SUBMAXILLARY GLAND SERINE PROTEASE, TONIN. STRUCTURE SOLUTION AND
TITLE    2 REFINEMENT AT 1.8 ANGSTROMS RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TONIN;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;
SOURCE   3 ORGANISM_COMMON: BLACK RAT;
SOURCE   4 ORGANISM_TAXID: 10117
KEYWDS    HYDROLASE(SERINE PROTEINASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.FUJINAGA,M.N.G.JAMES
REVDAT   4   13-JUL-11 1TON    1       VERSN
REVDAT   3   24-FEB-09 1TON    1       VERSN
REVDAT   2   01-APR-03 1TON    1       JRNL
REVDAT   1   16-JAN-88 1TON    0
JRNL        AUTH   M.FUJINAGA,M.N.JAMES
JRNL        TITL   RAT SUBMAXILLARY GLAND SERINE PROTEASE, TONIN. STRUCTURE
JRNL        TITL 2 SOLUTION AND REFINEMENT AT 1.8 A RESOLUTION.
JRNL        REF    J.MOL.BIOL.                   V. 195   373 1987
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   2821276
JRNL        DOI    10.1016/0022-2836(87)90658-9
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   P.L.ASHLEY,R.J.MACDONALD
REMARK   1  TITL   KALLIKREIN-RELATED M/RNAS OF THE RAT SUBMAXILLARY GLAND.
REMARK   1  TITL 2 NUCLEOTIDE SEQUENCES OF FOUR DISTINCT TYPES INCLUDING TONIN
REMARK   1  REF    BIOCHEMISTRY                  V.  24  4512 1985
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 2
REMARK   1  AUTH   C.LAZURE,R.LEDUC,N.G.SEIDAH,G.THIBAULT,J.GENEST,M.CHRETIEN
REMARK   1  TITL   AMINO ACID SEQUENCE OF RAT SUBMAXILLARY TONIN REVEALS
REMARK   1  TITL 2 SIMILARITIES TO SERINE PROTEASES
REMARK   1  REF    NATURE                        V. 307   555 1984
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1 REFERENCE 3
REMARK   1  AUTH   K.HAYAKAWA,J.A.KELLY,M.N.G.JAMES
REMARK   1  TITL   CRYSTAL DATA FOR TONIN, AN ENZYME INVOLVED IN THE FORMATION
REMARK   1  TITL 2 OF ANGIOTENSIN II
REMARK   1  REF    J.MOL.BIOL.                   V. 123   107 1978
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 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 + TEST SET) : 0.196
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  FIT/AGREEMENT OF MODEL WITH ALL DATA.
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            : 1734
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 149
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1TON 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) : 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   (%): 46.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.10000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       24.29000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       24.29000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      150.15000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       24.29000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       24.29000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       50.05000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       24.29000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       24.29000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      150.15000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       24.29000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       24.29000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       50.05000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      100.10000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
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 350   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      100.10000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     VAL A    95D
REMARK 465     THR A    95E
REMARK 465     ASN A    95F
REMARK 465     ASP A    95G
REMARK 465     THR A    95H
REMARK 465     GLU A    95I
REMARK 465     GLN A    95J
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     ILE A  95C   CA   C    O    CB   CG1  CG2  CD1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ARG A   86   CG   CD   NE   CZ   NH1  NH2
REMARK 480     PRO A   95K  CG   CD
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    PRO A  95K  CB    PRO A  95K  CG      0.293
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    ARG A  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ASP A  77   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG A  82   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ASP A  93   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    PRO A  95K  N   -  CA  -  CB  ANGL. DEV. =   8.8 DEGREES
REMARK 500    PRO A  95K  CA  -  CB  -  CG  ANGL. DEV. = -11.8 DEGREES
REMARK 500    GLU A 148   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES
REMARK 500    ASP A 178   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ASP A 189   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 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    ASN A  35     -133.82   -158.11
REMARK 500    ASP A 174     -115.30     40.88
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 A 352        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A 384        DISTANCE =  5.09 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE ZINC ION IS ALSO BONDED TO OE2 GLU 148 OF A
REMARK 600 SYMMETRY-RELATED MOLECULE.
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 A 247  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  97   NE2
REMARK 620 2 HIS A  57   NE2  99.1
REMARK 620 3 HIS A  99   NE2 100.5  99.1
REMARK 620 4 GLU A 148   OE2 143.8 101.2 105.5
REMARK 620 5 GLU A 148   OE1 101.2 153.0  94.5  52.4
REMARK 620 N                    1     2     3     4
REMARK 650
REMARK 650 HELIX
REMARK 650 THE SECONDARY STRUCTURE SPECIFICATIONS PRESENTED ON THE
REMARK 650 *HELIX* AND *TURN* RECORDS BELOW WERE EXTRACTED FROM THE
REMARK 650 PUBLICATION CITED ON THE *JRNL* RECORDS ABOVE.  THIS
REMARK 650 INFORMATION WAS GENERATED USING THE PROCEDURE DEFINED BY W.
REMARK 650 KABSCH AND C. SANDER (BIOPOLYMERS, V. 22, P. 2577, 1983).
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEETS *S1A* AND *S1B* FORM A SANDWICH.  SHEETS *S2A* AND
REMARK 700 *S2B* FORM A SANDWICH.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 247
DBREF  1TON A   16   246  UNP    P00759   KLK2_RAT        25    259
SEQRES   1 A  235  ILE VAL GLY GLY TYR LYS CYS GLU LYS ASN SER GLN PRO
SEQRES   2 A  235  TRP GLN VAL ALA VAL ILE ASN GLU TYR LEU CYS GLY GLY
SEQRES   3 A  235  VAL LEU ILE ASP PRO SER TRP VAL ILE THR ALA ALA HIS
SEQRES   4 A  235  CYS TYR SER ASN ASN TYR GLN VAL LEU LEU GLY ARG ASN
SEQRES   5 A  235  ASN LEU PHE LYS ASP GLU PRO PHE ALA GLN ARG ARG LEU
SEQRES   6 A  235  VAL ARG GLN SER PHE ARG HIS PRO ASP TYR ILE PRO LEU
SEQRES   7 A  235  ILE VAL THR ASN ASP THR GLU GLN PRO VAL HIS ASP HIS
SEQRES   8 A  235  SER ASN ASP LEU MET LEU LEU HIS LEU SER GLU PRO ALA
SEQRES   9 A  235  ASP ILE THR GLY GLY VAL LYS VAL ILE ASP LEU PRO THR
SEQRES  10 A  235  LYS GLU PRO LYS VAL GLY SER THR CYS LEU ALA SER GLY
SEQRES  11 A  235  TRP GLY SER THR ASN PRO SER GLU MET VAL VAL SER HIS
SEQRES  12 A  235  ASP LEU GLN CYS VAL ASN ILE HIS LEU LEU SER ASN GLU
SEQRES  13 A  235  LYS CYS ILE GLU THR TYR LYS ASP ASN VAL THR ASP VAL
SEQRES  14 A  235  MET LEU CYS ALA GLY GLU MET GLU GLY GLY LYS ASP THR
SEQRES  15 A  235  CYS ALA GLY ASP SER GLY GLY PRO LEU ILE CYS ASP GLY
SEQRES  16 A  235  VAL LEU GLN GLY ILE THR SER GLY GLY ALA THR PRO CYS
SEQRES  17 A  235  ALA LYS PRO LYS THR PRO ALA ILE TYR ALA LYS LEU ILE
SEQRES  18 A  235  LYS PHE THR SER TRP ILE LYS LYS VAL MET LYS GLU ASN
SEQRES  19 A  235  PRO
HET     ZN  A 247       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  HOH   *149(H2 O)
HELIX    1  H1 ALA A   56  CYS A   58  5                                   3
HELIX    2  H2 ASN A  165  TYR A  172  5INTERRUPTED AT CYS 168             8
HELIX    3  H3 VAL A  176  VAL A  179  5                                   4
HELIX    4  H4 LEU A  231  GLU A  244  13/10 FOR LEU 231-PHE 234          14
SHEET    1 S1A 3 VAL A  85  ARG A  90  0
SHEET    2 S1A 3 MET A 104  LEU A 108 -1
SHEET    3 S1A 3 TRP A  51  THR A  54 -1
SHEET    1 S1B 4 LEU A  41  ASP A  48  0
SHEET    2 S1B 4 GLN A  30  ILE A  34 -1
SHEET    3 S1B 4 GLN A  65  LEU A  68 -1
SHEET    4 S1B 4 GLN A  81  ARG A  83 -1
SHEET    1 S2A 2 TYR A  20  LYS A  21  0
SHEET    2 S2A 2 GLN A 156  LEU A 163 -1
SHEET    1 S2B 5 THR A 135  GLY A 140  0
SHEET    2 S2B 5 PRO A 198  CYS A 201 -1
SHEET    3 S2B 5 VAL A 208  THR A 213 -1
SHEET    4 S2B 5 ALA A 226  LYS A 230 -1
SHEET    5 S2B 5 MET A 180  GLY A 184 -1
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.01
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.01
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  2.02
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.02
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.00
LINK        ZN    ZN A 247                 NE2 HIS A  97     1555   1555  2.05
LINK        ZN    ZN A 247                 NE2 HIS A  57     1555   1555  2.04
LINK        ZN    ZN A 247                 NE2 HIS A  99     1555   1555  2.06
LINK        ZN    ZN A 247                 OE2 GLU A 148     1555   8555  2.07
LINK        ZN    ZN A 247                 OE1 GLU A 148     1555   8555  2.71
CISPEP   1 THR A  218    PRO A  219          0         3.15
SITE     1 AC1  4 HIS A  57  HIS A  97  HIS A  99  GLU A 148
CRYST1   48.580   48.580  200.200  90.00  90.00  90.00 P 43 21 2     8
ORIGX1      0.020585  0.000000  0.000000        0.00000
ORIGX2      0.000000  0.020585  0.000000        0.00000
ORIGX3      0.000000  0.000000  0.004995        0.00000
SCALE1      0.020585  0.000000  0.000000        0.00000
SCALE2      0.000000  0.020585  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004995        0.00000
      
PROCHECK
Go to PROCHECK summary
 References