spacer
spacer

PDBsum entry 3p7u

Go to PDB code: 
Top Page protein metals links
Hydrolase PDB id
3p7u
Jmol
Contents
Protein chain
316 a.a.
Metals
_ZN
_CA ×4
Waters ×307
HEADER    HYDROLASE                               12-OCT-10   3P7U
TITLE     RADIATION DAMAGE STUDY OF THERMOLYSIN - 160K STRUCTURE B (2.4 MGY)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOLYSIN;
COMPND   3 CHAIN: E;
COMPND   4 FRAGMENT: UNP RESIDUES 233-548;
COMPND   5 SYNONYM: THERMOSTABLE NEUTRAL PROTEINASE;
COMPND   6 EC: 3.4.24.27
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE   3 ORGANISM_TAXID: 1427
KEYWDS    ALPHA/BETA PROTEIN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.H.JUERS,M.WEIK
REVDAT   1   08-DEC-10 3P7U    0
JRNL        AUTH   D.H.JUERS,M.WEIK
JRNL        TITL   RADIATION DAMAGE STUDY OF THERMOLYSIN - 160K STRUCTURE B
JRNL        TITL 2 (2.4 MGY)
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.67
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 17552
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147
REMARK   3   R VALUE            (WORKING SET) : 0.145
REMARK   3   FREE R VALUE                     : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 888
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1191
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1420
REMARK   3   BIN FREE R VALUE SET COUNT          : 72
REMARK   3   BIN FREE R VALUE                    : 0.2700
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          : 5
REMARK   3   SOLVENT ATOMS            : 307
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.59
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.09000
REMARK   3    B22 (A**2) : -0.09000
REMARK   3    B33 (A**2) : 0.13000
REMARK   3    B12 (A**2) : -0.04000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.181
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.264
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2492 ; 0.016 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3394 ; 1.448 ; 1.924
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   315 ; 5.702 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;30.819 ;24.435
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   357 ;14.850 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;21.217 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   361 ; 0.101 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1978 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1156 ; 0.208 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1732 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   240 ; 0.180 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    18 ; 0.132 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    24 ; 0.171 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.275 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1585 ; 0.858 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2481 ; 1.474 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1060 ; 2.384 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   913 ; 3.445 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3P7U COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB062065.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-4
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17564
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.670
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.07600
REMARK 200  R SYM                      (I) : 0.07600
REMARK 200   FOR THE DATA SET  : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.11400
REMARK 200  R SYM FOR SHELL            (I) : 0.11400
REMARK 200   FOR SHELL         : 6.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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   (%): 48.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% DMSO, PH 5.0, VAPOR DIFFUSION,
REMARK 280  TEMPERATURE 298K
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       42.94667
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       85.89333
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       64.42000
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      107.36667
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       21.47333
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       42.94667
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       85.89333
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      107.36667
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       64.42000
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       21.47333
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH E 508  LIES ON A SPECIAL POSITION.
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   OE2  GLU E   187     O    HOH E   507              2.08
REMARK 500   O    HOH E   604     O    HOH E   625              2.11
REMARK 500   NH1  ARG E   260     O    HOH E   569              2.12
REMARK 500   O    HOH E   603     O    HOH E   624              2.14
REMARK 500   NE2  GLN E   308     O    HOH E   576              2.17
REMARK 500   O    HOH E   331     O    HOH E   593              2.18
REMARK 500   O    HOH E   431     O    HOH E   521              2.19
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 E   446     O    HOH E   446    10664     1.68
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 E  11   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG E  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 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    THR E  26      -55.59     71.70
REMARK 500    SER E  92     -175.32     62.82
REMARK 500    SER E 107     -161.29     59.51
REMARK 500    ASN E 111       49.54    -88.23
REMARK 500    THR E 152      -99.75   -119.93
REMARK 500    ASN E 159     -139.21     51.02
REMARK 500    THR E 194       74.00     46.39
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                              ZN E 321  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 361   O
REMARK 620 2 GLU E 166   OE2 100.5
REMARK 620 3 HIS E 142   NE2 108.9 133.2
REMARK 620 4 HIS E 146   NE2 108.9  94.9 108.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 318  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 393   O
REMARK 620 2 ASN E 183   O    90.1
REMARK 620 3 HOH E 341   O    83.5  87.5
REMARK 620 4 GLU E 190   OE2  95.1 166.6 105.3
REMARK 620 5 GLU E 177   OE2 173.4  92.2  90.4  84.0
REMARK 620 6 ASP E 185   OD2  98.1  93.0 178.3  74.1  87.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 317  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 187   O
REMARK 620 2 ASP E 138   OD2  88.9
REMARK 620 3 ASP E 185   OD1  78.8 164.1
REMARK 620 4 HOH E 334   O    76.5  97.5  89.4
REMARK 620 5 GLU E 190   OE2 124.7  94.8  84.3 155.7
REMARK 620 6 GLU E 177   OE1 148.3  73.2 122.2  80.1  83.5
REMARK 620 7 GLU E 190   OE1  75.3  83.9  83.4 151.7  50.6 126.6
REMARK 620 8 GLU E 177   OE2 142.2 121.4  74.1  77.4  78.3  48.2 125.9
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 319  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E  61   O
REMARK 620 2 ASP E  57   OD1  93.4
REMARK 620 3 HOH E 409   O   170.4  82.5
REMARK 620 4 HOH E 399   O    98.0 159.0  88.7
REMARK 620 5 ASP E  59   OD1  88.4 121.5  86.4  76.6
REMARK 620 6 HOH E 376   O    85.4  84.2 102.7  79.2 153.9
REMARK 620 7 ASP E  57   OD2  88.1  52.9  82.5 144.6  68.7 136.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 320  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE E 197   O
REMARK 620 2 HOH E 397   O    88.0
REMARK 620 3 THR E 194   OG1 106.5 144.0
REMARK 620 4 ASP E 200   OD1  76.6 142.2  73.8
REMARK 620 5 TYR E 193   O   163.4  81.2  76.2 119.4
REMARK 620 6 HOH E 342   O   108.6  74.0 128.0  78.6  80.6
REMARK 620 7 THR E 194   O    87.4  81.7  66.7 130.7  78.6 150.0
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 321
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P7P   RELATED DB: PDB
REMARK 900 RELATED ID: 3P7Q   RELATED DB: PDB
REMARK 900 RELATED ID: 3P7R   RELATED DB: PDB
REMARK 900 RELATED ID: 3P7S   RELATED DB: PDB
REMARK 900 RELATED ID: 3P7T   RELATED DB: PDB
REMARK 900 RELATED ID: 3P7V   RELATED DB: PDB
REMARK 900 RELATED ID: 3P7W   RELATED DB: PDB
DBREF  3P7U E    1   316  UNP    P00800   THER_BACTH     233    548
SEQADV 3P7U ASP E   37  UNP  P00800    ASN   269 VARIANT
SEQADV 3P7U GLU E  119  UNP  P00800    GLN   351 VARIANT
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     CA  E 317       1
HET     CA  E 318       1
HET     CA  E 319       1
HET     CA  E 320       1
HET     ZN  E 321       1
HETNAM      CA CALCIUM ION
HETNAM      ZN ZINC ION
FORMUL   2   CA    4(CA 2+)
FORMUL   6   ZN    ZN 2+
FORMUL   7  HOH   *307(H2 O)
HELIX    1   1 ALA E   64  TYR E   66  5                                   3
HELIX    2   2 ASP E   67  ASN E   89  1                                  23
HELIX    3   3 PRO E  132  GLY E  135  5                                   4
HELIX    4   4 GLY E  136  TYR E  151  1                                  16
HELIX    5   5 GLN E  158  ASN E  181  1                                  24
HELIX    6   6 ASP E  207  GLY E  212  5                                   6
HELIX    7   7 HIS E  216  ARG E  220  5                                   5
HELIX    8   8 THR E  224  GLY E  247  1                                  24
HELIX    9   9 GLY E  259  TYR E  274  1                                  16
HELIX   10  10 ASN E  280  GLY E  297  1                                  18
HELIX   11  11 SER E  300  VAL E  313  1                                  14
SHEET    1   A 5 ALA E  56  ASP E  57  0
SHEET    2   A 5 TYR E  28  TYR E  29 -1  N  TYR E  28   O  ASP E  57
SHEET    3   A 5 GLN E  17  TYR E  24 -1  N  THR E  23   O  TYR E  29
SHEET    4   A 5 THR E   4  ARG E  11 -1  N  GLY E   8   O  ILE E  20
SHEET    5   A 5 GLN E  61  PHE E  62  1  O  PHE E  62   N  VAL E   9
SHEET    1   B 3 GLN E  31  ASP E  32  0
SHEET    2   B 3 ILE E  39  ASP E  43 -1  O  ILE E  39   N  ASP E  32
SHEET    3   B 3 SER E  53  LEU E  54 -1  O  SER E  53   N  ASP E  43
SHEET    1   C 5 GLN E  31  ASP E  32  0
SHEET    2   C 5 ILE E  39  ASP E  43 -1  O  ILE E  39   N  ASP E  32
SHEET    3   C 5 ILE E 100  TYR E 106  1  O  ILE E 100   N  PHE E  40
SHEET    4   C 5 MET E 120  GLY E 123  1  O  MET E 120   N  ARG E 101
SHEET    5   C 5 ALA E 113  TRP E 115 -1  N  PHE E 114   O  VAL E 121
SHEET    1   D 2 GLU E 187  ILE E 188  0
SHEET    2   D 2 ARG E 203  SER E 204 -1  O  ARG E 203   N  ILE E 188
SHEET    1   E 2 GLY E 248  HIS E 250  0
SHEET    2   E 2 VAL E 253  VAL E 255 -1  O  VAL E 255   N  GLY E 248
LINK        ZN    ZN E 321                 O   HOH E 361     1555   1555  1.75
LINK         OE2 GLU E 166                ZN    ZN E 321     1555   1555  1.93
LINK         NE2 HIS E 142                ZN    ZN E 321     1555   1555  2.01
LINK         NE2 HIS E 146                ZN    ZN E 321     1555   1555  2.05
LINK        CA    CA E 318                 O   HOH E 393     1555   1555  2.07
LINK         O   GLU E 187                CA    CA E 317     1555   1555  2.23
LINK         O   GLN E  61                CA    CA E 319     1555   1555  2.28
LINK         O   ASN E 183                CA    CA E 318     1555   1555  2.32
LINK        CA    CA E 318                 O   HOH E 341     1555   1555  2.33
LINK         O   ILE E 197                CA    CA E 320     1555   1555  2.33
LINK        CA    CA E 320                 O   HOH E 397     1555   1555  2.34
LINK         OD1 ASP E  57                CA    CA E 319     1555   1555  2.34
LINK         OG1 THR E 194                CA    CA E 320     1555   1555  2.35
LINK         OD1 ASP E 200                CA    CA E 320     1555   1555  2.36
LINK        CA    CA E 319                 O   HOH E 409     1555   1555  2.39
LINK         OD2 ASP E 138                CA    CA E 317     1555   1555  2.40
LINK         O   TYR E 193                CA    CA E 320     1555   1555  2.40
LINK        CA    CA E 320                 O   HOH E 342     1555   1555  2.40
LINK         OD1 ASP E 185                CA    CA E 317     1555   1555  2.43
LINK        CA    CA E 319                 O   HOH E 399     1555   1555  2.43
LINK        CA    CA E 317                 O   HOH E 334     1555   1555  2.44
LINK         OD1 ASP E  59                CA    CA E 319     1555   1555  2.44
LINK         OE2 GLU E 190                CA    CA E 318     1555   1555  2.44
LINK        CA    CA E 319                 O   HOH E 376     1555   1555  2.45
LINK         OE2 GLU E 190                CA    CA E 317     1555   1555  2.46
LINK         O   THR E 194                CA    CA E 320     1555   1555  2.51
LINK         OE1 GLU E 177                CA    CA E 317     1555   1555  2.54
LINK         OE2 GLU E 177                CA    CA E 318     1555   1555  2.54
LINK         OD2 ASP E 185                CA    CA E 318     1555   1555  2.56
LINK         OD2 ASP E  57                CA    CA E 319     1555   1555  2.58
LINK         OE1 GLU E 190                CA    CA E 317     1555   1555  2.66
LINK         OE2 GLU E 177                CA    CA E 317     1555   1555  2.81
CISPEP   1 LEU E   50    PRO E   51          0        -1.51
SITE     1 AC1  6 ASP E 138  GLU E 177  ASP E 185  GLU E 187
SITE     2 AC1  6 GLU E 190  HOH E 334
SITE     1 AC2  6 GLU E 177  ASN E 183  ASP E 185  GLU E 190
SITE     2 AC2  6 HOH E 341  HOH E 393
SITE     1 AC3  6 ASP E  57  ASP E  59  GLN E  61  HOH E 376
SITE     2 AC3  6 HOH E 399  HOH E 409
SITE     1 AC4  6 TYR E 193  THR E 194  ILE E 197  ASP E 200
SITE     2 AC4  6 HOH E 342  HOH E 397
SITE     1 AC5  4 HIS E 142  HIS E 146  GLU E 166  HOH E 361
CRYST1   93.750   93.750  128.840  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      0.010667  0.006158  0.000000        0.00000
SCALE2      0.000000  0.012317  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007762        0.00000
      
PROCHECK
Go to PROCHECK summary
 References