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HEADER HYDROLASE 06-SEP-13 3WI7
TITLE CRYSTAL STRUCTURE OF THE NOVEL HALOALKANE DEHALOGENASE DATA FROM
TITLE 2 AGROBACTERIUM TUMEFACIENS C58
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM TUMEFACIENS;
SOURCE 3 ORGANISM_TAXID: 176299;
SOURCE 4 STRAIN: C58 / ATCC 33970;
SOURCE 5 GENE: DHAA, DHA, ATU6064, AGR_PTI_130;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3)
KEYWDS HALOALKANE DEHALOGENASE, HYDROLASE FOLD FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.GUAN,H.YABUKI,M.OKAI,J.OHTSUKA,M.TANOKURA
REVDAT 1 23-JUL-14 3WI7 0
JRNL AUTH L.GUAN,H.YABUKI,M.OKAI,J.OHTSUKA,M.TANOKURA
JRNL TITL CRYSTAL STRUCTURE OF THE NOVEL HALOALKANE DEHALOGENASE DATA
JRNL TITL 2 FROM AGROBACTERIUM TUMEFACIENS C58 REVEALS A SPECIAL
JRNL TITL 3 HALIDE-STABILIZING PAIR AND ENANTIOSELECTIVITY MECHANISM.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2014
JRNL REFN ESSN 1432-0614
JRNL PMID 24770384
JRNL DOI 10.1007/S00253-014-5751-2
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 71353
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3783
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5097
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 267
REMARK 3 BIN FREE R VALUE : 0.2950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4664
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 302
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.00000
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): 0.104
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.069
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4851 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4580 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6615 ; 1.970 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10494 ; 0.937 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 580 ; 6.307 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;34.965 ;23.167
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 730 ;12.785 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;18.371 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 720 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5499 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1205 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2326 ; 2.254 ; 2.300
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2325 ; 2.253 ; 2.299
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2904 ; 2.934 ; 3.443
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2905 ; 2.934 ; 3.444
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2525 ; 2.945 ; 2.574
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2525 ; 2.945 ; 2.574
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3712 ; 4.331 ; 3.760
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5631 ; 5.552 ;19.191
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5632 ; 5.552 ;19.197
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 3WI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB096366.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75138
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
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 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 (%): 49.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CHES, 1.0M POTASSIUM SODIUM
REMARK 280 TARTRATE, 0.2M LITHIUM SULFATE, 0.01M BARIUM CHLORIDE, PH 8.6,
REMARK 280 EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
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 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 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 MET A -5
REMARK 465 LYS A -4
REMARK 465 GLU A -3
REMARK 465 HIS A -2
REMARK 465 ARG A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 SER A 5
REMARK 465 GLY A 297
REMARK 465 ASN A 298
REMARK 465 MET B -5
REMARK 465 LYS B -4
REMARK 465 GLU B -3
REMARK 465 HIS B -2
REMARK 465 ARG B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 GLU B 3
REMARK 465 LYS B 4
REMARK 465 SER B 5
REMARK 465 GLY B 297
REMARK 465 ASN B 298
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 A 18 CB - CG - OD1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASP A 18 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 120 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 136 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP B 67 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 189 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 262 NE - CZ - NH2 ANGL. DEV. = -4.0 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 PRO A 44 56.34 -110.50
REMARK 500 THR A 45 -153.87 -107.60
REMARK 500 ASP A 98 62.75 33.21
REMARK 500 ASP A 108 -134.37 52.86
REMARK 500 GLU A 132 56.22 39.40
REMARK 500 LEU A 135 -37.24 -130.50
REMARK 500 GLU A 173 -61.10 -123.63
REMARK 500 PHE A 178 35.91 -93.54
REMARK 500 PHE A 247 -73.02 -151.10
REMARK 500 ILE A 273 -73.35 -106.77
REMARK 500 HIS A 274 -52.63 -136.61
REMARK 500 PRO B 44 53.98 -104.43
REMARK 500 THR B 45 -154.19 -104.90
REMARK 500 ASP B 108 -136.27 54.40
REMARK 500 LEU B 135 -37.60 -136.84
REMARK 500 GLU B 173 -63.79 -121.48
REMARK 500 PHE B 247 -75.11 -152.43
REMARK 500 ILE B 273 -78.18 -107.33
REMARK 500 HIS B 274 -53.47 -135.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WIB RELATED DB: PDB
DBREF 3WI7 A -5 298 UNP Q8U671 DHAA_AGRT5 1 304
DBREF 3WI7 B -5 298 UNP Q8U671 DHAA_AGRT5 1 304
SEQRES 1 A 304 MET LYS GLU HIS ARG HIS MET THR GLU LYS SER PRO HIS
SEQRES 2 A 304 SER ALA PHE GLY ASP GLY ALA LYS ALA TYR ASP VAL PRO
SEQRES 3 A 304 ALA PHE GLY LEU GLN ILE HIS THR VAL GLU HIS GLY SER
SEQRES 4 A 304 GLY ALA PRO ILE VAL PHE LEU HIS GLY ASN PRO THR SER
SEQRES 5 A 304 SER TYR LEU TRP ARG HIS ILE PHE ARG ARG LEU HIS GLY
SEQRES 6 A 304 HIS GLY ARG LEU LEU ALA VAL ASP LEU ILE GLY TYR GLY
SEQRES 7 A 304 GLN SER SER LYS PRO ASP ILE GLU TYR THR LEU GLU ASN
SEQRES 8 A 304 GLN GLN ARG TYR VAL ASP ALA TRP PHE ASP ALA LEU ASP
SEQRES 9 A 304 LEU ARG ASN VAL THR LEU VAL LEU GLN ASP TYR GLY ALA
SEQRES 10 A 304 ALA PHE GLY LEU ASN TRP ALA SER ARG ASN PRO ASP ARG
SEQRES 11 A 304 VAL ARG ALA VAL ALA PHE PHE GLU PRO VAL LEU ARG ASN
SEQRES 12 A 304 ILE ASP SER VAL ASP LEU SER PRO GLU PHE VAL THR ARG
SEQRES 13 A 304 ARG ALA LYS LEU ARG GLN PRO GLY GLU GLY GLU ILE PHE
SEQRES 14 A 304 VAL GLN GLN GLU ASN ARG PHE LEU THR GLU LEU PHE PRO
SEQRES 15 A 304 TRP PHE PHE LEU THR PRO LEU ALA PRO GLU ASP LEU ARG
SEQRES 16 A 304 GLN TYR GLN THR PRO PHE PRO THR PRO HIS SER ARG LYS
SEQRES 17 A 304 ALA ILE LEU ALA GLY PRO ARG ASN LEU PRO VAL ASP GLY
SEQRES 18 A 304 GLU PRO ALA SER THR VAL ALA PHE LEU GLU GLN ALA VAL
SEQRES 19 A 304 ASN TRP LEU ASN THR SER ASP THR PRO LYS LEU LEU LEU
SEQRES 20 A 304 THR PHE LYS PRO GLY PHE LEU LEU THR ASP ALA ILE LEU
SEQRES 21 A 304 LYS TRP SER GLN VAL THR ILE ARG ASN LEU GLU ILE GLU
SEQRES 22 A 304 ALA ALA GLY ALA GLY ILE HIS PHE VAL GLN GLU GLU GLN
SEQRES 23 A 304 PRO GLU THR ILE ALA ARG LEU LEU ASP ALA TRP LEU THR
SEQRES 24 A 304 ARG ILE ALA GLY ASN
SEQRES 1 B 304 MET LYS GLU HIS ARG HIS MET THR GLU LYS SER PRO HIS
SEQRES 2 B 304 SER ALA PHE GLY ASP GLY ALA LYS ALA TYR ASP VAL PRO
SEQRES 3 B 304 ALA PHE GLY LEU GLN ILE HIS THR VAL GLU HIS GLY SER
SEQRES 4 B 304 GLY ALA PRO ILE VAL PHE LEU HIS GLY ASN PRO THR SER
SEQRES 5 B 304 SER TYR LEU TRP ARG HIS ILE PHE ARG ARG LEU HIS GLY
SEQRES 6 B 304 HIS GLY ARG LEU LEU ALA VAL ASP LEU ILE GLY TYR GLY
SEQRES 7 B 304 GLN SER SER LYS PRO ASP ILE GLU TYR THR LEU GLU ASN
SEQRES 8 B 304 GLN GLN ARG TYR VAL ASP ALA TRP PHE ASP ALA LEU ASP
SEQRES 9 B 304 LEU ARG ASN VAL THR LEU VAL LEU GLN ASP TYR GLY ALA
SEQRES 10 B 304 ALA PHE GLY LEU ASN TRP ALA SER ARG ASN PRO ASP ARG
SEQRES 11 B 304 VAL ARG ALA VAL ALA PHE PHE GLU PRO VAL LEU ARG ASN
SEQRES 12 B 304 ILE ASP SER VAL ASP LEU SER PRO GLU PHE VAL THR ARG
SEQRES 13 B 304 ARG ALA LYS LEU ARG GLN PRO GLY GLU GLY GLU ILE PHE
SEQRES 14 B 304 VAL GLN GLN GLU ASN ARG PHE LEU THR GLU LEU PHE PRO
SEQRES 15 B 304 TRP PHE PHE LEU THR PRO LEU ALA PRO GLU ASP LEU ARG
SEQRES 16 B 304 GLN TYR GLN THR PRO PHE PRO THR PRO HIS SER ARG LYS
SEQRES 17 B 304 ALA ILE LEU ALA GLY PRO ARG ASN LEU PRO VAL ASP GLY
SEQRES 18 B 304 GLU PRO ALA SER THR VAL ALA PHE LEU GLU GLN ALA VAL
SEQRES 19 B 304 ASN TRP LEU ASN THR SER ASP THR PRO LYS LEU LEU LEU
SEQRES 20 B 304 THR PHE LYS PRO GLY PHE LEU LEU THR ASP ALA ILE LEU
SEQRES 21 B 304 LYS TRP SER GLN VAL THR ILE ARG ASN LEU GLU ILE GLU
SEQRES 22 B 304 ALA ALA GLY ALA GLY ILE HIS PHE VAL GLN GLU GLU GLN
SEQRES 23 B 304 PRO GLU THR ILE ALA ARG LEU LEU ASP ALA TRP LEU THR
SEQRES 24 B 304 ARG ILE ALA GLY ASN
HET NHE A 301 13
HET NHE A 302 13
HET GOL A 303 6
HET NHE B 301 13
HET GOL B 302 6
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN NHE N-CYCLOHEXYLTAURINE; CHES
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NHE 3(C8 H17 N O3 S)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 8 HOH *302(H2 O)
HELIX 1 1 HIS A 7 GLY A 11 5 5
HELIX 2 2 SER A 46 LEU A 49 5 4
HELIX 3 3 TRP A 50 LEU A 57 1 8
HELIX 4 4 THR A 82 ASP A 98 1 17
HELIX 5 5 TYR A 109 ASN A 121 1 13
HELIX 6 6 ASP A 139 LEU A 143 5 5
HELIX 7 7 SER A 144 ARG A 155 1 12
HELIX 8 8 GLY A 158 GLN A 165 1 8
HELIX 9 9 ASN A 168 GLU A 173 1 6
HELIX 10 10 GLU A 173 PHE A 178 1 6
HELIX 11 11 ALA A 184 THR A 193 1 10
HELIX 12 12 PRO A 198 SER A 200 5 3
HELIX 13 13 ARG A 201 LEU A 211 1 11
HELIX 14 14 PRO A 217 GLN A 226 1 10
HELIX 15 15 ALA A 227 SER A 234 1 8
HELIX 16 16 THR A 250 ILE A 261 1 12
HELIX 17 17 PHE A 275 GLN A 280 1 6
HELIX 18 18 GLN A 280 ALA A 296 1 17
HELIX 19 19 HIS B 7 GLY B 11 5 5
HELIX 20 20 SER B 46 LEU B 49 5 4
HELIX 21 21 TRP B 50 LEU B 57 1 8
HELIX 22 22 THR B 82 LEU B 97 1 16
HELIX 23 23 TYR B 109 ASN B 121 1 13
HELIX 24 24 ASP B 139 LEU B 143 5 5
HELIX 25 25 SER B 144 ARG B 155 1 12
HELIX 26 26 GLY B 158 GLN B 165 1 8
HELIX 27 27 ASN B 168 GLU B 173 1 6
HELIX 28 28 GLU B 173 PHE B 178 1 6
HELIX 29 29 ALA B 184 THR B 193 1 10
HELIX 30 30 PRO B 198 SER B 200 5 3
HELIX 31 31 ARG B 201 LEU B 211 1 11
HELIX 32 32 PRO B 217 GLN B 226 1 10
HELIX 33 33 ALA B 227 SER B 234 1 8
HELIX 34 34 THR B 250 ILE B 261 1 12
HELIX 35 35 PHE B 275 GLN B 280 1 6
HELIX 36 36 GLN B 280 ALA B 296 1 17
SHEET 1 A 8 LYS A 15 ALA A 21 0
SHEET 2 A 8 LEU A 24 HIS A 31 -1 O GLU A 30 N LYS A 15
SHEET 3 A 8 ARG A 62 VAL A 66 -1 O LEU A 63 N HIS A 31
SHEET 4 A 8 PRO A 36 LEU A 40 1 N PHE A 39 O LEU A 64
SHEET 5 A 8 VAL A 102 ASP A 108 1 O THR A 103 N PRO A 36
SHEET 6 A 8 VAL A 125 PRO A 133 1 O ALA A 129 N LEU A 104
SHEET 7 A 8 LYS A 238 PRO A 245 1 O LEU A 239 N PHE A 130
SHEET 8 A 8 LEU A 264 GLY A 272 1 O ALA A 269 N THR A 242
SHEET 1 B 8 LYS B 15 ALA B 21 0
SHEET 2 B 8 LEU B 24 HIS B 31 -1 O GLU B 30 N LYS B 15
SHEET 3 B 8 ARG B 62 VAL B 66 -1 O ALA B 65 N VAL B 29
SHEET 4 B 8 PRO B 36 LEU B 40 1 N ILE B 37 O LEU B 64
SHEET 5 B 8 VAL B 102 ASP B 108 1 O THR B 103 N VAL B 38
SHEET 6 B 8 VAL B 125 PRO B 133 1 O ARG B 126 N VAL B 102
SHEET 7 B 8 LYS B 238 PRO B 245 1 O LEU B 239 N PHE B 130
SHEET 8 B 8 LEU B 264 GLY B 272 1 O ALA B 269 N THR B 242
CISPEP 1 ASN A 43 PRO A 44 0 -5.91
CISPEP 2 GLU A 216 PRO A 217 0 -4.05
CISPEP 3 LYS A 244 PRO A 245 0 1.38
CISPEP 4 ASN B 43 PRO B 44 0 -8.29
CISPEP 5 GLU B 216 PRO B 217 0 -3.32
CISPEP 6 LYS B 244 PRO B 245 0 3.08
SITE 1 AC1 9 ASN A 43 ASP A 108 TYR A 109 PHE A 147
SITE 2 AC1 9 PHE A 170 GLY A 207 PRO A 208 PHE A 247
SITE 3 AC1 9 HIS A 274
SITE 1 AC2 10 PRO A 176 TRP A 177 PHE A 179 PRO A 182
SITE 2 AC2 10 ILE A 273 HOH A 449 HOH A 482 HOH A 523
SITE 3 AC2 10 SER B 144 PHE B 179
SITE 1 AC3 5 GLU A 80 TYR A 81 THR A 82 ASN A 210
SITE 2 AC3 5 HOH A 502
SITE 1 AC4 8 ASN B 43 ASP B 108 TYR B 109 PHE B 147
SITE 2 AC4 8 PHE B 170 GLY B 207 PRO B 208 HIS B 274
SITE 1 AC5 7 GLU B 80 TYR B 81 THR B 82 ARG B 209
SITE 2 AC5 7 ASN B 210 HOH B 485 HOH B 500
CRYST1 123.700 123.700 88.070 90.00 90.00 90.00 P 4 2 2 16
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 0.008084 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008084 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011355 0.00000
TER 2333 ALA A 296
TER 4666 ALA B 296
MASTER 379 0 5 36 16 0 12 6 5017 2 51 48
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