HEADER LYASE 07-APR-09 3GZH
TITLE CRYSTAL STRUCTURE OF PHOSPHATE-BOUND ADENYLOSUCCINATE LYASE FROM E.
TITLE 2 COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLOSUCCINATE LYASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.3.2.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83334;
SOURCE 4 STRAIN: O157:H7;
SOURCE 5 GENE: ECS1603, PURB, Z1860;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ALL-HELICAL FOLD, ADENYLOSUCCINATE LYASE, STRUCTURAL GENOMICS,
KEYWDS 2 BACTERIAL STRUCTURAL GENOMICS INITIATIVE, MONTREAL-KINGSTON
KEYWDS 3 BACTERIAL STRUCTURAL GENOMICS INITIATIVE, BSGI, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KOZLOV,K.GEHRING,MONTREAL-KINGSTON BACTERIAL STRUCTURAL GENOMICS
AUTHOR 2 INITIATIVE (BSGI)
REVDAT 3 13-JUL-11 3GZH 1 VERSN
REVDAT 2 15-SEP-09 3GZH 1 JRNL
REVDAT 1 25-AUG-09 3GZH 0
JRNL AUTH G.KOZLOV,L.NGUYEN,J.PEARSALL,K.GEHRING
JRNL TITL THE STRUCTURE OF PHOSPHATE-BOUND ESCHERICHIA COLI
JRNL TITL 2 ADENYLOSUCCINATE LYASE IDENTIFIES HIS171 AS A CATALYTIC
JRNL TITL 3 ACID.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 65 857 2009
JRNL REFN ESSN 1744-3091
JRNL PMID 19724117
JRNL DOI 10.1107/S1744309109029674
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 40348
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2150
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2666
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3723
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.26000
REMARK 3 B22 (A**2) : 3.22000
REMARK 3 B33 (A**2) : -0.96000
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): 0.139
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.783
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3839 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5221 ; 1.470 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 478 ; 5.685 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;34.922 ;24.231
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 657 ;14.379 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;14.356 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 584 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2918 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1813 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2687 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 249 ; 0.143 ; 0.200
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): 182 ; 0.176 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 64 ; 0.175 ; 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): 2351 ; 0.792 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3795 ; 1.480 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1543 ; 2.702 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1421 ; 4.341 ; 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: NULL
REMARK 4
REMARK 4 3GZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40348
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2PTS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM/POTASSIUM PHOSPHATE, 4%
REMARK 280 GLYCEROL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.65800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.12800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 75.05200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.65800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.12800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.05200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.65800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.12800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.05200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.65800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.12800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 75.05200
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 35860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.6 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -100.25600
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 -100.25600
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 78530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.4 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 -1.000000 0.000000 0.000000 77.31600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -100.25600
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 77.31600
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 -100.25600
REMARK 350 BIOMT3 4 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 A 914 LIES ON A SPECIAL POSITION.
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 -25
REMARK 465 GLY A -24
REMARK 465 SER A -23
REMARK 465 SER A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 ASP A -13
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 ASP A -11 CG OD1 OD2
REMARK 470 SER A 1 OG
REMARK 470 GLU A 2 CG CD OE1 OE2
REMARK 470 ASN A 73 OD1
REMARK 470 GLU A 223 CG CD OE1 OE2
REMARK 470 ARG A 413 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 456 CG CD CE NZ
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 ALA A 120 -5.58 67.33
REMARK 500 VAL A 142 -61.98 -120.03
REMARK 500 SER A 178 -159.09 -134.31
REMARK 500 ASN A 208 15.50 -166.64
REMARK 500 THR A 246 -141.46 -89.37
REMARK 500 TRP A 333 -132.21 50.68
REMARK 500 ARG A 335 157.36 155.65
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 712 DISTANCE = 5.25 ANGSTROMS
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 NA A 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 47 O
REMARK 620 2 ALA A 48 O 77.0
REMARK 620 3 HIS A 50 O 82.9 103.5
REMARK 620 4 ILE A 53 O 99.2 163.0 92.3
REMARK 620 5 VAL A 56 O 93.4 83.5 171.1 80.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 331 O
REMARK 620 2 TRP A 333 O 82.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PURB_ECO57 RELATED DB: TARGETDB
DBREF 3GZH A 2 456 UNP Q8X737 Q8X737_ECO57 2 456
SEQADV 3GZH MET A -25 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH GLY A -24 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH SER A -23 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH SER A -22 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH HIS A -21 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH HIS A -20 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH HIS A -19 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH HIS A -18 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH HIS A -17 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH HIS A -16 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH HIS A -15 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH HIS A -14 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH ASP A -13 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH TYR A -12 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH ASP A -11 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH ILE A -10 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH PRO A -9 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH THR A -8 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH THR A -7 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH GLU A -6 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH ASN A -5 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH LEU A -4 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH TYR A -3 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH PHE A -2 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH GLN A -1 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH GLY A 0 UNP Q8X737 EXPRESSION TAG
SEQADV 3GZH SER A 1 UNP Q8X737 EXPRESSION TAG
SEQRES 1 A 482 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS HIS ASP
SEQRES 2 A 482 TYR ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY
SEQRES 3 A 482 SER GLU LEU SER SER LEU THR ALA VAL SER PRO VAL ASP
SEQRES 4 A 482 GLY ARG TYR GLY ASP LYS VAL SER ALA LEU ARG GLY ILE
SEQRES 5 A 482 PHE SER GLU TYR GLY LEU LEU LYS PHE ARG VAL GLN VAL
SEQRES 6 A 482 GLU VAL ARG TRP LEU GLN LYS LEU ALA ALA HIS ALA ALA
SEQRES 7 A 482 ILE LYS GLU VAL PRO ALA PHE ALA ALA ASP ALA ILE GLY
SEQRES 8 A 482 TYR LEU ASP ALA ILE VAL ALA ASN PHE SER GLU GLU ASP
SEQRES 9 A 482 ALA ALA ARG ILE LYS THR ILE GLU ARG THR THR ASN HIS
SEQRES 10 A 482 ASP VAL LYS ALA VAL GLU TYR PHE LEU LYS GLU LYS VAL
SEQRES 11 A 482 ALA GLU ILE PRO GLU LEU HIS ALA VAL SER GLU PHE ILE
SEQRES 12 A 482 HIS PHE ALA CYS THR SER GLU ASP ILE ASN ASN LEU SER
SEQRES 13 A 482 HIS ALA LEU MET LEU LYS THR ALA ARG ASP GLU VAL ILE
SEQRES 14 A 482 LEU PRO TYR TRP ARG GLN LEU ILE ASP GLY ILE LYS ASP
SEQRES 15 A 482 LEU ALA VAL GLN TYR ARG ASP ILE PRO LEU LEU SER ARG
SEQRES 16 A 482 THR HIS GLY GLN PRO ALA THR PRO SER THR ILE GLY LYS
SEQRES 17 A 482 GLU MET ALA ASN VAL ALA TYR ARG MET GLU ARG GLN TYR
SEQRES 18 A 482 ARG GLN LEU ASN GLN VAL GLU ILE LEU GLY LYS ILE ASN
SEQRES 19 A 482 GLY ALA VAL GLY ASN TYR ASN ALA HIS ILE ALA ALA TYR
SEQRES 20 A 482 PRO GLU VAL ASP TRP HIS GLN PHE SER GLU GLU PHE VAL
SEQRES 21 A 482 THR SER LEU GLY ILE GLN TRP ASN PRO TYR THR THR GLN
SEQRES 22 A 482 ILE GLU PRO HIS ASP TYR ILE ALA GLU LEU PHE ASP CYS
SEQRES 23 A 482 VAL ALA ARG PHE ASN THR ILE LEU ILE ASP PHE ASP ARG
SEQRES 24 A 482 ASP VAL TRP GLY TYR ILE ALA LEU ASN HIS PHE LYS GLN
SEQRES 25 A 482 LYS THR ILE ALA GLY GLU ILE GLY SER SER THR MET PRO
SEQRES 26 A 482 HIS LYS VAL ASN PRO ILE ASP PHE GLU ASN SER GLU GLY
SEQRES 27 A 482 ASN LEU GLY LEU SER ASN ALA VAL LEU GLN HIS LEU ALA
SEQRES 28 A 482 SER LYS LEU PRO VAL SER ARG TRP GLN ARG ASP LEU THR
SEQRES 29 A 482 ASP SER THR VAL LEU ARG ASN LEU GLY VAL GLY ILE GLY
SEQRES 30 A 482 TYR ALA LEU ILE ALA TYR GLN SER THR LEU LYS GLY VAL
SEQRES 31 A 482 SER LYS LEU GLU VAL ASN ARG ASP HIS LEU LEU ASP GLU
SEQRES 32 A 482 LEU ASP HIS ASN TRP GLU VAL LEU ALA GLU PRO ILE GLN
SEQRES 33 A 482 THR VAL MET ARG ARG TYR GLY ILE GLU LYS PRO TYR GLU
SEQRES 34 A 482 LYS LEU LYS GLU LEU THR ARG GLY LYS ARG VAL ASP ALA
SEQRES 35 A 482 GLU GLY MET LYS GLN PHE ILE ASP GLY LEU ALA LEU PRO
SEQRES 36 A 482 GLU GLU GLU LYS ALA ARG LEU LYS ALA MET THR PRO ALA
SEQRES 37 A 482 ASN TYR ILE GLY ARG ALA ILE THR MET VAL ASP GLU LEU
SEQRES 38 A 482 LYS
HET NA A 501 1
HET NA A 502 1
HET PO4 A 503 5
HET PO4 A 504 5
HETNAM NA SODIUM ION
HETNAM PO4 PHOSPHATE ION
FORMUL 2 NA 2(NA 1+)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 6 HOH *317(H2 O)
HELIX 1 1 TYR A 16 ILE A 26 5 11
HELIX 2 2 SER A 28 HIS A 50 1 23
HELIX 3 3 ALA A 60 ASN A 73 1 14
HELIX 4 4 SER A 75 ASN A 90 1 16
HELIX 5 5 HIS A 91 ALA A 105 1 15
HELIX 6 6 ILE A 107 ALA A 112 1 6
HELIX 7 7 VAL A 113 ILE A 117 5 5
HELIX 8 8 THR A 122 VAL A 142 1 21
HELIX 9 9 VAL A 142 TYR A 161 1 20
HELIX 10 10 ILE A 180 VAL A 201 1 22
HELIX 11 11 TYR A 214 TYR A 221 1 8
HELIX 12 12 ASP A 225 LEU A 237 1 13
HELIX 13 13 HIS A 251 LEU A 281 1 31
HELIX 14 14 PRO A 304 LEU A 328 1 25
HELIX 15 15 LEU A 337 ARG A 344 1 8
HELIX 16 16 ASN A 345 LYS A 366 1 22
HELIX 17 17 ASN A 370 ASP A 379 1 10
HELIX 18 18 HIS A 380 VAL A 384 5 5
HELIX 19 19 LEU A 385 TYR A 396 1 12
HELIX 20 20 LYS A 400 ARG A 410 1 11
HELIX 21 21 ASP A 415 GLY A 425 1 11
HELIX 22 22 PRO A 429 ALA A 438 1 10
HELIX 23 23 ARG A 447 LEU A 455 1 9
SHEET 1 A 2 PRO A 165 THR A 170 0
SHEET 2 A 2 GLN A 173 THR A 179 -1 O SER A 178 N LEU A 166
SHEET 1 B 2 LEU A 204 GLY A 205 0
SHEET 2 B 2 GLN A 240 TRP A 241 1 O GLN A 240 N GLY A 205
SHEET 1 C 2 PHE A 284 GLN A 286 0
SHEET 2 C 2 LEU A 367 VAL A 369 -1 O GLU A 368 N LYS A 285
LINK O LEU A 47 NA NA A 501 1555 1555 2.90
LINK O ALA A 48 NA NA A 501 1555 1555 2.90
LINK O HIS A 50 NA NA A 501 1555 1555 2.48
LINK O ILE A 53 NA NA A 501 1555 1555 2.56
LINK O VAL A 56 NA NA A 501 1555 1555 2.53
LINK O SER A 331 NA NA A 502 1555 1555 2.44
LINK O TRP A 333 NA NA A 502 1555 1555 2.90
SITE 1 AC1 5 LEU A 47 ALA A 48 HIS A 50 ILE A 53
SITE 2 AC1 5 VAL A 56
SITE 1 AC2 4 ASP A 270 ASP A 274 SER A 331 TRP A 333
SITE 1 AC3 8 ARG A 15 TYR A 16 ASN A 309 SER A 340
SITE 2 AC3 8 THR A 341 ARG A 344 HOH A 669 HOH A 716
SITE 1 AC4 10 HIS A 91 THR A 122 SER A 123 GLN A 247
SITE 2 AC4 10 SER A 295 SER A 296 THR A 297 MET A 298
SITE 3 AC4 10 HOH A 774 HOH A 898
CRYST1 77.316 100.256 150.104 90.00 90.00 90.00 I 2 2 2 8
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 0.012934 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009974 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006662 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
