HEADER ISOMERASE 23-MAY-08 3D8H
TITLE CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM CRYPTOSPORIDIUM
TITLE 2 PARVUM, CGD7_4270
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOLYTIC PHOSPHOGLYCERATE MUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM PARVUM;
SOURCE 3 ORGANISM_TAXID: 353152;
SOURCE 4 STRAIN: IOWA II;
SOURCE 5 GENE: CGD7_4270;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A-THROMBIN-LIC
KEYWDS STRUCTURAL GENOMICS, MALARIA, CRYPTOSPORIDIUM, GLYCOLYSIS, ISOMERASE,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.WERNIMONT,J.LEW,G.WASNEY,Z.ALAM,I.KOZIERADZKI,D.COSSAR,
AUTHOR 2 M.SCHAPIRO,A.BOCHKAREV,C.H.ARROWSMITH,C.BOUNTRA,M.WILKSTROM,
AUTHOR 3 A.M.EDWARDS,R.HUI,J.D.ARTZ,T.HILLS,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 4 (SGC)
REVDAT 5 07-SEP-11 3D8H 1 JRNL
REVDAT 4 24-AUG-11 3D8H 1 JRNL
REVDAT 3 13-JUL-11 3D8H 1 VERSN
REVDAT 2 24-FEB-09 3D8H 1 VERSN
REVDAT 1 15-JUL-08 3D8H 0
JRNL AUTH T.HILLS,A.SRIVASTAVA,K.AYI,A.K.WERNIMONT,K.KAIN,A.P.WATERS,
JRNL AUTH 2 R.HUI,J.C.PIZARRO
JRNL TITL CHARACTERIZATION OF A NEW PHOSPHATASE FROM PLASMODIUM.
JRNL REF MOL.BIOCHEM.PARASITOL. V. 179 69 2011
JRNL REFN ISSN 0166-6851
JRNL PMID 21689687
JRNL DOI 10.1016/J.MOLBIOPARA.2011.06.001
REMARK 2
REMARK 2 RESOLUTION. 2.01 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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 39074
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1958
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2630
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 134
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3641
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.80000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : -1.55000
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): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.169
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.149
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.193
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
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): 3755 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5112 ; 1.141 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 469 ; 5.920 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;33.578 ;24.474
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 652 ;14.967 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.109 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 582 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2785 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1747 ; 0.185 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2560 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 212 ; 0.129 ; 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): 38 ; 0.140 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.127 ; 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): 2416 ; 0.384 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3777 ; 0.647 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1582 ; 1.020 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1331 ; 1.504 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 197 A 205 3
REMARK 3 1 B 197 B 205 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 B (A): 36 ; 0.030 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 B (A): 26 ; 0.120 ; 5.000
REMARK 3 TIGHT THERMAL 1 B (A**2): 36 ; 0.100 ; 0.500
REMARK 3 LOOSE THERMAL 1 B (A**2): 26 ; 0.810 ;10.000
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 : 1.40
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 3D8H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-08.
REMARK 100 THE RCSB ID CODE IS RCSB047724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39125
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.79600
REMARK 200 R SYM FOR SHELL (I) : 0.79600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.320
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 1XQ9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2 M NH4OAC, 0.1 M
REMARK 280 HEPES PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 70.12450
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 70.12450
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 26.12400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 79.18250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.12400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 79.18250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.12450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.12400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 79.18250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.12450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.12400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 79.18250
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 SER A 249
REMARK 465 GLU A 250
REMARK 465 GLU A 251
REMARK 465 GLU A 252
REMARK 465 LEU A 253
REMARK 465 LYS A 254
REMARK 465 ALA A 255
REMARK 465 LYS A 256
REMARK 465 MET A 257
REMARK 465 GLU A 258
REMARK 465 ALA A 259
REMARK 465 VAL A 260
REMARK 465 ALA A 261
REMARK 465 ASN A 262
REMARK 465 GLN A 263
REMARK 465 GLY A 264
REMARK 465 LYS A 265
REMARK 465 ALA A 266
REMARK 465 LYS A 267
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 LEU B 14
REMARK 465 VAL B 15
REMARK 465 SER B 249
REMARK 465 GLU B 252
REMARK 465 LEU B 253
REMARK 465 LYS B 254
REMARK 465 ALA B 255
REMARK 465 LYS B 256
REMARK 465 MET B 257
REMARK 465 GLU B 258
REMARK 465 ALA B 259
REMARK 465 VAL B 260
REMARK 465 ALA B 261
REMARK 465 ASN B 262
REMARK 465 GLN B 263
REMARK 465 GLY B 264
REMARK 465 LYS B 265
REMARK 465 ALA B 266
REMARK 465 LYS B 267
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 ARG A 38 CZ NH1 NH2
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 ARG A 133 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 134 CZ NH1 NH2
REMARK 470 LYS A 145 CE NZ
REMARK 470 GLU A 222 CG CD OE1 OE2
REMARK 470 ASN A 224 CG OD1 ND2
REMARK 470 LYS A 240 CD CE NZ
REMARK 470 ILE A 248 CG1 CG2 CD1
REMARK 470 ARG B 17 NE CZ NH1 NH2
REMARK 470 LYS B 123 CG CD CE NZ
REMARK 470 ASP B 127 CG OD1 OD2
REMARK 470 VAL B 129 CG1 CG2
REMARK 470 ARG B 133 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 134 CZ NH1 NH2
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 GLU B 218 CD OE1 OE2
REMARK 470 GLU B 222 CG CD OE1 OE2
REMARK 470 ASN B 224 CG OD1 ND2
REMARK 470 ILE B 225 CD1
REMARK 470 LYS B 240 CE NZ
REMARK 470 ILE B 248 CG1 CG2 CD1
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 GLN A 219 CD GLN A 219 OE1 0.234
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 A 40 -65.17 -101.40
REMARK 500 ASN A 93 33.58 -143.53
REMARK 500 VAL A 185 -58.34 -120.95
REMARK 500 ALA A 200 -138.54 -145.83
REMARK 500 ASN B 116 -169.29 -71.72
REMARK 500 PHE B 124 -163.63 -122.49
REMARK 500 VAL B 185 -57.61 -120.04
REMARK 500 ALA B 200 -133.64 -149.99
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3D8H A 20 267 UNP Q5CXZ9 Q5CXZ9_CRYPV 2 249
DBREF 3D8H B 20 266 UNP Q5CXZ9 Q5CXZ9_CRYPV 2 249
SEQADV 3D8H MET A 1 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H GLY A 2 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER A 3 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER A 4 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS A 5 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS A 6 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS A 7 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS A 8 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS A 9 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS A 10 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER A 11 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER A 12 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H GLY A 13 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H LEU A 14 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H VAL A 15 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H PRO A 16 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H ARG A 17 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H GLY A 18 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER A 19 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H MET B 1 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H GLY B 2 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER B 3 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER B 4 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS B 5 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS B 6 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS B 7 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS B 8 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS B 9 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H HIS B 10 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER B 11 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER B 12 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H GLY B 13 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H LEU B 14 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H VAL B 15 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H PRO B 16 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H ARG B 17 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H GLY B 18 UNP Q5CXZ9 EXPRESSION TAG
SEQADV 3D8H SER B 19 UNP Q5CXZ9 EXPRESSION TAG
SEQRES 1 A 267 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 267 LEU VAL PRO ARG GLY SER THR TYR LYS LEU THR LEU ILE
SEQRES 3 A 267 ARG HIS GLY GLU SER GLU TRP ASN LYS GLU ASN ARG PHE
SEQRES 4 A 267 THR GLY TRP THR ASP VAL SER LEU SER GLU GLN GLY VAL
SEQRES 5 A 267 SER GLU ALA ILE GLU ALA GLY ARG MET LEU LEU GLU LYS
SEQRES 6 A 267 GLY PHE LYS PHE ASP VAL VAL TYR THR SER VAL LEU LYS
SEQRES 7 A 267 ARG ALA ILE MET THR THR TRP THR VAL LEU LYS GLU LEU
SEQRES 8 A 267 GLY ASN ILE ASN CYS PRO ILE ILE ASN HIS TRP ARG LEU
SEQRES 9 A 267 ASN GLU ARG HIS TYR GLY ALA LEU GLN GLY LEU ASN LYS
SEQRES 10 A 267 SER GLU THR ALA SER LYS PHE GLY GLU ASP GLN VAL LYS
SEQRES 11 A 267 ILE TRP ARG ARG SER PHE ASP VAL PRO PRO PRO VAL LEU
SEQRES 12 A 267 GLU LYS SER ASP PRO ARG TRP PRO GLY ASN GLU LEU ILE
SEQRES 13 A 267 TYR LYS GLY ILE CYS PRO SER CYS LEU PRO THR THR GLU
SEQRES 14 A 267 CYS LEU LYS ASP THR VAL GLU ARG VAL LYS PRO TYR PHE
SEQRES 15 A 267 GLU ASP VAL ILE ALA PRO SER ILE MET SER GLY LYS SER
SEQRES 16 A 267 VAL LEU VAL SER ALA HIS GLY ASN SER LEU ARG ALA LEU
SEQRES 17 A 267 LEU TYR LEU LEU GLU GLY MET THR PRO GLU GLN ILE LEU
SEQRES 18 A 267 GLU VAL ASN ILE PRO THR ALA CYS PRO LEU VAL LEU GLU
SEQRES 19 A 267 LEU ASP ASP TYR LEU LYS VAL THR LYS LYS TYR TYR LEU
SEQRES 20 A 267 ILE SER GLU GLU GLU LEU LYS ALA LYS MET GLU ALA VAL
SEQRES 21 A 267 ALA ASN GLN GLY LYS ALA LYS
SEQRES 1 B 267 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 267 LEU VAL PRO ARG GLY SER THR TYR LYS LEU THR LEU ILE
SEQRES 3 B 267 ARG HIS GLY GLU SER GLU TRP ASN LYS GLU ASN ARG PHE
SEQRES 4 B 267 THR GLY TRP THR ASP VAL SER LEU SER GLU GLN GLY VAL
SEQRES 5 B 267 SER GLU ALA ILE GLU ALA GLY ARG MET LEU LEU GLU LYS
SEQRES 6 B 267 GLY PHE LYS PHE ASP VAL VAL TYR THR SER VAL LEU LYS
SEQRES 7 B 267 ARG ALA ILE MET THR THR TRP THR VAL LEU LYS GLU LEU
SEQRES 8 B 267 GLY ASN ILE ASN CYS PRO ILE ILE ASN HIS TRP ARG LEU
SEQRES 9 B 267 ASN GLU ARG HIS TYR GLY ALA LEU GLN GLY LEU ASN LYS
SEQRES 10 B 267 SER GLU THR ALA SER LYS PHE GLY GLU ASP GLN VAL LYS
SEQRES 11 B 267 ILE TRP ARG ARG SER PHE ASP VAL PRO PRO PRO VAL LEU
SEQRES 12 B 267 GLU LYS SER ASP PRO ARG TRP PRO GLY ASN GLU LEU ILE
SEQRES 13 B 267 TYR LYS GLY ILE CYS PRO SER CYS LEU PRO THR THR GLU
SEQRES 14 B 267 CYS LEU LYS ASP THR VAL GLU ARG VAL LYS PRO TYR PHE
SEQRES 15 B 267 GLU ASP VAL ILE ALA PRO SER ILE MET SER GLY LYS SER
SEQRES 16 B 267 VAL LEU VAL SER ALA HIS GLY ASN SER LEU ARG ALA LEU
SEQRES 17 B 267 LEU TYR LEU LEU GLU GLY MET THR PRO GLU GLN ILE LEU
SEQRES 18 B 267 GLU VAL ASN ILE PRO THR ALA CYS PRO LEU VAL LEU GLU
SEQRES 19 B 267 LEU ASP ASP TYR LEU LYS VAL THR LYS LYS TYR TYR LEU
SEQRES 20 B 267 ILE SER GLU GLU GLU LEU LYS ALA LYS MET GLU ALA VAL
SEQRES 21 B 267 ALA ASN GLN GLY LYS ALA LYS
FORMUL 3 HOH *206(H2 O)
HELIX 1 1 SER A 48 LYS A 65 1 18
HELIX 2 2 LEU A 77 GLY A 92 1 16
HELIX 3 3 TRP A 102 ASN A 105 5 4
HELIX 4 4 TYR A 109 GLN A 113 5 5
HELIX 5 5 ASN A 116 PHE A 124 1 9
HELIX 6 6 GLY A 125 SER A 135 1 11
HELIX 7 7 TRP A 150 LYS A 158 5 9
HELIX 8 8 CYS A 161 LEU A 165 5 5
HELIX 9 9 CYS A 170 VAL A 185 1 16
HELIX 10 10 VAL A 185 SER A 192 1 8
HELIX 11 11 HIS A 201 GLY A 214 1 14
HELIX 12 12 THR A 216 LEU A 221 1 6
HELIX 13 13 SER B 31 GLU B 36 1 6
HELIX 14 14 SER B 48 LYS B 65 1 18
HELIX 15 15 LEU B 77 LEU B 91 1 15
HELIX 16 16 TRP B 102 ASN B 105 5 4
HELIX 17 17 TYR B 109 GLN B 113 5 5
HELIX 18 18 SER B 118 PHE B 124 1 7
HELIX 19 19 GLY B 125 SER B 135 1 11
HELIX 20 20 TRP B 150 LYS B 158 5 9
HELIX 21 21 CYS B 161 LEU B 165 5 5
HELIX 22 22 CYS B 170 VAL B 185 1 16
HELIX 23 23 VAL B 185 SER B 192 1 8
HELIX 24 24 HIS B 201 GLY B 214 1 14
HELIX 25 25 THR B 216 GLU B 222 1 7
SHEET 1 A 6 ILE A 98 ASN A 100 0
SHEET 2 A 6 VAL A 71 THR A 74 1 N VAL A 72 O ILE A 99
SHEET 3 A 6 VAL A 196 ALA A 200 1 O SER A 199 N TYR A 73
SHEET 4 A 6 TYR A 21 ARG A 27 1 N THR A 24 O VAL A 198
SHEET 5 A 6 LEU A 231 LEU A 235 -1 O LEU A 233 N LEU A 23
SHEET 6 A 6 VAL A 241 TYR A 246 -1 O TYR A 245 N VAL A 232
SHEET 1 B 6 ILE B 98 ASN B 100 0
SHEET 2 B 6 VAL B 71 THR B 74 1 N VAL B 72 O ILE B 99
SHEET 3 B 6 VAL B 196 ALA B 200 1 O SER B 199 N TYR B 73
SHEET 4 B 6 TYR B 21 ARG B 27 1 N THR B 24 O VAL B 198
SHEET 5 B 6 LEU B 231 LEU B 235 -1 O LEU B 233 N LEU B 23
SHEET 6 B 6 VAL B 241 TYR B 246 -1 O LYS B 243 N GLU B 234
CRYST1 52.248 158.365 140.249 90.00 90.00 90.00 C 2 2 21 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 0.019139 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006315 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007130 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
