HEADER LYASE 16-JUN-05 2A0N
TITLE CRYSTAL STRUCTURE OF IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT
TITLE 2 HISF (EC 4.1.3.-) (TM1036) FROM THERMOTOGA MARITIMA AT 1.64 A
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IGP SYNTHASE CYCLASE SUBUNIT, IGP SYNTHASE SUBUNIT HISF,
COMPND 5 IMGP SYNTHASE SUBUNIT HISF, IGPS SUBUNIT HISF;
COMPND 6 EC: 4.1.3.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: HISF;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TM1036, IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF, EC
KEYWDS 2 4.1.3.-, IGP, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 5 20-SEP-23 2A0N 1 REMARK
REVDAT 4 25-JAN-23 2A0N 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2A0N 1 VERSN
REVDAT 2 24-FEB-09 2A0N 1 VERSN
REVDAT 1 19-JUL-05 2A0N 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE
JRNL TITL 2 SUBUNIT HISF (EC 4.1.3.-) (TM1036) FROM THERMOTOGA MARITIMA
JRNL TITL 3 AT 1.64 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0001
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 50488
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2704
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) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3630
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 204
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1915
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 279
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.45
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) : -0.04000
REMARK 3 B12 (A**2) : 0.01000
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): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.068
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.353
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2018 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1918 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2724 ; 1.908 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4433 ; 1.699 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 256 ; 5.213 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 84 ;36.281 ;24.524
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 362 ;10.150 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;20.161 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 317 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2257 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 417 ; 0.017 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 421 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2068 ; 0.194 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1188 ; 0.096 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 190 ; 0.167 ; 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): 3 ; 0.086 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 14 ; 0.181 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.167 ; 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): 1266 ; 1.901 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 527 ; 0.555 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2031 ; 3.040 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 798 ; 5.007 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 693 ; 7.148 ;11.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 251
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2282 79.1115 37.3060
REMARK 3 T TENSOR
REMARK 3 T11: -0.0745 T22: -0.0361
REMARK 3 T33: -0.0531 T12: -0.0031
REMARK 3 T13: 0.0254 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 1.5126 L22: 0.6465
REMARK 3 L33: 0.8217 L12: -0.1393
REMARK 3 L13: -0.0954 L23: 0.0937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0412 S12: -0.1588 S13: 0.1606
REMARK 3 S21: 0.0671 S22: -0.0102 S23: 0.0454
REMARK 3 S31: -0.0769 S32: -0.0755 S33: -0.0311
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. THE ADDITIONAL DENSITY NEAR CYS-9 HAS BEEN
REMARK 3 MODELED AS AN UNL, UNKNOWN LIGAND. THIS RESIDUE IS COVALENTLY
REMARK 3 BOUND TO SG OF CYS-9.
REMARK 4
REMARK 4 2A0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979748
REMARK 200 MONOCHROMATOR : FLAT MIRROR; SIDE-DEFLECTING
REMARK 200 MONOCHROMATOR (SI 111)
REMARK 200 OPTICS : FLAT MIRROR; SIDE-DEFLECTING
REMARK 200 MONOCHROMATOR (SI 111)
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, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53271
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 48.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.90
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
REMARK 200 R MERGE FOR SHELL (I) : 0.01400
REMARK 200 R SYM FOR SHELL (I) : 0.01369
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1VH7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2NONE NAL, 20.0% PEG-3350, NO
REMARK 280 BUFFER, PH 6.9, VAPOR DIFFUSION, SITTING DROP, NANODROP,
REMARK 280 TEMPERATURE 273K
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 51.94267
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 103.88533
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 77.91400
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 129.85667
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 25.97133
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 51.94267
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 103.88533
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 129.85667
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 77.91400
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 25.97133
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 GLY A 252
REMARK 465 LEU A 253
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 LEU A 2 CB CG CD1 CD2
REMARK 470 LYS A 19 CD CE NZ
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 ARG A 27 CZ NH1 NH2
REMARK 470 LYS A 68 CE NZ
REMARK 470 ARG A 230 CZ NH1 NH2
REMARK 470 GLU A 251 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 135 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 233 CB - CG - OD2 ANGL. DEV. = 5.6 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 LEU A 2 32.21 -83.39
REMARK 500 ASN A 103 -86.57 -144.72
REMARK 500 ALA A 224 -91.36 -130.21
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 IOD A 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 282903 RELATED DB: TARGETDB
DBREF 2A0N A 1 253 UNP Q9X0C6 HIS6_THEMA 1 253
SEQADV 2A0N MET A -11 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N GLY A -10 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N SER A -9 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N ASP A -8 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N LYS A -7 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N ILE A -6 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N HIS A -5 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N HIS A -4 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N HIS A -3 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N HIS A -2 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N HIS A -1 UNP Q9X0C6 EXPRESSION TAG
SEQADV 2A0N HIS A 0 UNP Q9X0C6 EXPRESSION TAG
SEQRES 1 A 265 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 265 LEU ALA LYS ARG ILE ILE ALA CYS LEU ASP VAL LYS ASP
SEQRES 3 A 265 GLY ARG VAL VAL LYS GLY THR ASN PHE GLU ASN LEU ARG
SEQRES 4 A 265 ASP SER GLY ASP PRO VAL GLU LEU GLY LYS PHE TYR SER
SEQRES 5 A 265 GLU ILE GLY ILE ASP GLU LEU VAL PHE LEU ASP ILE THR
SEQRES 6 A 265 ALA SER VAL GLU LYS ARG LYS THR MET LEU GLU LEU VAL
SEQRES 7 A 265 GLU LYS VAL ALA GLU GLN ILE ASP ILE PRO PHE THR VAL
SEQRES 8 A 265 GLY GLY GLY ILE HIS ASP PHE GLU THR ALA SER GLU LEU
SEQRES 9 A 265 ILE LEU ARG GLY ALA ASP LYS VAL SER ILE ASN THR ALA
SEQRES 10 A 265 ALA VAL GLU ASN PRO SER LEU ILE THR GLN ILE ALA GLN
SEQRES 11 A 265 THR PHE GLY SER GLN ALA VAL VAL VAL ALA ILE ASP ALA
SEQRES 12 A 265 LYS ARG VAL ASP GLY GLU PHE MET VAL PHE THR TYR SER
SEQRES 13 A 265 GLY LYS LYS ASN THR GLY ILE LEU LEU ARG ASP TRP VAL
SEQRES 14 A 265 VAL GLU VAL GLU LYS ARG GLY ALA GLY GLU ILE LEU LEU
SEQRES 15 A 265 THR SER ILE ASP ARG ASP GLY THR LYS SER GLY TYR ASP
SEQRES 16 A 265 THR GLU MET ILE ARG PHE VAL ARG PRO LEU THR THR LEU
SEQRES 17 A 265 PRO ILE ILE ALA SER GLY GLY ALA GLY LYS MET GLU HIS
SEQRES 18 A 265 PHE LEU GLU ALA PHE LEU ALA GLY ALA ASP ALA ALA LEU
SEQRES 19 A 265 ALA ALA SER VAL PHE HIS PHE ARG GLU ILE ASP VAL ARG
SEQRES 20 A 265 GLU LEU LYS GLU TYR LEU LYS LYS HIS GLY VAL ASN VAL
SEQRES 21 A 265 ARG LEU GLU GLY LEU
HET IOD A 254 1
HET IOD A 255 1
HET IOD A 256 1
HET IOD A 257 2
HET IOD A 258 2
HET IOD A 259 1
HET IOD A 260 1
HET PO4 A 261 5
HET UNL A 300 30
HETNAM IOD IODIDE ION
HETNAM PO4 PHOSPHATE ION
HETNAM UNL UNKNOWN LIGAND
FORMUL 2 IOD 7(I 1-)
FORMUL 9 PO4 O4 P 3-
FORMUL 11 HOH *279(H2 O)
HELIX 1 1 ASP A 31 GLY A 43 1 13
HELIX 2 2 ALA A 54 ILE A 73 1 20
HELIX 3 3 ASP A 85 GLY A 96 1 12
HELIX 4 4 ASN A 103 ASN A 109 1 7
HELIX 5 5 PRO A 110 GLY A 121 1 12
HELIX 6 6 LEU A 153 ARG A 163 1 11
HELIX 7 7 ASP A 183 ARG A 191 1 9
HELIX 8 8 PRO A 192 THR A 194 5 3
HELIX 9 9 LYS A 206 ALA A 216 1 11
HELIX 10 10 ALA A 224 PHE A 229 1 6
HELIX 11 11 ASP A 233 HIS A 244 1 12
SHEET 1 A 8 ARG A 16 VAL A 17 0
SHEET 2 A 8 ARG A 5 LYS A 13 -1 N LYS A 13 O ARG A 16
SHEET 3 A 8 GLU A 46 ASP A 51 1 O VAL A 48 N LEU A 10
SHEET 4 A 8 PHE A 77 GLY A 80 1 O GLY A 80 N ASP A 51
SHEET 5 A 8 LYS A 99 ILE A 102 1 O SER A 101 N VAL A 79
SHEET 6 A 8 VAL A 125 VAL A 134 1 O VAL A 126 N VAL A 100
SHEET 7 A 8 GLU A 137 THR A 142 -1 O MET A 139 N LYS A 132
SHEET 8 A 8 LYS A 147 LEU A 152 -1 O ILE A 151 N VAL A 140
SHEET 1 B 8 ARG A 16 VAL A 17 0
SHEET 2 B 8 ARG A 5 LYS A 13 -1 N LYS A 13 O ARG A 16
SHEET 3 B 8 ALA A 220 ALA A 223 1 O ALA A 221 N ILE A 7
SHEET 4 B 8 ILE A 198 SER A 201 1 N ALA A 200 O LEU A 222
SHEET 5 B 8 GLU A 167 SER A 172 1 N ILE A 168 O ILE A 199
SHEET 6 B 8 VAL A 125 VAL A 134 1 N ILE A 129 O LEU A 169
SHEET 7 B 8 GLU A 137 THR A 142 -1 O MET A 139 N LYS A 132
SHEET 8 B 8 LYS A 147 LEU A 152 -1 O ILE A 151 N VAL A 140
LINK SG CYS A 9 C25 UNL A 300 1555 1555 1.61
SITE 1 AC1 2 SER A 101 PO4 A 261
SITE 1 AC2 1 ARG A 163
SITE 1 AC3 2 GLU A 251 HOH A 577
SITE 1 AC4 2 GLU A 34 GLN A 72
SITE 1 AC5 3 HOH A 377 HOH A 412 HOH A 458
SITE 1 AC6 8 GLY A 82 ASN A 103 THR A 104 IOD A 254
SITE 2 AC6 8 HOH A 302 HOH A 401 HOH A 533 HOH A 535
SITE 1 AC7 18 CYS A 9 ASP A 11 ASP A 176 GLY A 177
SITE 2 AC7 18 LEU A 222 ALA A 223 ALA A 224 SER A 225
SITE 3 AC7 18 VAL A 226 HOH A 306 HOH A 489 HOH A 518
SITE 4 AC7 18 HOH A 530 HOH A 531 HOH A 532 HOH A 538
SITE 5 AC7 18 HOH A 542 HOH A 569
CRYST1 96.610 96.610 155.828 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 0.010350 0.005980 0.000000 0.00000
SCALE2 0.000000 0.011950 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006420 0.00000
(ATOM LINES ARE NOT SHOWN.)
END