HEADER ISOMERASE 17-JAN-11 3QD5
TITLE CRYSTAL STRUCTURE OF A PUTATIVE RIBOSE-5-PHOSPHATE ISOMERASE FROM
TITLE 2 COCCIDIOIDES IMMITIS SOLVED BY COMBINED IODIDE ION SAD AND MR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE RIBOSE-5-PHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.3.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COCCIDIOIDES IMMITIS;
SOURCE 3 ORGANISM_TAXID: 246410;
SOURCE 4 STRAIN: RS;
SOURCE 5 GENE: CIMG_07932, 4559626;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: AVA0421
KEYWDS STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 2 INFECTIOUS DISEASE, SSGCID, COCCIDIOIDOMYCOSIS, PUTATIVE
KEYWDS 3 UNCHARACTERIZED PROTEIN, HYPOTHETICAL PROTEIN, RIBOSE-5-PHOSPHATE
KEYWDS 4 ISOMERASE, IODIDE ION, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 3 27-SEP-17 3QD5 1 REMARK
REVDAT 2 26-OCT-11 3QD5 1 JRNL VERSN
REVDAT 1 09-FEB-11 3QD5 0
JRNL AUTH T.E.EDWARDS,A.B.ABRAMOV,E.R.SMITH,R.O.BAYDO,J.T.LEONARD,
JRNL AUTH 2 D.J.LEIBLY,K.B.THOMPKINS,M.C.CLIFTON,A.S.GARDBERG,
JRNL AUTH 3 B.L.STAKER,W.C.VAN VOORHIS,P.J.MYLER,L.J.STEWART
JRNL TITL STRUCTURAL CHARACTERIZATION OF A RIBOSE-5-PHOSPHATE
JRNL TITL 2 ISOMERASE B FROM THE PATHOGENIC FUNGUS COCCIDIOIDES IMMITIS.
JRNL REF BMC STRUCT.BIOL. V. 11 39 2011
JRNL REFN ESSN 1472-6807
JRNL PMID 21995815
JRNL DOI 10.1186/1472-6807-11-39
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 22275
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1205
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) : 1434
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.1850
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2369
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 213
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.11000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : -0.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.813
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
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): 2456 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3345 ; 1.364 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 340 ; 7.517 ; 5.235
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;38.448 ;24.286
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 404 ;12.031 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;13.156 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 407 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1810 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1612 ; 0.729 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2594 ; 1.313 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 844 ; 2.329 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 744 ; 3.778 ; 4.500
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 : 2
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 -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2803 10.1056 16.8113
REMARK 3 T TENSOR
REMARK 3 T11: 0.0162 T22: 0.0161
REMARK 3 T33: 0.0207 T12: 0.0065
REMARK 3 T13: -0.0010 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.2894 L22: 0.7335
REMARK 3 L33: 0.3365 L12: -0.1113
REMARK 3 L13: -0.0407 L23: 0.2273
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.0222 S13: 0.0008
REMARK 3 S21: -0.0600 S22: 0.0279 S23: 0.0745
REMARK 3 S31: -0.0389 S32: -0.0225 S33: -0.0166
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 42.2236 -7.3692 12.0159
REMARK 3 T TENSOR
REMARK 3 T11: 0.0241 T22: 0.0121
REMARK 3 T33: 0.0119 T12: -0.0058
REMARK 3 T13: 0.0004 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.4193 L22: 0.6069
REMARK 3 L33: 0.2319 L12: 0.0459
REMARK 3 L13: 0.0006 L23: -0.0629
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: -0.0009 S13: -0.0282
REMARK 3 S21: -0.0736 S22: 0.0309 S23: -0.0123
REMARK 3 S31: 0.0178 S32: 0.0031 S33: -0.0279
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3QD5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23513
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4900
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) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.15200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD, MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: COIMA.00584.A.A1 PS00647 82 MG/ML
REMARK 280 AGAINST JCSG+ SCREEN CONDITION B9, 20% PEG 6000, 0.1 M NA
REMARK 280 CITRATE PH 5.0, AND SOAKED INTO 20% PEG 6000, 0.1 M NA CITRATE
REMARK 280 PH 5.0, 0.7 M NAI, 22% ETHYLENE GLYCOL FOR ONE MINUTE, CRYSTAL
REMARK 280 TRACKING ID 216516B9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.57500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.94500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.57500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.94500
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 83.36359
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 58.72631
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 I IOD A 176 LIES ON A SPECIAL POSITION.
REMARK 375 I IOD B 175 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 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 163
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
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 32 CG OD1 OD2
REMARK 470 LYS A 50 CG CD CE NZ
REMARK 470 HIS A 55 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 120 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 147 CG CD OE1 NE2
REMARK 470 LYS A 157 CG CD CE NZ
REMARK 470 GLN B 59 CG CD OE1 NE2
REMARK 470 LYS B 148 CG CD CE NZ
REMARK 470 ASN B 163 CG OD1 ND2
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 B 104 O HOH B 256 2.13
REMARK 500 O HOH A 189 O HOH A 244 2.17
REMARK 500 I IOD B 176 O HOH B 255 2.18
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 EDO A 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 174
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 172
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 174
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 180
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: COIMA.00584.A RELATED DB: TARGETDB
DBREF 3QD5 A -3 163 PDB 3QD5 3QD5 -3 163
DBREF 3QD5 B -3 163 PDB 3QD5 3QD5 -3 163
SEQRES 1 A 167 GLY PRO GLY SER MET ALA ALA THR PRO LEU PRO PRO LEU
SEQRES 2 A 167 ARG LEU ALA ILE ALA CYS ASP ASP ALA GLY VAL SER TYR
SEQRES 3 A 167 LYS GLU ALA LEU LYS ALA HIS LEU SER ASP ASN PRO LEU
SEQRES 4 A 167 VAL SER SER ILE THR ASP VAL GLY VAL THR SER THR THR
SEQRES 5 A 167 ASP LYS THR ALA TYR PRO HIS VAL ALA ILE GLN ALA ALA
SEQRES 6 A 167 GLN LEU ILE LYS ASP GLY LYS VAL ASP ARG ALA LEU MET
SEQRES 7 A 167 ILE CSO GLY THR GLY LEU GLY VAL ALA ILE SER ALA ASN
SEQRES 8 A 167 LYS VAL PRO GLY ILE ARG ALA VAL THR ALA HIS ASP THR
SEQRES 9 A 167 PHE SER VAL GLU ARG ALA ILE LEU SER ASN ASP ALA GLN
SEQRES 10 A 167 VAL LEU CYS PHE GLY GLN ARG VAL ILE GLY ILE GLU LEU
SEQRES 11 A 167 ALA LYS ARG LEU ALA GLY GLU TRP LEU THR TYR ARG PHE
SEQRES 12 A 167 ASP GLN LYS SER ALA SER ALA GLN LYS VAL GLN ALA ILE
SEQRES 13 A 167 SER ASP TYR GLU LYS LYS PHE VAL GLU VAL ASN
SEQRES 1 B 167 GLY PRO GLY SER MET ALA ALA THR PRO LEU PRO PRO LEU
SEQRES 2 B 167 ARG LEU ALA ILE ALA CYS ASP ASP ALA GLY VAL SER TYR
SEQRES 3 B 167 LYS GLU ALA LEU LYS ALA HIS LEU SER ASP ASN PRO LEU
SEQRES 4 B 167 VAL SER SER ILE THR ASP VAL GLY VAL THR SER THR THR
SEQRES 5 B 167 ASP LYS THR ALA TYR PRO HIS VAL ALA ILE GLN ALA ALA
SEQRES 6 B 167 GLN LEU ILE LYS ASP GLY LYS VAL ASP ARG ALA LEU MET
SEQRES 7 B 167 ILE CSO GLY THR GLY LEU GLY VAL ALA ILE SER ALA ASN
SEQRES 8 B 167 LYS VAL PRO GLY ILE ARG ALA VAL THR ALA HIS ASP THR
SEQRES 9 B 167 PHE SER VAL GLU ARG ALA ILE LEU SER ASN ASP ALA GLN
SEQRES 10 B 167 VAL LEU CYS PHE GLY GLN ARG VAL ILE GLY ILE GLU LEU
SEQRES 11 B 167 ALA LYS ARG LEU ALA GLY GLU TRP LEU THR TYR ARG PHE
SEQRES 12 B 167 ASP GLN LYS SER ALA SER ALA GLN LYS VAL GLN ALA ILE
SEQRES 13 B 167 SER ASP TYR GLU LYS LYS PHE VAL GLU VAL ASN
MODRES 3QD5 CSO A 76 CYS S-HYDROXYCYSTEINE
MODRES 3QD5 CSO B 76 CYS S-HYDROXYCYSTEINE
HET CSO A 76 11
HET CSO B 76 11
HET EDO A 164 4
HET IOD A 165 1
HET IOD A 166 1
HET IOD A 167 1
HET IOD A 168 1
HET IOD A 169 1
HET IOD A 170 1
HET IOD A 171 1
HET IOD A 172 1
HET IOD A 173 1
HET IOD A 174 1
HET IOD A 175 1
HET IOD A 176 1
HET IOD A 177 1
HET EDO B 164 4
HET IOD B 165 1
HET IOD B 166 1
HET IOD B 167 1
HET IOD B 168 1
HET IOD B 169 1
HET IOD B 170 1
HET IOD B 171 1
HET IOD B 172 1
HET IOD B 173 1
HET IOD B 174 1
HET IOD B 175 1
HET IOD B 176 1
HET IOD B 177 1
HET IOD B 178 1
HET IOD B 179 1
HET IOD B 180 1
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM IOD IODIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 4 IOD 29(I 1-)
FORMUL 34 HOH *213(H2 O)
HELIX 1 1 GLY A 19 ASP A 32 1 14
HELIX 2 2 ALA A 52 ASP A 66 1 15
HELIX 3 3 GLY A 79 LYS A 88 1 10
HELIX 4 4 ASP A 99 SER A 109 1 11
HELIX 5 5 GLY A 123 LEU A 135 1 13
HELIX 6 6 SER A 143 LYS A 157 1 15
HELIX 7 7 GLY B 19 ASP B 32 1 14
HELIX 8 8 ALA B 52 ASP B 66 1 15
HELIX 9 9 GLY B 79 LYS B 88 1 10
HELIX 10 10 ASP B 99 SER B 109 1 11
HELIX 11 11 GLY B 123 LEU B 135 1 13
HELIX 12 12 ALA B 144 LYS B 157 1 14
SHEET 1 A 5 VAL A 36 GLY A 43 0
SHEET 2 A 5 LEU A 9 CYS A 15 1 N ILE A 13 O VAL A 42
SHEET 3 A 5 ARG A 71 CSO A 76 1 O ILE A 75 N ALA A 14
SHEET 4 A 5 VAL A 114 GLY A 118 1 O LEU A 115 N MET A 74
SHEET 5 A 5 ALA A 94 THR A 96 1 N VAL A 95 O CYS A 116
SHEET 1 B 2 PHE A 159 GLU A 161 0
SHEET 2 B 2 PHE B 159 GLU B 161 -1 O VAL B 160 N VAL A 160
SHEET 1 C 5 VAL B 36 ASP B 41 0
SHEET 2 C 5 LEU B 9 CYS B 15 1 N LEU B 11 O SER B 38
SHEET 3 C 5 ARG B 71 CSO B 76 1 O LEU B 73 N ALA B 12
SHEET 4 C 5 VAL B 114 GLY B 118 1 O LEU B 115 N MET B 74
SHEET 5 C 5 ALA B 94 THR B 96 1 N VAL B 95 O CYS B 116
LINK C ILE A 75 N CSO A 76 1555 1555 1.33
LINK C CSO A 76 N GLY A 77 1555 1555 1.32
LINK C ILE B 75 N CSO B 76 1555 1555 1.32
LINK C CSO B 76 N GLY B 77 1555 1555 1.33
CISPEP 1 GLY A 43 VAL A 44 0 -3.19
CISPEP 2 GLY B 43 VAL B 44 0 -3.52
SITE 1 AC1 5 ARG A 71 ASP A 111 ALA A 112 HOH A 205
SITE 2 AC1 5 HOH A 256
SITE 1 AC2 5 ARG B 71 ASP B 111 ALA B 112 HOH B 212
SITE 2 AC2 5 HOH B 264
SITE 1 AC3 2 IOD A 166 HOH A 241
SITE 1 AC4 1 IOD A 165
SITE 1 AC5 2 IOD A 168 HOH B 182
SITE 1 AC6 2 ARG A 138 IOD A 167
SITE 1 AC7 4 CSO A 76 THR A 78 GLY A 81 HOH A 195
SITE 1 AC8 1 IOD A 171
SITE 1 AC9 4 GLY A 77 ARG A 120 IOD A 170 HOH A 278
SITE 1 BC1 2 ALA A 52 ALA B 151
SITE 1 BC2 2 GLN A 62 TYR B 155
SITE 1 BC3 2 ASP A 99 THR A 100
SITE 1 BC4 2 HOH A 243 ARG B 120
SITE 1 BC5 1 IOD B 180
SITE 1 BC6 4 TYR A 155 SER B 46 HOH B 202 HOH B 214
SITE 1 BC7 2 ALA B 52 HIS B 55
SITE 1 BC8 2 ASP B 99 THR B 100
SITE 1 BC9 3 HIS B 29 HOH B 253 HOH B 255
SITE 1 CC1 2 GLN B 141 LYS B 142
SITE 1 CC2 1 HOH B 191
SITE 1 CC3 2 IOD B 166 HOH B 197
CRYST1 103.150 49.890 61.970 90.00 108.62 90.00 C 1 2 1 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 0.009695 0.000000 0.003266 0.00000
SCALE2 0.000000 0.020044 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017028 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
