HEADER LYASE 17-JUN-10 3NJB
TITLE CRYSTAL STRUCTURE OF ENOYL-COA HYDRATASE FROM MYCOBACTERIUM SMEGMATIS,
TITLE 2 IODIDE SOAK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-COA HYDRATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 4.2.1.17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 246196;
SOURCE 4 STRAIN: ATCC 700084 / MC(2)155;
SOURCE 5 GENE: MSMEG_1388;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS SSGCID, ENOYL-COA HYDRATASE, IODIDE SAD, SEATTLE STRUCTURAL GENOMICS
KEYWDS 2 CENTER FOR INFECTIOUS DISEASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 5 21-FEB-24 3NJB 1 REMARK SEQADV
REVDAT 4 07-MAR-18 3NJB 1 REMARK
REVDAT 3 11-MAR-15 3NJB 1 JRNL REMARK VERSN
REVDAT 2 06-JUL-11 3NJB 1 JRNL
REVDAT 1 28-JUL-10 3NJB 0
JRNL AUTH J.ABENDROTH,A.S.GARDBERG,J.I.ROBINSON,J.S.CHRISTENSEN,
JRNL AUTH 2 B.L.STAKER,P.J.MYLER,L.J.STEWART,T.E.EDWARDS
JRNL TITL SAD PHASING USING IODIDE IONS IN A HIGH-THROUGHPUT
JRNL TITL 2 STRUCTURAL GENOMICS ENVIRONMENT.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 12 83 2011
JRNL REFN ISSN 1345-711X
JRNL PMID 21359836
JRNL DOI 10.1007/S10969-011-9101-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.BAUGH,I.PHAN,D.W.BEGLEY,M.C.CLIFTON,B.ARMOUR,D.M.DRANOW,
REMARK 1 AUTH 2 B.M.TAYLOR,M.M.MURUTHI,J.ABENDROTH,J.W.FAIRMAN,D.FOX,
REMARK 1 AUTH 3 S.H.DIETERICH,B.L.STAKER,A.S.GARDBERG,R.CHOI,S.N.HEWITT,
REMARK 1 AUTH 4 A.J.NAPULI,J.MYERS,L.K.BARRETT,Y.ZHANG,M.FERRELL,E.MUNDT,
REMARK 1 AUTH 5 K.THOMPKINS,N.TRAN,S.LYONS-ABBOTT,A.ABRAMOV,A.SEKAR,
REMARK 1 AUTH 6 D.SERBZHINSKIY,D.LORIMER,G.W.BUCHKO,R.STACY,L.J.STEWART,
REMARK 1 AUTH 7 T.E.EDWARDS,W.C.VAN VOORHIS,P.J.MYLER
REMARK 1 TITL INCREASING THE STRUCTURAL COVERAGE OF TUBERCULOSIS DRUG
REMARK 1 TITL 2 TARGETS.
REMARK 1 REF TUBERCULOSIS (EDINB) 2014
REMARK 1 REFN ESSN 1873-281X
REMARK 1 PMID 25613812
REMARK 1 DOI 10.1016/J.TUBE.2014.12.003
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 41229
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) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2080
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2886
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE SET COUNT : 125
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4391
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 493
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.169
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.584
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4545 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3039 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6192 ; 1.331 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7365 ; 0.931 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 595 ; 5.567 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 208 ;38.169 ;22.981
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 703 ;12.396 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;13.874 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 692 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5204 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 952 ; 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): 2914 ; 0.648 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1187 ; 0.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4663 ; 1.178 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1631 ; 2.009 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1520 ; 3.113 ; 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 : 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 7 A 312 6
REMARK 3 1 B 7 B 312 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 3651 ; 0.300 ; 5.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 3651 ; 1.740 ;10.000
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): 40.1170 63.1060 34.4340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0451 T22: 0.0030
REMARK 3 T33: 0.0362 T12: -0.0072
REMARK 3 T13: -0.0047 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.3525 L22: 0.2453
REMARK 3 L33: 0.2701 L12: -0.0992
REMARK 3 L13: -0.1052 L23: 0.0784
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: 0.0138 S13: 0.0462
REMARK 3 S21: -0.0323 S22: 0.0023 S23: -0.0276
REMARK 3 S31: -0.0870 S32: 0.0179 S33: 0.0112
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): 34.9770 38.8820 10.6020
REMARK 3 T TENSOR
REMARK 3 T11: 0.0449 T22: 0.0378
REMARK 3 T33: 0.0017 T12: -0.0032
REMARK 3 T13: -0.0031 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.3944 L22: 0.3201
REMARK 3 L33: 0.2769 L12: -0.1686
REMARK 3 L13: -0.0733 L23: 0.0476
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: 0.0606 S13: -0.0093
REMARK 3 S21: -0.0856 S22: -0.0030 S23: 0.0193
REMARK 3 S31: -0.0149 S32: -0.0206 S33: 0.0048
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
REMARK 4
REMARK 4 3NJB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059900.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 0.00
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 : RIGAKI SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41229
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 45.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD, MR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM NAOAC, 100M BISTRISPROPANE, 20%
REMARK 280 PEG 3350; PROTEIN AT 27MG/ML, SOAKED IN 100MM BISTRISPROPANE, 25%
REMARK 280 PEG 3350, 400MM NAI; CRYO: 15% EDO, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 290K, PH 8.5, PH 0.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 85.03000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 85.03000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 85.03000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 85.03000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 85.03000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 85.03000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 85.03000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 85.03000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 85.03000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 85.03000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 85.03000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 85.03000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 85.03000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 85.03000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 85.03000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 85.03000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 85.03000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 85.03000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 85.03000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 85.03000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 85.03000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 85.03000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 85.03000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 85.03000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 85.03000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 85.03000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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 -20
REMARK 465 ALA 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 HIS A -13
REMARK 465 MET A -12
REMARK 465 GLY A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 ALA A -7
REMARK 465 GLN A -6
REMARK 465 THR A -5
REMARK 465 GLN A -4
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 THR A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 4
REMARK 465 ILE A 5
REMARK 465 ARG A 6
REMARK 465 PRO A 7
REMARK 465 LEU A 77
REMARK 465 SER A 78
REMARK 465 ALA A 79
REMARK 465 TYR A 80
REMARK 465 ALA A 81
REMARK 465 GLU A 82
REMARK 465 GLY A 83
REMARK 465 SER A 84
REMARK 465 SER A 85
REMARK 465 SER A 86
REMARK 465 ALA A 87
REMARK 465 GLY A 88
REMARK 465 GLY A 89
REMARK 465 GLY A 90
REMARK 465 SER A 91
REMARK 465 MET B -20
REMARK 465 ALA B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 MET B -12
REMARK 465 GLY B -11
REMARK 465 THR B -10
REMARK 465 LEU B -9
REMARK 465 GLU B -8
REMARK 465 ALA B -7
REMARK 465 GLN B -6
REMARK 465 THR B -5
REMARK 465 GLN B -4
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 THR B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 4
REMARK 465 ILE B 5
REMARK 465 ARG B 6
REMARK 465 LEU B 77
REMARK 465 SER B 78
REMARK 465 ALA B 79
REMARK 465 TYR B 80
REMARK 465 ALA B 81
REMARK 465 GLU B 82
REMARK 465 GLY B 83
REMARK 465 SER B 84
REMARK 465 SER B 85
REMARK 465 SER B 86
REMARK 465 ALA B 87
REMARK 465 GLY B 88
REMARK 465 GLY B 89
REMARK 465 GLY B 90
REMARK 465 SER B 91
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 76 CG OD1 OD2
REMARK 470 PRO A 92 CG CD
REMARK 470 GLU A 94 CG CD OE1 OE2
REMARK 470 LYS A 101 CG CD CE NZ
REMARK 470 LEU A 105 CG CD1 CD2
REMARK 470 ARG A 292 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 76 CG OD1 OD2
REMARK 470 GLU B 94 CG CD OE1 OE2
REMARK 470 LYS B 101 CG CD CE NZ
REMARK 470 LEU B 105 CG CD1 CD2
REMARK 470 GLU B 211 CG CD OE1 OE2
REMARK 470 GLU B 233 CG CD OE1 OE2
REMARK 470 ARG B 292 CG CD NE CZ NH1 NH2
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 I IOD A 314 O HOH A 506 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 307 NE - CZ - NH1 ANGL. DEV. = -3.1 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 ASP A 22 -109.86 65.90
REMARK 500 ASP A 110 30.75 -99.44
REMARK 500 ALA A 149 -127.23 58.91
REMARK 500 VAL A 176 142.01 -171.92
REMARK 500 TRP A 177 -3.54 87.61
REMARK 500 ASP B 22 -106.75 62.09
REMARK 500 ALA B 149 -130.63 57.58
REMARK 500 VAL B 176 136.50 -174.10
REMARK 500 TRP B 177 -0.53 93.35
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 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 324
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYSMA.00358.I RELATED DB: TARGETDB
DBREF 3NJB A 1 312 UNP A0QS86 A0QS86_MYCS2 1 312
DBREF 3NJB B 1 312 UNP A0QS86 A0QS86_MYCS2 1 312
SEQADV 3NJB MET A -20 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB ALA A -19 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS A -18 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS A -17 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS A -16 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS A -15 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS A -14 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS A -13 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB MET A -12 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLY A -11 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB THR A -10 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB LEU A -9 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLU A -8 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB ALA A -7 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLN A -6 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB THR A -5 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLN A -4 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLY A -3 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB PRO A -2 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLY A -1 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB SER A 0 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB MET B -20 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB ALA B -19 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS B -18 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS B -17 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS B -16 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS B -15 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS B -14 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB HIS B -13 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB MET B -12 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLY B -11 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB THR B -10 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB LEU B -9 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLU B -8 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB ALA B -7 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLN B -6 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB THR B -5 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLN B -4 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLY B -3 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB PRO B -2 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB GLY B -1 UNP A0QS86 EXPRESSION TAG
SEQADV 3NJB SER B 0 UNP A0QS86 EXPRESSION TAG
SEQRES 1 A 333 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 333 ALA GLN THR GLN GLY PRO GLY SER MET THR HIS ALA ILE
SEQRES 3 A 333 ARG PRO VAL ASP PHE ASP ASN LEU LYS THR MET THR TYR
SEQRES 4 A 333 GLU VAL THR ASP ARG VAL ALA ARG ILE THR PHE ASN ARG
SEQRES 5 A 333 PRO GLU LYS GLY ASN ALA ILE VAL ALA ASP THR PRO LEU
SEQRES 6 A 333 GLU LEU SER ALA LEU VAL GLU ARG ALA ASP LEU ASP PRO
SEQRES 7 A 333 ASP VAL HIS VAL ILE LEU VAL SER GLY ARG GLY GLU GLY
SEQRES 8 A 333 PHE CYS ALA GLY PHE ASP LEU SER ALA TYR ALA GLU GLY
SEQRES 9 A 333 SER SER SER ALA GLY GLY GLY SER PRO TYR GLU GLY THR
SEQRES 10 A 333 VAL LEU SER GLY LYS THR GLN ALA LEU ASN HIS LEU PRO
SEQRES 11 A 333 ASP GLU PRO TRP ASP PRO MET VAL ASP TYR GLN MET MET
SEQRES 12 A 333 SER ARG PHE VAL ARG GLY PHE ALA SER LEU MET HIS CYS
SEQRES 13 A 333 ASP LYS PRO THR VAL VAL LYS ILE HIS GLY TYR CYS VAL
SEQRES 14 A 333 ALA GLY GLY THR ASP ILE ALA LEU HIS ALA ASP GLN VAL
SEQRES 15 A 333 ILE ALA ALA ALA ASP ALA LYS ILE GLY TYR PRO PRO MET
SEQRES 16 A 333 ARG VAL TRP GLY VAL PRO ALA ALA GLY LEU TRP ALA HIS
SEQRES 17 A 333 ARG LEU GLY ASP GLN ARG ALA LYS ARG LEU LEU PHE THR
SEQRES 18 A 333 GLY ASP CYS ILE THR GLY ALA GLN ALA ALA GLU TRP GLY
SEQRES 19 A 333 LEU ALA VAL GLU ALA PRO ASP PRO ALA ASP LEU ASP ALA
SEQRES 20 A 333 ARG THR GLU ARG LEU VAL GLU ARG ILE ALA ALA MET PRO
SEQRES 21 A 333 VAL ASN GLN LEU ILE MET ALA LYS LEU ALA CYS ASN THR
SEQRES 22 A 333 ALA LEU LEU ASN GLN GLY VAL ALA THR SER GLN MET VAL
SEQRES 23 A 333 SER THR VAL PHE ASP GLY ILE ALA ARG HIS THR PRO GLU
SEQRES 24 A 333 GLY HIS ALA PHE VAL ALA THR ALA ARG GLU HIS GLY PHE
SEQRES 25 A 333 ARG GLU ALA VAL ARG ARG ARG ASP GLU PRO MET GLY ASP
SEQRES 26 A 333 HIS GLY ARG ARG ALA SER ASP VAL
SEQRES 1 B 333 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 B 333 ALA GLN THR GLN GLY PRO GLY SER MET THR HIS ALA ILE
SEQRES 3 B 333 ARG PRO VAL ASP PHE ASP ASN LEU LYS THR MET THR TYR
SEQRES 4 B 333 GLU VAL THR ASP ARG VAL ALA ARG ILE THR PHE ASN ARG
SEQRES 5 B 333 PRO GLU LYS GLY ASN ALA ILE VAL ALA ASP THR PRO LEU
SEQRES 6 B 333 GLU LEU SER ALA LEU VAL GLU ARG ALA ASP LEU ASP PRO
SEQRES 7 B 333 ASP VAL HIS VAL ILE LEU VAL SER GLY ARG GLY GLU GLY
SEQRES 8 B 333 PHE CYS ALA GLY PHE ASP LEU SER ALA TYR ALA GLU GLY
SEQRES 9 B 333 SER SER SER ALA GLY GLY GLY SER PRO TYR GLU GLY THR
SEQRES 10 B 333 VAL LEU SER GLY LYS THR GLN ALA LEU ASN HIS LEU PRO
SEQRES 11 B 333 ASP GLU PRO TRP ASP PRO MET VAL ASP TYR GLN MET MET
SEQRES 12 B 333 SER ARG PHE VAL ARG GLY PHE ALA SER LEU MET HIS CYS
SEQRES 13 B 333 ASP LYS PRO THR VAL VAL LYS ILE HIS GLY TYR CYS VAL
SEQRES 14 B 333 ALA GLY GLY THR ASP ILE ALA LEU HIS ALA ASP GLN VAL
SEQRES 15 B 333 ILE ALA ALA ALA ASP ALA LYS ILE GLY TYR PRO PRO MET
SEQRES 16 B 333 ARG VAL TRP GLY VAL PRO ALA ALA GLY LEU TRP ALA HIS
SEQRES 17 B 333 ARG LEU GLY ASP GLN ARG ALA LYS ARG LEU LEU PHE THR
SEQRES 18 B 333 GLY ASP CYS ILE THR GLY ALA GLN ALA ALA GLU TRP GLY
SEQRES 19 B 333 LEU ALA VAL GLU ALA PRO ASP PRO ALA ASP LEU ASP ALA
SEQRES 20 B 333 ARG THR GLU ARG LEU VAL GLU ARG ILE ALA ALA MET PRO
SEQRES 21 B 333 VAL ASN GLN LEU ILE MET ALA LYS LEU ALA CYS ASN THR
SEQRES 22 B 333 ALA LEU LEU ASN GLN GLY VAL ALA THR SER GLN MET VAL
SEQRES 23 B 333 SER THR VAL PHE ASP GLY ILE ALA ARG HIS THR PRO GLU
SEQRES 24 B 333 GLY HIS ALA PHE VAL ALA THR ALA ARG GLU HIS GLY PHE
SEQRES 25 B 333 ARG GLU ALA VAL ARG ARG ARG ASP GLU PRO MET GLY ASP
SEQRES 26 B 333 HIS GLY ARG ARG ALA SER ASP VAL
HET IOD A 313 1
HET IOD A 314 1
HET IOD A 315 1
HET IOD A 316 1
HET IOD A 317 1
HET IOD A 318 1
HET IOD A 319 1
HET IOD A 320 1
HET IOD A 321 1
HET IOD A 322 1
HET IOD A 323 1
HET IOD A 324 1
HET IOD A 325 1
HET IOD A 326 1
HET IOD A 327 1
HET IOD B 313 1
HET IOD B 314 1
HET IOD B 315 1
HET IOD B 316 1
HET IOD B 317 1
HET IOD B 318 1
HET IOD B 319 1
HET IOD B 320 1
HET IOD B 321 1
HET IOD B 322 1
HET IOD B 323 1
HET IOD B 324 1
HETNAM IOD IODIDE ION
FORMUL 3 IOD 27(I 1-)
FORMUL 30 HOH *493(H2 O)
HELIX 1 1 ARG A 31 GLY A 35 5 5
HELIX 2 2 ALA A 40 ASP A 56 1 17
HELIX 3 3 SER A 99 ASN A 106 1 8
HELIX 4 4 ASP A 114 ALA A 130 1 17
HELIX 5 5 ALA A 130 CYS A 135 1 6
HELIX 6 6 ALA A 149 LEU A 156 1 8
HELIX 7 7 PRO A 172 ARG A 175 5 4
HELIX 8 8 LEU A 184 GLY A 190 1 7
HELIX 9 9 GLY A 190 PHE A 199 1 10
HELIX 10 10 GLY A 206 TRP A 212 1 7
HELIX 11 11 ASP A 220 ALA A 222 5 3
HELIX 12 12 ASP A 223 ALA A 237 1 15
HELIX 13 13 PRO A 239 GLN A 257 1 19
HELIX 14 14 GLY A 258 THR A 276 1 19
HELIX 15 15 THR A 276 GLY A 290 1 15
HELIX 16 16 GLY A 290 GLU A 300 1 11
HELIX 17 17 PRO A 301 GLY A 303 5 3
HELIX 18 18 ARG B 31 GLY B 35 5 5
HELIX 19 19 ALA B 40 ASP B 56 1 17
HELIX 20 20 SER B 99 ASN B 106 1 8
HELIX 21 21 ASP B 114 ALA B 130 1 17
HELIX 22 22 ALA B 130 CYS B 135 1 6
HELIX 23 23 ALA B 149 LEU B 156 1 8
HELIX 24 24 PRO B 172 VAL B 176 5 5
HELIX 25 25 LEU B 184 GLY B 190 1 7
HELIX 26 26 GLY B 190 PHE B 199 1 10
HELIX 27 27 GLY B 206 TRP B 212 1 7
HELIX 28 28 ASP B 220 ALA B 222 5 3
HELIX 29 29 ASP B 223 ALA B 237 1 15
HELIX 30 30 PRO B 239 GLN B 257 1 19
HELIX 31 31 GLY B 258 ARG B 274 1 17
HELIX 32 32 THR B 276 GLY B 290 1 15
HELIX 33 33 GLY B 290 GLU B 300 1 11
HELIX 34 34 PRO B 301 GLY B 303 5 3
SHEET 1 A 5 MET A 16 THR A 21 0
SHEET 2 A 5 VAL A 24 PHE A 29 -1 O ARG A 26 N GLU A 19
SHEET 3 A 5 VAL A 61 GLY A 66 1 O VAL A 61 N ALA A 25
SHEET 4 A 5 THR A 139 ILE A 143 1 O VAL A 140 N VAL A 64
SHEET 5 A 5 GLN A 160 ALA A 163 1 O GLN A 160 N VAL A 141
SHEET 1 B 3 TYR A 146 VAL A 148 0
SHEET 2 B 3 LYS A 168 GLY A 170 1 O LYS A 168 N CYS A 147
SHEET 3 B 3 CYS A 203 THR A 205 -1 O ILE A 204 N ILE A 169
SHEET 1 C 5 MET B 16 THR B 21 0
SHEET 2 C 5 VAL B 24 PHE B 29 -1 O ARG B 26 N GLU B 19
SHEET 3 C 5 VAL B 61 GLY B 66 1 O LEU B 63 N ALA B 25
SHEET 4 C 5 THR B 139 ILE B 143 1 O VAL B 140 N VAL B 64
SHEET 5 C 5 GLN B 160 ALA B 163 1 O GLN B 160 N VAL B 141
SHEET 1 D 3 TYR B 146 VAL B 148 0
SHEET 2 D 3 LYS B 168 GLY B 170 1 O LYS B 168 N CYS B 147
SHEET 3 D 3 CYS B 203 THR B 205 -1 O ILE B 204 N ILE B 169
SITE 1 AC1 2 ARG B 31 GLU B 33
SITE 1 AC2 2 ARG A 298 HOH A 506
SITE 1 AC3 1 ARG B 308
SITE 1 AC4 1 ARG A 307
SITE 1 AC5 1 GLY B 306
SITE 1 AC6 2 GLY A 100 IOD A 323
SITE 1 AC7 1 ARG B 298
SITE 1 AC8 1 ASP A 22
SITE 1 AC9 1 GLY B 100
SITE 1 BC1 1 HOH A 488
SITE 1 BC2 2 GLY B 258 THR B 261
SITE 1 BC3 2 GLY A 258 THR A 261
SITE 1 BC4 1 IOD A 316
SITE 1 BC5 1 HOH A 402
SITE 1 BC6 1 HOH B 608
SITE 1 BC7 1 GLY B 68
SITE 1 BC8 1 SER A 47
SITE 1 BC9 2 GLY B 95 SER B 99
CRYST1 170.060 170.060 170.060 90.00 90.00 90.00 I 2 3 48
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 0.005880 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005880 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005880 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
