HEADER LYASE 01-APR-11 3RD8
TITLE CRYSTAL STRUCTURE OF FUMARATE HYDRATASE CLASS II MYCOBACTERIUM
TITLE 2 SMEGMATIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUMARATE HYDRATASE CLASS II;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.2;
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_5240;
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, FUMARATE HYDRATASE CLASS II, HYDRATASE, LYASE, STRUCTURAL
KEYWDS 2 GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 3 13-SEP-23 3RD8 1 SEQADV
REVDAT 2 22-APR-15 3RD8 1 JRNL VERSN
REVDAT 1 08-JUN-11 3RD8 0
JRNL AUTH L.BAUGH,I.PHAN,D.W.BEGLEY,M.C.CLIFTON,B.ARMOUR,D.M.DRANOW,
JRNL AUTH 2 B.M.TAYLOR,M.M.MURUTHI,J.ABENDROTH,J.W.FAIRMAN,D.FOX,
JRNL AUTH 3 S.H.DIETERICH,B.L.STAKER,A.S.GARDBERG,R.CHOI,S.N.HEWITT,
JRNL AUTH 4 A.J.NAPULI,J.MYERS,L.K.BARRETT,Y.ZHANG,M.FERRELL,E.MUNDT,
JRNL AUTH 5 K.THOMPKINS,N.TRAN,S.LYONS-ABBOTT,A.ABRAMOV,A.SEKAR,
JRNL AUTH 6 D.SERBZHINSKIY,D.LORIMER,G.W.BUCHKO,R.STACY,L.J.STEWART,
JRNL AUTH 7 T.E.EDWARDS,W.C.VAN VOORHIS,P.J.MYLER
JRNL TITL INCREASING THE STRUCTURAL COVERAGE OF TUBERCULOSIS DRUG
JRNL TITL 2 TARGETS.
JRNL REF TUBERCULOSIS (EDINB) V. 95 142 2015
JRNL REFN ISSN 1472-9792
JRNL PMID 25613812
JRNL 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) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 26630
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1332
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) : 1855
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3312
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 278
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.35000
REMARK 3 B22 (A**2) : 1.64000
REMARK 3 B33 (A**2) : -1.29000
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): 0.225
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.173
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.155
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3374 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2178 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4595 ; 1.335 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5344 ; 0.965 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 459 ; 5.304 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;35.415 ;24.632
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 526 ;12.411 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;15.944 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 550 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3871 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 637 ; 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): 2271 ; 0.507 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 933 ; 0.134 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3605 ; 0.892 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1103 ; 1.743 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 988 ; 2.713 ; 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 : 3
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 7 A 151
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7060 69.7330 -28.2920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1754 T22: 0.2569
REMARK 3 T33: 0.0692 T12: -0.0567
REMARK 3 T13: -0.0375 T23: 0.1247
REMARK 3 L TENSOR
REMARK 3 L11: 1.7095 L22: 1.0661
REMARK 3 L33: 0.7023 L12: -0.3524
REMARK 3 L13: -0.0846 L23: -0.0802
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: 0.4095 S13: 0.1534
REMARK 3 S21: -0.2868 S22: 0.0939 S23: 0.0622
REMARK 3 S31: -0.1120 S32: -0.0993 S33: -0.0968
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 : A 152 A 393
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0730 44.5260 -9.1610
REMARK 3 T TENSOR
REMARK 3 T11: 0.0564 T22: 0.1429
REMARK 3 T33: 0.0568 T12: -0.0446
REMARK 3 T13: -0.0181 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 0.7416 L22: 0.8508
REMARK 3 L33: 0.4940 L12: -0.0720
REMARK 3 L13: -0.0097 L23: -0.1051
REMARK 3 S TENSOR
REMARK 3 S11: -0.0652 S12: 0.1233 S13: -0.1140
REMARK 3 S21: -0.0618 S22: 0.1576 S23: 0.1532
REMARK 3 S31: 0.0747 S32: -0.1268 S33: -0.0924
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 394 A 465
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0570 12.4410 15.6870
REMARK 3 T TENSOR
REMARK 3 T11: 0.3232 T22: 0.3346
REMARK 3 T33: 0.9025 T12: -0.0362
REMARK 3 T13: -0.0644 T23: 0.4714
REMARK 3 L TENSOR
REMARK 3 L11: 0.3704 L22: 3.8105
REMARK 3 L33: 7.2816 L12: -0.1343
REMARK 3 L13: 1.9632 L23: 0.3761
REMARK 3 S TENSOR
REMARK 3 S11: 0.3100 S12: -0.3085 S13: -0.6580
REMARK 3 S21: 0.3323 S22: 0.4604 S23: -0.0995
REMARK 3 S31: 1.2400 S32: -0.3474 S33: -0.7704
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 3RD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064787.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
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 : RIGAKU VARIMAX
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 : 26708
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 97.5
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1100
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.52300
REMARK 200 R SYM FOR SHELL (I) : 0.52300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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 3NO9, MODIFIED BY CHAINSAW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MOLECULAR DIMENSIONS PACT SCREEN F9:
REMARK 280 200MM NA/K TARTRATE, 100M BISTRISPROPANE PH 6.5, 20% PEG 3350;
REMARK 280 MYSMA.01507.A.A1 PS00681 AT 67.55MG/ML, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 36.24500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.62500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 69.51000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.24500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.62500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.51000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.24500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.62500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.51000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.24500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 52.62500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.51000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -189.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 72.49000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 105.25000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 72.49000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 105.25000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 669 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -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 ALA A 2
REMARK 465 ASP A 3
REMARK 465 THR A 4
REMARK 465 ASP A 5
REMARK 465 VAL A 6
REMARK 465 ASP A 445
REMARK 465 LYS A 446
REMARK 465 ASP A 466
REMARK 465 GLY A 467
REMARK 465 GLU A 468
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 42 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 72 CG CD OE1 OE2
REMARK 470 GLU A 237 CG CD OE1 OE2
REMARK 470 GLU A 394 CG CD OE1 OE2
REMARK 470 ARG A 397 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 399 CG CD1 CD2
REMARK 470 SER A 402 OG
REMARK 470 ILE A 406 CG1 CG2 CD1
REMARK 470 LYS A 424 CG CD CE NZ
REMARK 470 GLN A 425 CG CD OE1 NE2
REMARK 470 LEU A 427 CG CD1 CD2
REMARK 470 LYS A 430 CG CD CE NZ
REMARK 470 LYS A 431 CG CD CE NZ
REMARK 470 ILE A 433 CG1 CG2 CD1
REMARK 470 ARG A 434 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 435 CG CD OE1 NE2
REMARK 470 VAL A 437 CG1 CG2
REMARK 470 ILE A 438 CG1 CG2 CD1
REMARK 470 ARG A 440 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 442 CG CD1 CD2
REMARK 470 ILE A 443 CG1 CG2 CD1
REMARK 470 LEU A 449 CG CD1 CD2
REMARK 470 GLU A 450 CG CD OE1 OE2
REMARK 470 LEU A 452 CG CD1 CD2
REMARK 470 ARG A 454 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 465 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 27 -149.60 -134.15
REMARK 500 ILE A 39 -57.92 -123.57
REMARK 500 ALA A 189 -168.97 -121.98
REMARK 500 THR A 227 -129.67 48.18
REMARK 500 PHE A 354 -119.08 46.18
REMARK 500 VAL A 358 49.82 -106.78
REMARK 500 CYS A 385 -68.50 -134.40
REMARK 500 SER A 405 2.86 -69.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYSMA.01507.A RELATED DB: TARGETDB
DBREF 3RD8 A 1 468 UNP A0R2U8 A0R2U8_MYCS2 1 468
SEQADV 3RD8 MET A -20 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 ALA A -19 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 HIS A -18 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 HIS A -17 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 HIS A -16 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 HIS A -15 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 HIS A -14 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 HIS A -13 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 MET A -12 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 GLY A -11 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 THR A -10 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 LEU A -9 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 GLU A -8 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 ALA A -7 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 GLN A -6 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 THR A -5 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 GLN A -4 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 GLY A -3 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 PRO A -2 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 GLY A -1 UNP A0R2U8 EXPRESSION TAG
SEQADV 3RD8 SER A 0 UNP A0R2U8 EXPRESSION TAG
SEQRES 1 A 489 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 489 ALA GLN THR GLN GLY PRO GLY SER MET ALA ASP THR ASP
SEQRES 3 A 489 VAL GLU TYR ARG ILE GLU HIS ASP THR MET GLY GLU VAL
SEQRES 4 A 489 ARG VAL PRO LYS ASP ALA LEU TRP ARG ALA GLN THR GLN
SEQRES 5 A 489 ARG ALA VAL GLU ASN PHE PRO ILE SER PHE ARG GLY LEU
SEQRES 6 A 489 GLU ARG THR GLN ILE ARG ALA LEU GLY LEU LEU LYS ALA
SEQRES 7 A 489 ALA CYS ALA GLN VAL ASN LYS ASP LEU GLY LEU LEU ASP
SEQRES 8 A 489 PRO GLU LYS ALA ASP ALA ILE ILE ALA ALA ALA GLY GLU
SEQRES 9 A 489 ILE ALA GLU GLY LYS HIS ASP ASP GLN PHE PRO ILE ASP
SEQRES 10 A 489 VAL PHE GLN THR GLY SER GLY THR SER SER ASN MET ASN
SEQRES 11 A 489 THR ASN GLU VAL ILE ALA SER ILE ALA ALA ALA ASN GLY
SEQRES 12 A 489 VAL THR VAL HIS PRO ASN ASP HIS VAL ASN MET SER GLN
SEQRES 13 A 489 SER SER ASN ASP THR PHE PRO THR ALA THR HIS ILE ALA
SEQRES 14 A 489 ALA THR GLU ALA ALA VAL ARG HIS LEU ILE PRO ALA LEU
SEQRES 15 A 489 GLU VAL LEU HIS ALA SER LEU ALA ALA LYS ALA LYS GLN
SEQRES 16 A 489 TRP ARG THR VAL VAL LYS SER GLY ARG THR HIS LEU MET
SEQRES 17 A 489 ASP ALA VAL PRO VAL THR LEU GLY GLN GLU PHE GLY GLY
SEQRES 18 A 489 TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU ARG VAL LYS
SEQRES 19 A 489 ALA THR LEU PRO ARG LEU GLY GLU LEU ALA ILE GLY GLY
SEQRES 20 A 489 THR ALA VAL GLY THR GLY LEU ASN ALA PRO GLU GLY PHE
SEQRES 21 A 489 GLY ALA LYS VAL VAL GLU VAL LEU VAL ASN GLU THR GLY
SEQRES 22 A 489 LEU ALA GLU LEU ARG THR ALA VAL ASP SER PHE GLU ALA
SEQRES 23 A 489 GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA SER GLY ALA
SEQRES 24 A 489 LEU ARG THR ILE ALA VAL SER LEU THR LYS ILE ALA ASN
SEQRES 25 A 489 ASP ILE ARG TRP MET GLY SER GLY PRO LEU THR GLY LEU
SEQRES 26 A 489 ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO GLY SER SER
SEQRES 27 A 489 ILE MET PRO GLY LYS VAL ASN PRO VAL LEU PRO GLU ALA
SEQRES 28 A 489 VAL THR GLN VAL ALA CYS GLN VAL VAL GLY ASN ASP ALA
SEQRES 29 A 489 ALA ILE ALA PHE GLY GLY ALA SER GLY ALA PHE GLU LEU
SEQRES 30 A 489 ASN VAL TYR ILE PRO MET MET ALA ARG ASN LEU LEU GLU
SEQRES 31 A 489 SER PHE THR LEU LEU SER ASN VAL SER ARG LEU PHE ALA
SEQRES 32 A 489 GLU ARG CYS ILE ASP GLY LEU VAL ALA ASN GLU GLU ARG
SEQRES 33 A 489 LEU ARG GLU LEU ALA GLU SER SER PRO SER ILE VAL THR
SEQRES 34 A 489 PRO LEU ASN SER ALA ILE GLY TYR GLU GLU ALA ALA LYS
SEQRES 35 A 489 VAL ALA LYS GLN ALA LEU ALA GLU LYS LYS THR ILE ARG
SEQRES 36 A 489 GLN THR VAL ILE ASP ARG GLY LEU ILE GLY ASP LYS LEU
SEQRES 37 A 489 SER LEU GLU GLU LEU ASP ARG ARG LEU ASP VAL LEU ALA
SEQRES 38 A 489 MET ALA ARG VAL LYS ASP GLY GLU
FORMUL 2 HOH *278(H2 O)
HELIX 1 1 ARG A 27 PHE A 37 1 11
HELIX 2 2 GLU A 45 LEU A 66 1 22
HELIX 3 3 ASP A 70 GLY A 87 1 18
HELIX 4 4 HIS A 89 PHE A 93 5 5
HELIX 5 5 GLY A 103 ASN A 121 1 19
HELIX 6 6 SER A 136 HIS A 156 1 21
HELIX 7 7 HIS A 156 TRP A 175 1 20
HELIX 8 8 LEU A 194 GLY A 220 1 27
HELIX 9 9 GLY A 238 GLY A 252 1 15
HELIX 10 10 PHE A 263 ALA A 268 1 6
HELIX 11 11 ARG A 269 GLY A 297 1 29
HELIX 12 12 PRO A 325 ALA A 350 1 26
HELIX 13 13 TYR A 359 CYS A 385 1 27
HELIX 14 14 ILE A 386 LEU A 389 5 4
HELIX 15 15 ASN A 392 SER A 403 1 12
HELIX 16 16 PRO A 404 PRO A 409 5 6
HELIX 17 17 LEU A 410 LYS A 430 1 21
HELIX 18 18 THR A 432 ARG A 440 1 9
HELIX 19 19 SER A 448 ASP A 457 1 10
HELIX 20 20 ASP A 457 ALA A 462 1 6
SHEET 1 A 2 TYR A 8 ASP A 13 0
SHEET 2 A 2 GLY A 16 PRO A 21 -1 O VAL A 18 N GLU A 11
SHEET 1 B 2 VAL A 179 THR A 184 0
SHEET 2 B 2 MET A 187 THR A 193 -1 O VAL A 192 N LYS A 180
SHEET 1 C 2 GLU A 221 LEU A 222 0
SHEET 2 C 2 ARG A 257 THR A 258 1 O ARG A 257 N LEU A 222
SHEET 1 D 2 ILE A 307 GLN A 308 0
SHEET 2 D 2 VAL A 390 ALA A 391 -1 O VAL A 390 N GLN A 308
CISPEP 1 GLY A 299 PRO A 300 0 4.27
CRYST1 72.490 105.250 139.020 90.00 90.00 90.00 I 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013795 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007193 0.00000
(ATOM LINES ARE NOT SHOWN.)
END