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HEADER HYDROLASE 27-MAY-10 3AJA
TITLE CRYSTAL STRUCTURE OF MSMEG_6394
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 36-337;
COMPND 5 SYNONYM: MSMEG_6394 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 246196;
SOURCE 4 STRAIN: STRAIN ATCC 700084 / MC(2)155;
SOURCE 5 GENE: MSMEG_6394;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28B
KEYWDS ALPHA-BETA HYDROLASE, SERINE ESTERASE, CUTINASE, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.VIVIAN,J.SCOBLE,T.BEDDOE,J.ROSSJOHN
REVDAT 1 11-AUG-10 3AJA 0
JRNL AUTH P.K.CRELLIN,J.P.VIVIAN,J.SCOBLE,F.M.CHOW,N.P.WEST,
JRNL AUTH 2 R.BRAMMANANTH,N.I.PROELLOCKS,A.SHAHINE,J.LE NOURS,
JRNL AUTH 3 M.C.J.WILCE,W.J.BRITTON,R.L.COPPEL,J.ROSSJOHN,T.BEDDOE
JRNL TITL FUNCTIONAL CHARACTERISATION OF A LIPASE ESSENTIAL FOR
JRNL TITL 2 MYCOBACTERIAL VIABILITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 17098
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 932
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 560
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3670
REMARK 3 BIN FREE R VALUE SET COUNT : 34
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3924
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 114.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 103.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18000
REMARK 3 B22 (A**2) : -0.18000
REMARK 3 B33 (A**2) : 0.36000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.355
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.299
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.613
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4025 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5503 ; 1.508 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 521 ; 5.817 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 178 ;35.605 ;25.169
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 589 ;20.035 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.852 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 607 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3160 ; 0.008 ; 0.022
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): 2612 ; 0.462 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4213 ; 0.849 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1413 ; 1.547 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1290 ; 2.401 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1645 ; 0.10 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 1645 ; 0.16 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 250 ; 0.15 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 250 ; 0.96 ; 2.00
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 71 A 334
REMARK 3 ORIGIN FOR THE GROUP (A): 71.1600 31.3820 9.4650
REMARK 3 T TENSOR
REMARK 3 T11: 0.7813 T22: 0.1106
REMARK 3 T33: 0.2797 T12: 0.2494
REMARK 3 T13: 0.0260 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 3.6263 L22: 4.3375
REMARK 3 L33: 3.8462 L12: 1.4158
REMARK 3 L13: 0.5366 L23: 1.3839
REMARK 3 S TENSOR
REMARK 3 S11: 0.3537 S12: 0.4090 S13: -0.1802
REMARK 3 S21: 0.0312 S22: -0.0145 S23: -0.1241
REMARK 3 S31: 0.3975 S32: 0.1190 S33: -0.3392
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 71 B 334
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8390 13.5030 33.5920
REMARK 3 T TENSOR
REMARK 3 T11: 0.5756 T22: 0.2042
REMARK 3 T33: 0.2440 T12: -0.0701
REMARK 3 T13: 0.1115 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 3.5250 L22: 4.2590
REMARK 3 L33: 4.4564 L12: 0.3102
REMARK 3 L13: -0.6713 L23: -0.1466
REMARK 3 S TENSOR
REMARK 3 S11: 0.0480 S12: 0.2430 S13: -0.0098
REMARK 3 S21: 0.1795 S22: -0.0093 S23: 0.4574
REMARK 3 S31: -0.3667 S32: -0.6912 S33: -0.0387
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3AJA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB029320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97941, 0.97930, 0.96411
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20363
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1M SODIUM FORMATE, 0.1M BISTRIS-
REMARK 280 PROPANE, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+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 65.21700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 65.21700
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.76650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 65.21700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.38325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 65.21700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 157.14975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 65.21700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 157.14975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.21700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.38325
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 65.21700
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 65.21700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 104.76650
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 65.21700
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 65.21700
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 104.76650
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 65.21700
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 157.14975
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 65.21700
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 52.38325
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 65.21700
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 52.38325
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 65.21700
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 157.14975
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 65.21700
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 65.21700
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 104.76650
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 36
REMARK 465 ARG A 37
REMARK 465 ARG A 38
REMARK 465 PRO A 39
REMARK 465 ASP A 40
REMARK 465 THR A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 THR A 44
REMARK 465 PRO A 45
REMARK 465 PRO A 46
REMARK 465 PRO A 47
REMARK 465 SER A 48
REMARK 465 ALA A 49
REMARK 465 GLU A 50
REMARK 465 PRO A 51
REMARK 465 PRO A 52
REMARK 465 GLY A 53
REMARK 465 GLY A 54
REMARK 465 VAL A 55
REMARK 465 VAL A 56
REMARK 465 VAL A 57
REMARK 465 PRO A 58
REMARK 465 PRO A 59
REMARK 465 GLY A 60
REMARK 465 THR A 61
REMARK 465 ARG A 62
REMARK 465 LYS A 63
REMARK 465 PRO A 64
REMARK 465 ARG A 65
REMARK 465 PRO A 66
REMARK 465 GLU A 67
REMARK 465 PHE A 68
REMARK 465 GLN A 69
REMARK 465 SER A 70
REMARK 465 SER A 294
REMARK 465 ALA A 295
REMARK 465 ALA A 296
REMARK 465 GLY A 297
REMARK 465 LYS A 335
REMARK 465 HIS A 336
REMARK 465 GLY A 337
REMARK 465 MET B 36
REMARK 465 ARG B 37
REMARK 465 ARG B 38
REMARK 465 PRO B 39
REMARK 465 ASP B 40
REMARK 465 THR B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 THR B 44
REMARK 465 PRO B 45
REMARK 465 PRO B 46
REMARK 465 PRO B 47
REMARK 465 SER B 48
REMARK 465 ALA B 49
REMARK 465 GLU B 50
REMARK 465 PRO B 51
REMARK 465 PRO B 52
REMARK 465 GLY B 53
REMARK 465 GLY B 54
REMARK 465 VAL B 55
REMARK 465 VAL B 56
REMARK 465 VAL B 57
REMARK 465 PRO B 58
REMARK 465 PRO B 59
REMARK 465 GLY B 60
REMARK 465 THR B 61
REMARK 465 ARG B 62
REMARK 465 LYS B 63
REMARK 465 PRO B 64
REMARK 465 ARG B 65
REMARK 465 PRO B 66
REMARK 465 GLU B 67
REMARK 465 PHE B 68
REMARK 465 GLN B 69
REMARK 465 SER B 70
REMARK 465 LYS B 335
REMARK 465 HIS B 336
REMARK 465 GLY B 337
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 O ASP B 72 O HOH B 25 2.00
REMARK 500 CB CYS B 73 SG CYS B 165 2.08
REMARK 500 OD2 ASP A 209 NH2 ARG A 250 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 PRO A 74 C - N - CD ANGL. DEV. = -18.1 DEGREES
REMARK 500 LEU B 244 CA - CB - CG ANGL. DEV. = 13.8 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 72 -65.40 149.98
REMARK 500 ASP A 75 -73.53 -53.50
REMARK 500 THR A 97 -26.95 -140.71
REMARK 500 PHE A 99 75.92 -119.31
REMARK 500 PHE A 131 88.34 -156.33
REMARK 500 SER A 176 -111.94 29.82
REMARK 500 PRO A 222 46.41 -81.71
REMARK 500 SER A 267 105.32 -51.78
REMARK 500 ASN A 283 58.59 -143.26
REMARK 500 LEU A 302 72.71 -104.85
REMARK 500 ASP B 72 -76.24 130.39
REMARK 500 THR B 97 -24.19 -142.82
REMARK 500 LYS B 139 30.22 -91.82
REMARK 500 SER B 176 -112.55 31.42
REMARK 500 PRO B 222 44.12 -83.86
REMARK 500 VAL B 236 107.15 -57.62
REMARK 500 SER B 267 109.25 -54.64
REMARK 500 LEU B 302 25.44 -75.77
REMARK 500 PRO B 306 31.09 -94.99
REMARK 500 ASN B 312 46.57 32.15
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3AJA A 36 337 UNP A0R619 A0R619_MYCS2 36 337
DBREF 3AJA B 36 337 UNP A0R619 A0R619_MYCS2 36 337
SEQRES 1 A 302 MET ARG ARG PRO ASP THR PRO ALA THR PRO PRO PRO SER
SEQRES 2 A 302 ALA GLU PRO PRO GLY GLY VAL VAL VAL PRO PRO GLY THR
SEQRES 3 A 302 ARG LYS PRO ARG PRO GLU PHE GLN SER ALA ASP CYS PRO
SEQRES 4 A 302 ASP VAL MET MET VAL SER ILE PRO GLY THR TRP GLU SER
SEQRES 5 A 302 SER PRO THR ASP ASP PRO PHE ASN PRO THR GLN PHE PRO
SEQRES 6 A 302 LEU SER LEU MET SER ASN ILE SER LYS PRO LEU ALA GLU
SEQRES 7 A 302 GLN PHE GLY PRO ASP ARG LEU GLN VAL TYR THR THR PRO
SEQRES 8 A 302 TYR THR ALA GLN PHE HIS ASN PRO PHE ALA ALA ASP LYS
SEQRES 9 A 302 GLN MET SER TYR ASN ASP SER ARG ALA GLU GLY MET ARG
SEQRES 10 A 302 THR THR VAL LYS ALA MET THR ASP MET ASN ASP ARG CYS
SEQRES 11 A 302 PRO LEU THR SER TYR VAL ILE ALA GLY PHE SER GLN GLY
SEQRES 12 A 302 ALA VAL ILE ALA GLY ASP ILE ALA SER ASP ILE GLY ASN
SEQRES 13 A 302 GLY ARG GLY PRO VAL ASP GLU ASP LEU VAL LEU GLY VAL
SEQRES 14 A 302 THR LEU ILE ALA ASP GLY ARG ARG GLN MET GLY VAL GLY
SEQRES 15 A 302 GLN ASP VAL GLY PRO ASN PRO ALA GLY GLN GLY ALA GLU
SEQRES 16 A 302 ILE THR LEU HIS GLU VAL PRO ALA LEU SER ALA LEU GLY
SEQRES 17 A 302 LEU THR MET THR GLY PRO ARG PRO GLY GLY PHE GLY ALA
SEQRES 18 A 302 LEU ASP ASN ARG THR ASN GLN ILE CYS GLY SER GLY ASP
SEQRES 19 A 302 LEU ILE CYS SER ALA PRO GLU GLN ALA PHE SER VAL PHE
SEQRES 20 A 302 ASN LEU PRO LYS THR LEU GLU THR LEU SER GLY SER ALA
SEQRES 21 A 302 ALA GLY PRO VAL HIS ALA LEU TYR ASN THR PRO GLN PHE
SEQRES 22 A 302 TRP VAL GLU ASN GLY GLN THR ALA THR GLN TRP THR LEU
SEQRES 23 A 302 GLU TRP ALA ARG ASN LEU VAL GLU ASN ALA PRO HIS PRO
SEQRES 24 A 302 LYS HIS GLY
SEQRES 1 B 302 MET ARG ARG PRO ASP THR PRO ALA THR PRO PRO PRO SER
SEQRES 2 B 302 ALA GLU PRO PRO GLY GLY VAL VAL VAL PRO PRO GLY THR
SEQRES 3 B 302 ARG LYS PRO ARG PRO GLU PHE GLN SER ALA ASP CYS PRO
SEQRES 4 B 302 ASP VAL MET MET VAL SER ILE PRO GLY THR TRP GLU SER
SEQRES 5 B 302 SER PRO THR ASP ASP PRO PHE ASN PRO THR GLN PHE PRO
SEQRES 6 B 302 LEU SER LEU MET SER ASN ILE SER LYS PRO LEU ALA GLU
SEQRES 7 B 302 GLN PHE GLY PRO ASP ARG LEU GLN VAL TYR THR THR PRO
SEQRES 8 B 302 TYR THR ALA GLN PHE HIS ASN PRO PHE ALA ALA ASP LYS
SEQRES 9 B 302 GLN MET SER TYR ASN ASP SER ARG ALA GLU GLY MET ARG
SEQRES 10 B 302 THR THR VAL LYS ALA MET THR ASP MET ASN ASP ARG CYS
SEQRES 11 B 302 PRO LEU THR SER TYR VAL ILE ALA GLY PHE SER GLN GLY
SEQRES 12 B 302 ALA VAL ILE ALA GLY ASP ILE ALA SER ASP ILE GLY ASN
SEQRES 13 B 302 GLY ARG GLY PRO VAL ASP GLU ASP LEU VAL LEU GLY VAL
SEQRES 14 B 302 THR LEU ILE ALA ASP GLY ARG ARG GLN MET GLY VAL GLY
SEQRES 15 B 302 GLN ASP VAL GLY PRO ASN PRO ALA GLY GLN GLY ALA GLU
SEQRES 16 B 302 ILE THR LEU HIS GLU VAL PRO ALA LEU SER ALA LEU GLY
SEQRES 17 B 302 LEU THR MET THR GLY PRO ARG PRO GLY GLY PHE GLY ALA
SEQRES 18 B 302 LEU ASP ASN ARG THR ASN GLN ILE CYS GLY SER GLY ASP
SEQRES 19 B 302 LEU ILE CYS SER ALA PRO GLU GLN ALA PHE SER VAL PHE
SEQRES 20 B 302 ASN LEU PRO LYS THR LEU GLU THR LEU SER GLY SER ALA
SEQRES 21 B 302 ALA GLY PRO VAL HIS ALA LEU TYR ASN THR PRO GLN PHE
SEQRES 22 B 302 TRP VAL GLU ASN GLY GLN THR ALA THR GLN TRP THR LEU
SEQRES 23 B 302 GLU TRP ALA ARG ASN LEU VAL GLU ASN ALA PRO HIS PRO
SEQRES 24 B 302 LYS HIS GLY
FORMUL 3 HOH *32(H2 O)
HELIX 1 1 MET A 104 PHE A 115 1 12
HELIX 2 2 SER A 142 CYS A 165 1 24
HELIX 3 3 SER A 176 ASN A 191 1 16
HELIX 4 4 ASP A 197 ASP A 199 5 3
HELIX 5 5 GLY A 228 LEU A 233 1 6
HELIX 6 6 VAL A 236 LEU A 242 1 7
HELIX 7 7 PHE A 254 ASP A 258 5 5
HELIX 8 8 PRO A 275 PHE A 279 5 5
HELIX 9 9 ASN A 283 GLY A 293 1 11
HELIX 10 10 ALA A 316 ALA A 331 1 16
HELIX 11 11 MET B 104 PHE B 115 1 12
HELIX 12 12 SER B 142 CYS B 165 1 24
HELIX 13 13 SER B 176 ASN B 191 1 16
HELIX 14 14 ASP B 197 ASP B 199 5 3
HELIX 15 15 GLY B 228 LEU B 233 1 6
HELIX 16 16 VAL B 236 LEU B 242 1 7
HELIX 17 17 PHE B 254 ASP B 258 5 5
HELIX 18 18 PRO B 275 PHE B 279 5 5
HELIX 19 19 ASN B 283 GLY B 293 1 11
HELIX 20 20 GLY B 297 LEU B 302 1 6
HELIX 21 21 TYR B 303 THR B 305 5 3
HELIX 22 22 ALA B 316 ALA B 331 1 16
SHEET 1 A 6 LEU A 120 THR A 124 0
SHEET 2 A 6 VAL A 76 ILE A 81 1 N MET A 78 O GLN A 121
SHEET 3 A 6 SER A 169 PHE A 175 1 O SER A 169 N MET A 77
SHEET 4 A 6 VAL A 201 ILE A 207 1 O ILE A 207 N GLY A 174
SHEET 5 A 6 THR A 261 ILE A 264 1 O ASN A 262 N VAL A 204
SHEET 6 A 6 GLN A 218 ASP A 219 1 N GLN A 218 O THR A 261
SHEET 1 B 2 VAL A 310 GLU A 311 0
SHEET 2 B 2 GLN A 314 THR A 315 -1 O GLN A 314 N GLU A 311
SHEET 1 C 6 LEU B 120 THR B 124 0
SHEET 2 C 6 VAL B 76 ILE B 81 1 N MET B 78 O TYR B 123
SHEET 3 C 6 SER B 169 PHE B 175 1 O SER B 169 N MET B 77
SHEET 4 C 6 VAL B 201 ILE B 207 1 O LEU B 202 N TYR B 170
SHEET 5 C 6 THR B 261 ILE B 264 1 O ASN B 262 N VAL B 204
SHEET 6 C 6 GLN B 218 ASP B 219 1 N GLN B 218 O THR B 261
SHEET 1 D 2 VAL B 310 GLU B 311 0
SHEET 2 D 2 GLN B 314 THR B 315 -1 O GLN B 314 N GLU B 311
SSBOND 1 CYS A 73 CYS A 165 1555 1555 1.60
SSBOND 2 CYS A 265 CYS A 272 1555 1555 2.05
SSBOND 3 CYS B 73 CYS B 165 1555 1555 2.11
SSBOND 4 CYS B 265 CYS B 272 1555 1555 2.11
CISPEP 1 GLY A 194 PRO A 195 0 1.27
CISPEP 2 GLY B 194 PRO B 195 0 1.43
CRYST1 130.434 130.434 209.533 90.00 90.00 90.00 I 41 2 2 32
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 0.007667 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007667 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004773 0.00000
TER 1953 PRO A 334
TER 3926 PRO B 334
MASTER 490 0 0 22 16 0 0 6 3956 2 8 48
END |