| content |
HEADER IMMUNE SYSTEM 23-OCT-03 1R88
TITLE THE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS MPT51
TITLE 2 (FBPC1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MPT51/MPB51 ANTIGEN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FIBRONECTIN-BINDING PROTEIN C1 (FBPC1, MPT51);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: FBPC1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS MYCOBACTERIUM TUBERCULOSIS, ALFA/BETA HYDROLASE FOLD,
KEYWDS 2 ANTIGEN 85, MPT51, FBPC1
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.WILSON,W.N.MAUGHAN,L.KREMER,G.S.BESRA,K.FUTTERER
REVDAT 1 30-DEC-03 1R88 0
JRNL AUTH R.A.WILSON,W.N.MAUGHAN,L.KREMER,G.S.BESRA,
JRNL AUTH 2 K.FUTTERER
JRNL TITL THE STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS MPT51
JRNL TITL 2 (FBPC1) DEFINES A NEW FAMILY OF NON-CATALYTIC
JRNL TITL 3 ALPHA/BETA HYDROLASES
JRNL REF J.MOL.BIOL. V. 335 519 2004
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 69287
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3668
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.71
REMARK 3 BIN RESOLUTION RANGE LOW : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8757
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 472
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4336
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.12000
REMARK 3 B22 (A**2) : -1.31000
REMARK 3 B33 (A**2) : -1.81000
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): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.164
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4070 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3424 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5562 ; 0.955 ; 1.899
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7938 ; 0.753 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 5.347 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 546 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4798 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 882 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 851 ; 0.182 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4006 ; 0.222 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2008 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 285 ; 0.117 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 8 ; 0.291 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 61 ; 0.185 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 31 ; 0.193 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 2626 ; 0.173 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4116 ; 0.329 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1444 ; 0.610 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1446 ; 0.919 ; 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 : 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 5 A 281 6
REMARK 3 1 B 5 B 281 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 3430 ; 0.06 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 3430 ; 0.21 ; 10.00
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 5 A 281
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4889 32.2448 29.0048
REMARK 3 T TENSOR
REMARK 3 T11: 0.0023 T22: 0.0485
REMARK 3 T33: 0.0574 T12: 0.0106
REMARK 3 T13: -0.0024 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.8557 L22: 1.6357
REMARK 3 L33: 0.8622 L12: -0.3689
REMARK 3 L13: -0.2751 L23: 0.0959
REMARK 3 S TENSOR
REMARK 3 S11: -0.0359 S12: -0.0233 S13: -0.0655
REMARK 3 S21: 0.0120 S22: 0.0171 S23: 0.0011
REMARK 3 S31: 0.0873 S32: 0.0316 S33: 0.0188
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 5 B 281
REMARK 3 ORIGIN FOR THE GROUP (A): 47.0994 2.1454 60.0301
REMARK 3 T TENSOR
REMARK 3 T11: 0.0109 T22: 0.0510
REMARK 3 T33: 0.0630 T12: -0.0083
REMARK 3 T13: -0.0074 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.7531 L22: 0.8626
REMARK 3 L33: 1.6703 L12: 0.1958
REMARK 3 L13: 0.3316 L23: 0.0916
REMARK 3 S TENSOR
REMARK 3 S11: -0.0335 S12: 0.0776 S13: 0.0060
REMARK 3 S21: -0.0958 S22: 0.0304 S23: 0.0206
REMARK 3 S31: 0.0080 S32: -0.0160 S33: 0.0032
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3 RIDING POSITIONS
REMARK 4
REMARK 4 1R88 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-OCT-2003.
REMARK 100 THE RCSB ID CODE IS RCSB020558.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78268
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07700
REMARK 200 FOR THE DATA SET : 22.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48900
REMARK 200 FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 29.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.45000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 26
REMARK 465 ALA A 27
REMARK 465 GLU A 28
REMARK 465 PRO A 29
REMARK 465 THR A 30
REMARK 465 ALA A 31
REMARK 465 LYS A 32
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 MET B 26
REMARK 465 ALA B 27
REMARK 465 GLU B 28
REMARK 465 PRO B 29
REMARK 465 THR B 30
REMARK 465 ALA B 31
REMARK 465 LYS B 32
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 242 O HOH 264 4456 2.15
REMARK 500 O HOH 227 O HOH 299 4556 2.18
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 168 SD MET A 168 CE -0.046
REMARK 500 MET A 250 SD MET A 250 CE -0.053
REMARK 500 MET A 290 CG MET A 290 SD 0.047
REMARK 500 MET B 168 SD MET B 168 CE -0.048
REMARK 500 MET B 255 SD MET B 255 CE -0.039
REMARK 500 MET B 290 CG MET B 290 SD 0.048
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 M RES CSSEQI PSI PHI
REMARK 500 ALA A 145 -114.74 56.75
REMARK 500 ALA B 145 -114.38 58.34
DBREF 1R88 A 27 299 SWS Q48923 MP51_MYCTU 27 299
DBREF 1R88 B 27 299 SWS Q48923 MP51_MYCTU 27 299
SEQADV 1R88 MET A 26 SWS Q48923 INITIATING MET
SEQADV 1R88 HIS A 300 SWS Q48923 HIS TAG
SEQADV 1R88 HIS A 301 SWS Q48923 HIS TAG
SEQADV 1R88 HIS A 302 SWS Q48923 HIS TAG
SEQADV 1R88 HIS A 303 SWS Q48923 HIS TAG
SEQADV 1R88 HIS A 304 SWS Q48923 HIS TAG
SEQADV 1R88 HIS A 305 SWS Q48923 HIS TAG
SEQADV 1R88 MET B 26 SWS Q48923 INITIATING MET
SEQADV 1R88 HIS B 300 SWS Q48923 HIS TAG
SEQADV 1R88 HIS B 301 SWS Q48923 HIS TAG
SEQADV 1R88 HIS B 302 SWS Q48923 HIS TAG
SEQADV 1R88 HIS B 303 SWS Q48923 HIS TAG
SEQADV 1R88 HIS B 304 SWS Q48923 HIS TAG
SEQADV 1R88 HIS B 305 SWS Q48923 HIS TAG
SEQRES 1 A 280 MET ALA GLU PRO THR ALA LYS ALA ALA PRO TYR GLU ASN
SEQRES 2 A 280 LEU MET VAL PRO SER PRO SER MET GLY ARG ASP ILE PRO
SEQRES 3 A 280 VAL ALA PHE LEU ALA GLY GLY PRO HIS ALA VAL TYR LEU
SEQRES 4 A 280 LEU ASP ALA PHE ASN ALA GLY PRO ASP VAL SER ASN TRP
SEQRES 5 A 280 VAL THR ALA GLY ASN ALA MET ASN THR LEU ALA GLY LYS
SEQRES 6 A 280 GLY ILE SER VAL VAL ALA PRO ALA GLY GLY ALA TYR SER
SEQRES 7 A 280 MET TYR THR ASN TRP GLU GLN ASP GLY SER LYS GLN TRP
SEQRES 8 A 280 ASP THR PHE LEU SER ALA GLU LEU PRO ASP TRP LEU ALA
SEQRES 9 A 280 ALA ASN ARG GLY LEU ALA PRO GLY GLY HIS ALA ALA VAL
SEQRES 10 A 280 GLY ALA ALA GLN GLY GLY TYR GLY ALA MET ALA LEU ALA
SEQRES 11 A 280 ALA PHE HIS PRO ASP ARG PHE GLY PHE ALA GLY SER MET
SEQRES 12 A 280 SER GLY PHE LEU TYR PRO SER ASN THR THR THR ASN GLY
SEQRES 13 A 280 ALA ILE ALA ALA GLY MET GLN GLN PHE GLY GLY VAL ASP
SEQRES 14 A 280 THR ASN GLY MET TRP GLY ALA PRO GLN LEU GLY ARG TRP
SEQRES 15 A 280 LYS TRP HIS ASP PRO TRP VAL HIS ALA SER LEU LEU ALA
SEQRES 16 A 280 GLN ASN ASN THR ARG VAL TRP VAL TRP SER PRO THR ASN
SEQRES 17 A 280 PRO GLY ALA SER ASP PRO ALA ALA MET ILE GLY GLN ALA
SEQRES 18 A 280 ALA GLU ALA MET GLY ASN SER ARG MET PHE TYR ASN GLN
SEQRES 19 A 280 TYR ARG SER VAL GLY GLY HIS ASN GLY HIS PHE ASP PHE
SEQRES 20 A 280 PRO ALA SER GLY ASP ASN GLY TRP GLY SER TRP ALA PRO
SEQRES 21 A 280 GLN LEU GLY ALA MET SER GLY ASP ILE VAL GLY ALA ILE
SEQRES 22 A 280 ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 B 280 MET ALA GLU PRO THR ALA LYS ALA ALA PRO TYR GLU ASN
SEQRES 2 B 280 LEU MET VAL PRO SER PRO SER MET GLY ARG ASP ILE PRO
SEQRES 3 B 280 VAL ALA PHE LEU ALA GLY GLY PRO HIS ALA VAL TYR LEU
SEQRES 4 B 280 LEU ASP ALA PHE ASN ALA GLY PRO ASP VAL SER ASN TRP
SEQRES 5 B 280 VAL THR ALA GLY ASN ALA MET ASN THR LEU ALA GLY LYS
SEQRES 6 B 280 GLY ILE SER VAL VAL ALA PRO ALA GLY GLY ALA TYR SER
SEQRES 7 B 280 MET TYR THR ASN TRP GLU GLN ASP GLY SER LYS GLN TRP
SEQRES 8 B 280 ASP THR PHE LEU SER ALA GLU LEU PRO ASP TRP LEU ALA
SEQRES 9 B 280 ALA ASN ARG GLY LEU ALA PRO GLY GLY HIS ALA ALA VAL
SEQRES 10 B 280 GLY ALA ALA GLN GLY GLY TYR GLY ALA MET ALA LEU ALA
SEQRES 11 B 280 ALA PHE HIS PRO ASP ARG PHE GLY PHE ALA GLY SER MET
SEQRES 12 B 280 SER GLY PHE LEU TYR PRO SER ASN THR THR THR ASN GLY
SEQRES 13 B 280 ALA ILE ALA ALA GLY MET GLN GLN PHE GLY GLY VAL ASP
SEQRES 14 B 280 THR ASN GLY MET TRP GLY ALA PRO GLN LEU GLY ARG TRP
SEQRES 15 B 280 LYS TRP HIS ASP PRO TRP VAL HIS ALA SER LEU LEU ALA
SEQRES 16 B 280 GLN ASN ASN THR ARG VAL TRP VAL TRP SER PRO THR ASN
SEQRES 17 B 280 PRO GLY ALA SER ASP PRO ALA ALA MET ILE GLY GLN ALA
SEQRES 18 B 280 ALA GLU ALA MET GLY ASN SER ARG MET PHE TYR ASN GLN
SEQRES 19 B 280 TYR ARG SER VAL GLY GLY HIS ASN GLY HIS PHE ASP PHE
SEQRES 20 B 280 PRO ALA SER GLY ASP ASN GLY TRP GLY SER TRP ALA PRO
SEQRES 21 B 280 GLN LEU GLY ALA MET SER GLY ASP ILE VAL GLY ALA ILE
SEQRES 22 B 280 ARG HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *400(H2 O1)
HELIX 1 1 SER A 75 ALA A 80 1 6
HELIX 2 2 ASN A 82 ALA A 88 1 7
HELIX 3 3 GLN A 115 ALA A 122 1 8
HELIX 4 4 ALA A 122 ARG A 132 1 11
HELIX 5 5 ALA A 145 HIS A 158 1 14
HELIX 6 6 ASN A 176 GLY A 192 1 17
HELIX 7 7 THR A 195 GLY A 200 1 6
HELIX 8 8 ALA A 201 GLY A 205 5 5
HELIX 9 9 TRP A 207 ASP A 211 5 5
HELIX 10 10 HIS A 215 ASN A 222 1 8
HELIX 11 11 ASP A 238 ILE A 243 5 6
HELIX 12 12 GLN A 245 VAL A 263 1 19
HELIX 13 13 GLY A 279 ARG A 299 1 21
HELIX 14 14 SER B 75 ALA B 80 1 6
HELIX 15 15 ASN B 82 ALA B 88 1 7
HELIX 16 16 TRP B 116 ALA B 122 1 7
HELIX 17 17 ALA B 122 ARG B 132 1 11
HELIX 18 18 ALA B 145 HIS B 158 1 14
HELIX 19 19 ASN B 176 GLY B 192 1 17
HELIX 20 20 THR B 195 GLY B 200 1 6
HELIX 21 21 ALA B 201 ASP B 211 5 11
HELIX 22 22 HIS B 215 ASN B 222 1 8
HELIX 23 23 ASP B 238 ILE B 243 5 6
HELIX 24 24 GLN B 245 VAL B 263 1 19
HELIX 25 25 GLY B 279 ARG B 299 1 21
SHEET 1 A 8 GLU A 37 SER A 43 0
SHEET 2 A 8 ARG A 48 LEU A 55 -1 O ILE A 50 N VAL A 41
SHEET 3 A 8 SER A 93 PRO A 97 -1 O ALA A 96 N ALA A 53
SHEET 4 A 8 ALA A 61 LEU A 65 1 N VAL A 62 O VAL A 95
SHEET 5 A 8 HIS A 139 ALA A 144 1 O ALA A 140 N TYR A 63
SHEET 6 A 8 PHE A 162 MET A 168 1 O GLY A 166 N ALA A 141
SHEET 7 A 8 ARG A 225 TRP A 229 1 O TRP A 229 N SER A 167
SHEET 8 A 8 GLY A 268 ASP A 271 1 O HIS A 269 N VAL A 228
SHEET 1 B 8 GLU B 37 SER B 43 0
SHEET 2 B 8 ARG B 48 LEU B 55 -1 O ILE B 50 N VAL B 41
SHEET 3 B 8 SER B 93 PRO B 97 -1 O ALA B 96 N ALA B 53
SHEET 4 B 8 ALA B 61 LEU B 65 1 N VAL B 62 O VAL B 95
SHEET 5 B 8 HIS B 139 ALA B 144 1 O ALA B 140 N TYR B 63
SHEET 6 B 8 PHE B 162 MET B 168 1 O GLY B 166 N ALA B 141
SHEET 7 B 8 ARG B 225 TRP B 229 1 O TRP B 227 N SER B 167
SHEET 8 B 8 GLY B 268 ASP B 271 1 O HIS B 269 N VAL B 228
SHEET 1 C 2 ASN B 107 TRP B 108 0
SHEET 2 C 2 ASP B 111 GLN B 115 -1 O LYS B 114 N TRP B 108
CRYST1 59.900 108.900 109.800 90.00 90.00 90.00 P 21 21 21 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 0.016694 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009183 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009107 0.00000
TER 1969 ARG A 299
TER 3938 ARG B 299
MASTER 357 0 0 25 18 0 0 6 4336 2 0 44
END |