HEADER LIGASE 22-DEC-08 3FMI
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS DETHIOBIOTIN
TITLE 2 SYNTHETASE COMPLEXED WITH 7-KETO 8-AMINOPELARGONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DETHIOBIOTIN SYNTHETASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DTB SYNTHETASE, DTBS;
COMPND 5 EC: 6.3.3.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: BIOD, MT1621, MTCY336.33C, RV1570;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS RV1570, BIOD, LIGASE, ATP-BINDING, BIOTIN BIOSYNTHESIS, MAGNESIUM,
KEYWDS 2 NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DEY,J.C.SACCHETTINI
REVDAT 3 06-SEP-23 3FMI 1 REMARK SEQADV LINK
REVDAT 2 25-AUG-10 3FMI 1 JRNL
REVDAT 1 30-JUN-09 3FMI 0
JRNL AUTH S.DEY,J.M.LANE,R.E.LEE,E.J.RUBIN,J.C.SACCHETTINI
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS BIOTIN BIOSYNTHESIS ENZYMES
JRNL TITL 3 7,8-DIAMINOPELARGONIC ACID SYNTHASE AND DETHIOBIOTIN
JRNL TITL 4 SYNTHETASE .
JRNL REF BIOCHEMISTRY V. 49 6746 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20565114
JRNL DOI 10.1021/BI902097J
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 43644
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2323
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) : 2.18
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3087
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 168
REMARK 3 BIN FREE R VALUE : 0.3700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6328
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.93000
REMARK 3 B22 (A**2) : 1.01000
REMARK 3 B33 (A**2) : -1.94000
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): 0.296
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.230
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.688
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6462 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8834 ; 1.471 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 902 ; 6.122 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 205 ;35.318 ;23.366
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 927 ;19.368 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;18.636 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1109 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4795 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2858 ; 0.224 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4405 ; 0.315 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 544 ; 0.188 ; 0.500
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): 61 ; 0.224 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.241 ; 0.500
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): 4575 ; 2.811 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7100 ; 4.046 ; 7.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2050 ; 5.563 ; 9.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1734 ; 7.052 ;11.000
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 : NULL
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 3FMI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000050772.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46066
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.330
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 3FGN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.68600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.78450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.56850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.78450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.68600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.56850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 3250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 -24
REMARK 465 GLY A -23
REMARK 465 SER A -22
REMARK 465 SER A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 LEU A -11
REMARK 465 GLN A -10
REMARK 465 GLY A -9
REMARK 465 THR A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 MET B -24
REMARK 465 GLY B -23
REMARK 465 SER B -22
REMARK 465 SER B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 LEU B -11
REMARK 465 GLN B -10
REMARK 465 GLY B -9
REMARK 465 THR B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLY B 226
REMARK 465 MET C -24
REMARK 465 GLY C -23
REMARK 465 SER C -22
REMARK 465 SER C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 SER C -14
REMARK 465 SER C -13
REMARK 465 GLY C -12
REMARK 465 LEU C -11
REMARK 465 GLN C -10
REMARK 465 GLY C -9
REMARK 465 THR C -8
REMARK 465 GLU C -7
REMARK 465 ASN C -6
REMARK 465 LEU C -5
REMARK 465 TYR C -4
REMARK 465 PHE C -3
REMARK 465 GLN C -2
REMARK 465 GLY C 226
REMARK 465 MET D -24
REMARK 465 GLY D -23
REMARK 465 SER D -22
REMARK 465 SER D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 SER D -14
REMARK 465 SER D -13
REMARK 465 GLY D -12
REMARK 465 LEU D -11
REMARK 465 GLN D -10
REMARK 465 GLY D -9
REMARK 465 THR D -8
REMARK 465 GLU D -7
REMARK 465 ASN D -6
REMARK 465 LEU D -5
REMARK 465 TYR D -4
REMARK 465 PHE D -3
REMARK 465 GLN D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 GLY D 226
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 193 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG D 125 NE - CZ - NH2 ANGL. DEV. = -3.3 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 LEU A 65 -78.72 -146.18
REMARK 500 ALA B 84 167.66 -48.03
REMARK 500 PRO B 86 173.91 -58.29
REMARK 500 MET C 1 128.24 -21.17
REMARK 500 LEU C 65 -78.77 -140.93
REMARK 500 LEU C 143 117.64 -31.61
REMARK 500 PRO C 174 -103.31 -14.28
REMARK 500 ALA D 84 168.01 -48.73
REMARK 500 PRO D 101 126.39 -35.36
REMARK 500 PRO D 175 -138.07 -55.54
REMARK 500 ALA D 200 -56.41 -20.67
REMARK 500 ALA D 201 -4.89 -52.31
REMARK 500 ALA D 205 -66.21 169.71
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 SO4 A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAP A 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAP B 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAP C 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 252
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FGN RELATED DB: PDB
REMARK 900 STRUCTURE OF DETHIOBIOTIN SYNTHETASE FROM MYCOBACTERIUM TUBERCULOSIS
REMARK 900 RELATED ID: 3FMF RELATED DB: PDB
DBREF 3FMI A 1 226 UNP O06620 BIOD_MYCTU 1 226
DBREF 3FMI B 1 226 UNP O06620 BIOD_MYCTU 1 226
DBREF 3FMI C 1 226 UNP O06620 BIOD_MYCTU 1 226
DBREF 3FMI D 1 226 UNP O06620 BIOD_MYCTU 1 226
SEQADV 3FMI MET A -24 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY A -23 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER A -22 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER A -21 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS A -20 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS A -19 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS A -18 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS A -17 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS A -16 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS A -15 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER A -14 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER A -13 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY A -12 UNP O06620 EXPRESSION TAG
SEQADV 3FMI LEU A -11 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLN A -10 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY A -9 UNP O06620 EXPRESSION TAG
SEQADV 3FMI THR A -8 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLU A -7 UNP O06620 EXPRESSION TAG
SEQADV 3FMI ASN A -6 UNP O06620 EXPRESSION TAG
SEQADV 3FMI LEU A -5 UNP O06620 EXPRESSION TAG
SEQADV 3FMI TYR A -4 UNP O06620 EXPRESSION TAG
SEQADV 3FMI PHE A -3 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLN A -2 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER A -1 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS A 0 UNP O06620 EXPRESSION TAG
SEQADV 3FMI MET B -24 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY B -23 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER B -22 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER B -21 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS B -20 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS B -19 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS B -18 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS B -17 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS B -16 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS B -15 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER B -14 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER B -13 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY B -12 UNP O06620 EXPRESSION TAG
SEQADV 3FMI LEU B -11 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLN B -10 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY B -9 UNP O06620 EXPRESSION TAG
SEQADV 3FMI THR B -8 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLU B -7 UNP O06620 EXPRESSION TAG
SEQADV 3FMI ASN B -6 UNP O06620 EXPRESSION TAG
SEQADV 3FMI LEU B -5 UNP O06620 EXPRESSION TAG
SEQADV 3FMI TYR B -4 UNP O06620 EXPRESSION TAG
SEQADV 3FMI PHE B -3 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLN B -2 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER B -1 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS B 0 UNP O06620 EXPRESSION TAG
SEQADV 3FMI MET C -24 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY C -23 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER C -22 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER C -21 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS C -20 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS C -19 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS C -18 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS C -17 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS C -16 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS C -15 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER C -14 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER C -13 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY C -12 UNP O06620 EXPRESSION TAG
SEQADV 3FMI LEU C -11 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLN C -10 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY C -9 UNP O06620 EXPRESSION TAG
SEQADV 3FMI THR C -8 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLU C -7 UNP O06620 EXPRESSION TAG
SEQADV 3FMI ASN C -6 UNP O06620 EXPRESSION TAG
SEQADV 3FMI LEU C -5 UNP O06620 EXPRESSION TAG
SEQADV 3FMI TYR C -4 UNP O06620 EXPRESSION TAG
SEQADV 3FMI PHE C -3 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLN C -2 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER C -1 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS C 0 UNP O06620 EXPRESSION TAG
SEQADV 3FMI MET D -24 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY D -23 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER D -22 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER D -21 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS D -20 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS D -19 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS D -18 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS D -17 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS D -16 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS D -15 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER D -14 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER D -13 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY D -12 UNP O06620 EXPRESSION TAG
SEQADV 3FMI LEU D -11 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLN D -10 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLY D -9 UNP O06620 EXPRESSION TAG
SEQADV 3FMI THR D -8 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLU D -7 UNP O06620 EXPRESSION TAG
SEQADV 3FMI ASN D -6 UNP O06620 EXPRESSION TAG
SEQADV 3FMI LEU D -5 UNP O06620 EXPRESSION TAG
SEQADV 3FMI TYR D -4 UNP O06620 EXPRESSION TAG
SEQADV 3FMI PHE D -3 UNP O06620 EXPRESSION TAG
SEQADV 3FMI GLN D -2 UNP O06620 EXPRESSION TAG
SEQADV 3FMI SER D -1 UNP O06620 EXPRESSION TAG
SEQADV 3FMI HIS D 0 UNP O06620 EXPRESSION TAG
SEQRES 1 A 251 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 251 LEU GLN GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET
SEQRES 3 A 251 THR ILE LEU VAL VAL THR GLY THR GLY THR GLY VAL GLY
SEQRES 4 A 251 LYS THR VAL VAL CYS ALA ALA LEU ALA SER ALA ALA ARG
SEQRES 5 A 251 GLN ALA GLY ILE ASP VAL ALA VAL CYS LYS PRO VAL GLN
SEQRES 6 A 251 THR GLY THR ALA ARG GLY ASP ASP ASP LEU ALA GLU VAL
SEQRES 7 A 251 GLY ARG LEU ALA GLY VAL THR GLN LEU ALA GLY LEU ALA
SEQRES 8 A 251 ARG TYR PRO GLN PRO MET ALA PRO ALA ALA ALA ALA GLU
SEQRES 9 A 251 HIS ALA GLY MET ALA LEU PRO ALA ARG ASP GLN ILE VAL
SEQRES 10 A 251 ARG LEU ILE ALA ASP LEU ASP ARG PRO GLY ARG LEU THR
SEQRES 11 A 251 LEU VAL GLU GLY ALA GLY GLY LEU LEU VAL GLU LEU ALA
SEQRES 12 A 251 GLU PRO GLY VAL THR LEU ARG ASP VAL ALA VAL ASP VAL
SEQRES 13 A 251 ALA ALA ALA ALA LEU VAL VAL VAL THR ALA ASP LEU GLY
SEQRES 14 A 251 THR LEU ASN HIS THR LYS LEU THR LEU GLU ALA LEU ALA
SEQRES 15 A 251 ALA GLN GLN VAL SER CSX ALA GLY LEU VAL ILE GLY SER
SEQRES 16 A 251 TRP PRO ASP PRO PRO GLY LEU VAL ALA ALA SER ASN ARG
SEQRES 17 A 251 SER ALA LEU ALA ARG ILE ALA MET VAL ARG ALA ALA LEU
SEQRES 18 A 251 PRO ALA GLY ALA ALA SER LEU ASP ALA GLY ASP PHE ALA
SEQRES 19 A 251 ALA MET SER ALA ALA ALA PHE ASP ARG ASN TRP VAL ALA
SEQRES 20 A 251 GLY LEU VAL GLY
SEQRES 1 B 251 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 251 LEU GLN GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET
SEQRES 3 B 251 THR ILE LEU VAL VAL THR GLY THR GLY THR GLY VAL GLY
SEQRES 4 B 251 LYS THR VAL VAL CYS ALA ALA LEU ALA SER ALA ALA ARG
SEQRES 5 B 251 GLN ALA GLY ILE ASP VAL ALA VAL CYS LYS PRO VAL GLN
SEQRES 6 B 251 THR GLY THR ALA ARG GLY ASP ASP ASP LEU ALA GLU VAL
SEQRES 7 B 251 GLY ARG LEU ALA GLY VAL THR GLN LEU ALA GLY LEU ALA
SEQRES 8 B 251 ARG TYR PRO GLN PRO MET ALA PRO ALA ALA ALA ALA GLU
SEQRES 9 B 251 HIS ALA GLY MET ALA LEU PRO ALA ARG ASP GLN ILE VAL
SEQRES 10 B 251 ARG LEU ILE ALA ASP LEU ASP ARG PRO GLY ARG LEU THR
SEQRES 11 B 251 LEU VAL GLU GLY ALA GLY GLY LEU LEU VAL GLU LEU ALA
SEQRES 12 B 251 GLU PRO GLY VAL THR LEU ARG ASP VAL ALA VAL ASP VAL
SEQRES 13 B 251 ALA ALA ALA ALA LEU VAL VAL VAL THR ALA ASP LEU GLY
SEQRES 14 B 251 THR LEU ASN HIS THR LYS LEU THR LEU GLU ALA LEU ALA
SEQRES 15 B 251 ALA GLN GLN VAL SER CSX ALA GLY LEU VAL ILE GLY SER
SEQRES 16 B 251 TRP PRO ASP PRO PRO GLY LEU VAL ALA ALA SER ASN ARG
SEQRES 17 B 251 SER ALA LEU ALA ARG ILE ALA MET VAL ARG ALA ALA LEU
SEQRES 18 B 251 PRO ALA GLY ALA ALA SER LEU ASP ALA GLY ASP PHE ALA
SEQRES 19 B 251 ALA MET SER ALA ALA ALA PHE ASP ARG ASN TRP VAL ALA
SEQRES 20 B 251 GLY LEU VAL GLY
SEQRES 1 C 251 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 251 LEU GLN GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET
SEQRES 3 C 251 THR ILE LEU VAL VAL THR GLY THR GLY THR GLY VAL GLY
SEQRES 4 C 251 LYS THR VAL VAL CYS ALA ALA LEU ALA SER ALA ALA ARG
SEQRES 5 C 251 GLN ALA GLY ILE ASP VAL ALA VAL CYS LYS PRO VAL GLN
SEQRES 6 C 251 THR GLY THR ALA ARG GLY ASP ASP ASP LEU ALA GLU VAL
SEQRES 7 C 251 GLY ARG LEU ALA GLY VAL THR GLN LEU ALA GLY LEU ALA
SEQRES 8 C 251 ARG TYR PRO GLN PRO MET ALA PRO ALA ALA ALA ALA GLU
SEQRES 9 C 251 HIS ALA GLY MET ALA LEU PRO ALA ARG ASP GLN ILE VAL
SEQRES 10 C 251 ARG LEU ILE ALA ASP LEU ASP ARG PRO GLY ARG LEU THR
SEQRES 11 C 251 LEU VAL GLU GLY ALA GLY GLY LEU LEU VAL GLU LEU ALA
SEQRES 12 C 251 GLU PRO GLY VAL THR LEU ARG ASP VAL ALA VAL ASP VAL
SEQRES 13 C 251 ALA ALA ALA ALA LEU VAL VAL VAL THR ALA ASP LEU GLY
SEQRES 14 C 251 THR LEU ASN HIS THR LYS LEU THR LEU GLU ALA LEU ALA
SEQRES 15 C 251 ALA GLN GLN VAL SER CSX ALA GLY LEU VAL ILE GLY SER
SEQRES 16 C 251 TRP PRO ASP PRO PRO GLY LEU VAL ALA ALA SER ASN ARG
SEQRES 17 C 251 SER ALA LEU ALA ARG ILE ALA MET VAL ARG ALA ALA LEU
SEQRES 18 C 251 PRO ALA GLY ALA ALA SER LEU ASP ALA GLY ASP PHE ALA
SEQRES 19 C 251 ALA MET SER ALA ALA ALA PHE ASP ARG ASN TRP VAL ALA
SEQRES 20 C 251 GLY LEU VAL GLY
SEQRES 1 D 251 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 251 LEU GLN GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET
SEQRES 3 D 251 THR ILE LEU VAL VAL THR GLY THR GLY THR GLY VAL GLY
SEQRES 4 D 251 LYS THR VAL VAL CYS ALA ALA LEU ALA SER ALA ALA ARG
SEQRES 5 D 251 GLN ALA GLY ILE ASP VAL ALA VAL CYS LYS PRO VAL GLN
SEQRES 6 D 251 THR GLY THR ALA ARG GLY ASP ASP ASP LEU ALA GLU VAL
SEQRES 7 D 251 GLY ARG LEU ALA GLY VAL THR GLN LEU ALA GLY LEU ALA
SEQRES 8 D 251 ARG TYR PRO GLN PRO MET ALA PRO ALA ALA ALA ALA GLU
SEQRES 9 D 251 HIS ALA GLY MET ALA LEU PRO ALA ARG ASP GLN ILE VAL
SEQRES 10 D 251 ARG LEU ILE ALA ASP LEU ASP ARG PRO GLY ARG LEU THR
SEQRES 11 D 251 LEU VAL GLU GLY ALA GLY GLY LEU LEU VAL GLU LEU ALA
SEQRES 12 D 251 GLU PRO GLY VAL THR LEU ARG ASP VAL ALA VAL ASP VAL
SEQRES 13 D 251 ALA ALA ALA ALA LEU VAL VAL VAL THR ALA ASP LEU GLY
SEQRES 14 D 251 THR LEU ASN HIS THR LYS LEU THR LEU GLU ALA LEU ALA
SEQRES 15 D 251 ALA GLN GLN VAL SER CSX ALA GLY LEU VAL ILE GLY SER
SEQRES 16 D 251 TRP PRO ASP PRO PRO GLY LEU VAL ALA ALA SER ASN ARG
SEQRES 17 D 251 SER ALA LEU ALA ARG ILE ALA MET VAL ARG ALA ALA LEU
SEQRES 18 D 251 PRO ALA GLY ALA ALA SER LEU ASP ALA GLY ASP PHE ALA
SEQRES 19 D 251 ALA MET SER ALA ALA ALA PHE ASP ARG ASN TRP VAL ALA
SEQRES 20 D 251 GLY LEU VAL GLY
MODRES 3FMI CSX A 163 CYS S-OXY CYSTEINE
MODRES 3FMI CSX B 163 CYS S-OXY CYSTEINE
MODRES 3FMI CSX C 163 CYS S-OXY CYSTEINE
MODRES 3FMI CSX D 163 CYS S-OXY CYSTEINE
HET CSX A 163 7
HET CSX B 163 7
HET CSX C 163 7
HET CSX D 163 7
HET SO4 A 250 5
HET KAP A 430 13
HET KAP B 430 13
HET SO4 B 251 5
HET SO4 C 253 5
HET KAP C 430 13
HET SO4 D 252 5
HETNAM CSX S-OXY CYSTEINE
HETNAM SO4 SULFATE ION
HETNAM KAP 7-KETO-8-AMINOPELARGONIC ACID
FORMUL 1 CSX 4(C3 H7 N O3 S)
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 6 KAP 3(C9 H17 N O3)
FORMUL 12 HOH *210(H2 O)
HELIX 1 1 GLY A 14 ALA A 29 1 16
HELIX 2 2 THR A 43 GLY A 46 5 4
HELIX 3 3 ASP A 48 GLY A 58 1 11
HELIX 4 4 ALA A 73 ALA A 81 1 9
HELIX 5 5 ALA A 87 ASP A 97 1 11
HELIX 6 6 LEU A 124 VAL A 131 1 8
HELIX 7 7 GLY A 144 GLN A 159 1 16
HELIX 8 8 GLY A 176 ALA A 190 1 15
HELIX 9 9 GLY A 199 LEU A 203 5 5
HELIX 10 10 ASP A 204 PHE A 216 1 13
HELIX 11 11 ASP A 217 GLY A 223 1 7
HELIX 12 12 LEU A 224 GLY A 226 5 3
HELIX 13 13 GLY B 14 ALA B 29 1 16
HELIX 14 14 ASP B 48 GLY B 58 1 11
HELIX 15 15 ALA B 73 GLY B 82 1 10
HELIX 16 16 ALA B 87 ASP B 99 1 13
HELIX 17 17 LEU B 124 VAL B 131 1 8
HELIX 18 18 GLY B 144 GLN B 159 1 16
HELIX 19 19 GLY B 176 ALA B 190 1 15
HELIX 20 20 GLY B 199 LEU B 203 5 5
HELIX 21 21 ASP B 204 PHE B 216 1 13
HELIX 22 22 ASP B 217 LEU B 224 1 8
HELIX 23 23 GLY C 14 ALA C 29 1 16
HELIX 24 24 GLY C 42 GLY C 46 5 5
HELIX 25 25 ASP C 48 ALA C 57 1 10
HELIX 26 26 ALA C 73 ALA C 81 1 9
HELIX 27 27 ALA C 87 ASP C 97 1 11
HELIX 28 28 THR C 123 VAL C 131 1 9
HELIX 29 29 GLY C 144 ALA C 158 1 15
HELIX 30 30 GLY C 176 ALA C 190 1 15
HELIX 31 31 GLY C 199 LEU C 203 5 5
HELIX 32 32 ASP C 204 PHE C 216 1 13
HELIX 33 33 ASP C 217 GLY C 223 1 7
HELIX 34 34 GLY D 14 ALA D 29 1 16
HELIX 35 35 ASP D 48 GLY D 58 1 11
HELIX 36 36 ALA D 73 GLY D 82 1 10
HELIX 37 37 ALA D 87 LEU D 98 1 12
HELIX 38 38 LEU D 124 ALA D 132 1 9
HELIX 39 39 GLY D 144 GLN D 159 1 16
HELIX 40 40 GLY D 176 ALA D 190 1 15
HELIX 41 41 GLY D 199 LEU D 203 5 5
HELIX 42 42 ALA D 205 PHE D 216 1 12
HELIX 43 43 ASP D 217 GLY D 223 1 7
SHEET 1 A 7 GLN A 61 TYR A 68 0
SHEET 2 A 7 VAL A 33 THR A 41 1 N VAL A 35 O GLN A 61
SHEET 3 A 7 LEU A 104 GLU A 108 1 O LEU A 106 N CYS A 36
SHEET 4 A 7 THR A 2 GLY A 8 1 N VAL A 6 O VAL A 107
SHEET 5 A 7 ALA A 134 VAL A 139 1 O LEU A 136 N VAL A 5
SHEET 6 A 7 CSX A 163 TRP A 171 1 O ALA A 164 N ALA A 135
SHEET 7 A 7 VAL A 192 PRO A 197 1 O ARG A 193 N LEU A 166
SHEET 1 B 2 GLU A 116 ALA A 118 0
SHEET 2 B 2 VAL A 122 THR A 123 -1 O VAL A 122 N LEU A 117
SHEET 1 C 7 GLN B 61 ALA B 63 0
SHEET 2 C 7 ASP B 32 CYS B 36 1 N VAL B 35 O GLN B 61
SHEET 3 C 7 ARG B 103 GLY B 112 1 O LEU B 106 N CYS B 36
SHEET 4 C 7 ILE B 3 GLY B 8 1 N VAL B 6 O VAL B 107
SHEET 5 C 7 ALA B 134 VAL B 139 1 O VAL B 138 N THR B 7
SHEET 6 C 7 CSX B 163 TRP B 171 1 O VAL B 167 N VAL B 139
SHEET 7 C 7 VAL B 192 PRO B 197 1 O LEU B 196 N TRP B 171
SHEET 1 D 2 VAL B 39 THR B 41 0
SHEET 2 D 2 ALA B 66 TYR B 68 1 O TYR B 68 N GLN B 40
SHEET 1 E 2 GLU B 116 ALA B 118 0
SHEET 2 E 2 VAL B 122 THR B 123 -1 O VAL B 122 N LEU B 117
SHEET 1 F 7 LEU C 62 ARG C 67 0
SHEET 2 F 7 VAL C 33 GLN C 40 1 N LYS C 37 O ALA C 63
SHEET 3 F 7 LEU C 104 GLU C 108 1 O LEU C 106 N CYS C 36
SHEET 4 F 7 THR C 2 GLY C 8 1 N THR C 2 O THR C 105
SHEET 5 F 7 ALA C 134 VAL C 139 1 O LEU C 136 N VAL C 5
SHEET 6 F 7 CSX C 163 TRP C 171 1 O ALA C 164 N ALA C 135
SHEET 7 F 7 VAL C 192 PRO C 197 1 O LEU C 196 N TRP C 171
SHEET 1 G 7 GLN D 61 ALA D 63 0
SHEET 2 G 7 ASP D 32 CYS D 36 1 N VAL D 35 O GLN D 61
SHEET 3 G 7 ARG D 103 GLY D 112 1 O LEU D 106 N CYS D 36
SHEET 4 G 7 ILE D 3 GLY D 8 1 N VAL D 6 O VAL D 107
SHEET 5 G 7 ALA D 134 VAL D 139 1 O VAL D 138 N THR D 7
SHEET 6 G 7 CSX D 163 TRP D 171 1 O ALA D 164 N ALA D 135
SHEET 7 G 7 VAL D 192 PRO D 197 1 O ARG D 193 N LEU D 166
SHEET 1 H 2 VAL D 39 THR D 41 0
SHEET 2 H 2 ALA D 66 TYR D 68 1 O TYR D 68 N GLN D 40
SHEET 1 I 2 GLU D 116 ALA D 118 0
SHEET 2 I 2 VAL D 122 THR D 123 -1 O VAL D 122 N LEU D 117
LINK C SER A 162 N CSX A 163 1555 1555 1.33
LINK C CSX A 163 N ALA A 164 1555 1555 1.34
LINK C SER B 162 N CSX B 163 1555 1555 1.32
LINK C CSX B 163 N ALA B 164 1555 1555 1.33
LINK C SER C 162 N CSX C 163 1555 1555 1.33
LINK C CSX C 163 N ALA C 164 1555 1555 1.33
LINK C SER D 162 N CSX D 163 1555 1555 1.33
LINK C CSX D 163 N ALA D 164 1555 1555 1.33
CISPEP 1 GLU A 119 PRO A 120 0 0.78
CISPEP 2 ASP A 173 PRO A 174 0 -5.80
CISPEP 3 ALA B 110 GLY B 111 0 -25.41
CISPEP 4 GLU B 119 PRO B 120 0 -11.82
CISPEP 5 ASP B 173 PRO B 174 0 -6.16
CISPEP 6 GLU C 119 PRO C 120 0 -7.20
CISPEP 7 ASP C 173 PRO C 174 0 7.50
CISPEP 8 PRO C 174 PRO C 175 0 20.89
CISPEP 9 GLU D 119 PRO D 120 0 -5.79
CISPEP 10 ASP D 173 PRO D 174 0 -3.73
SITE 1 AC1 6 GLY A 12 VAL A 13 GLY A 14 LYS A 15
SITE 2 AC1 6 THR A 16 HOH A 272
SITE 1 AC2 10 LEU A 143 GLY A 144 THR A 145 LEU A 146
SITE 2 AC2 10 ASN A 147 THR B 11 THR B 41 PRO B 71
SITE 3 AC2 10 MET B 72 ALA B 73
SITE 1 AC3 14 THR A 11 THR A 41 ASP A 47 PRO A 71
SITE 2 AC3 14 ALA A 73 VAL A 115 LEU B 143 GLY B 144
SITE 3 AC3 14 THR B 145 LEU B 146 ASN B 147 HOH B 227
SITE 4 AC3 14 HOH B 229 HOH B 230
SITE 1 AC4 6 GLY B 12 VAL B 13 GLY B 14 LYS B 15
SITE 2 AC4 6 THR B 16 HOH B 234
SITE 1 AC5 5 GLY C 12 VAL C 13 GLY C 14 LYS C 15
SITE 2 AC5 5 THR C 16
SITE 1 AC6 16 THR C 11 THR C 41 ARG C 45 ASP C 47
SITE 2 AC6 16 PRO C 71 MET C 72 ALA C 73 VAL C 115
SITE 3 AC6 16 HOH C 228 HOH C 247 HOH C 249 LEU D 143
SITE 4 AC6 16 GLY D 144 THR D 145 LEU D 146 ASN D 147
SITE 1 AC7 6 GLY D 12 VAL D 13 GLY D 14 LYS D 15
SITE 2 AC7 6 THR D 16 HOH D 241
CRYST1 55.372 105.137 151.569 90.00 90.00 90.00 P 21 21 21 16
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 0.018060 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009511 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END