HEADER TRANSFERASE 05-NOV-07 2VFW
TITLE RV1086 NATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHORT-CHAIN Z-ISOPRENYL DIPHOSPHATE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 30-256;
COMPND 5 SYNONYM: Z-FPP SYNTHETASE, Z-ISOPRENYL DIPHOSPHATE SYNTHASE, Z-FPPS,
COMPND 6 RV1086;
COMPND 7 EC: 2.5.1.68;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PEPTIDOGLYCAN SYNTHESIS, CELL WALL BIOGENESIS/DEGRADATION, SECRETED,
KEYWDS 2 CELL SHAPE, TRANSFERASE, PRENYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.NAISMITH,W.WANG,C.DONG
REVDAT 6 07-FEB-18 2VFW 1 JRNL
REVDAT 5 13-DEC-17 2VFW 1 SOURCE
REVDAT 4 13-JUL-11 2VFW 1 VERSN
REVDAT 3 24-FEB-09 2VFW 1 VERSN
REVDAT 2 22-JUL-08 2VFW 1 JRNL REMARK ATOM
REVDAT 1 13-NOV-07 2VFW 0
JRNL AUTH W.WANG,C.DONG,M.MCNEIL,D.KAUR,S.MAHAPATRA,D.C.CRICK,
JRNL AUTH 2 J.H.NAISMITH
JRNL TITL THE STRUCTURAL BASIS OF CHAIN LENGTH CONTROL IN RV1086.
JRNL REF J. MOL. BIOL. V. 381 129 2008
JRNL REFN ESSN 1089-8638
JRNL PMID 18597781
JRNL DOI 10.1016/J.JMB.2008.05.060
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 3 NUMBER OF REFLECTIONS : 17126
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 911
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1073
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3556
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.31000
REMARK 3 B22 (A**2) : 0.75000
REMARK 3 B33 (A**2) : -0.44000
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): 0.605
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.308
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.232
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.314
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3640 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4954 ; 1.242 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 452 ; 5.649 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;37.697 ;22.778
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 572 ;15.759 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;18.892 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 546 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2822 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1555 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2459 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 103 ; 0.150 ; 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): 52 ; 0.187 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.132 ; 0.200
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): 2300 ; 0.478 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3598 ; 0.840 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1535 ; 1.238 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1356 ; 1.952 ; 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 : 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 30 A 256
REMARK 3 ORIGIN FOR THE GROUP (A): -31.6570 -0.2190 -2.7740
REMARK 3 T TENSOR
REMARK 3 T11: -0.0298 T22: -0.3481
REMARK 3 T33: 0.0396 T12: 0.0136
REMARK 3 T13: 0.0168 T23: -0.0513
REMARK 3 L TENSOR
REMARK 3 L11: 2.6940 L22: 0.8245
REMARK 3 L33: 2.7794 L12: -0.1457
REMARK 3 L13: 0.9651 L23: -0.1330
REMARK 3 S TENSOR
REMARK 3 S11: -0.0337 S12: 0.0551 S13: -0.0330
REMARK 3 S21: 0.0892 S22: 0.0014 S23: 0.0895
REMARK 3 S31: -0.0647 S32: -0.1383 S33: 0.0324
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 30 B 256
REMARK 3 ORIGIN FOR THE GROUP (A): -27.3470 1.2520 -31.8760
REMARK 3 T TENSOR
REMARK 3 T11: -0.0207 T22: -0.2990
REMARK 3 T33: 0.0006 T12: -0.0026
REMARK 3 T13: -0.0375 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 3.9324 L22: 0.5635
REMARK 3 L33: 2.7913 L12: 0.0630
REMARK 3 L13: -1.1991 L23: -0.2396
REMARK 3 S TENSOR
REMARK 3 S11: 0.0344 S12: -0.0164 S13: 0.1213
REMARK 3 S21: 0.0381 S22: -0.0723 S23: 0.0710
REMARK 3 S31: -0.1155 S32: 0.0334 S33: 0.0378
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 : 1.20
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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2VFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1290034354.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
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 : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17126
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 52.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
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 -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 29.43900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.61350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.84050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.61350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.43900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.84050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.8 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 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 SER A 201 133.31 -39.45
REMARK 500 CYS B 39 78.65 -105.62
REMARK 500 SER B 201 121.61 -38.42
REMARK 500 SER B 219 -7.33 72.81
REMARK 500 LEU B 222 57.57 36.60
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 A1257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1257
DBREF 2VFW A 30 256 UNP O53434 ZFPP_MYCTU 30 256
DBREF 2VFW B 30 256 UNP O53434 ZFPP_MYCTU 30 256
SEQRES 1 A 227 ASP LEU PRO ARG HIS ILE ALA VAL LEU CYS ASP GLY ASN
SEQRES 2 A 227 ARG ARG TRP ALA ARG SER ALA GLY TYR ASP ASP VAL SER
SEQRES 3 A 227 TYR GLY TYR ARG MET GLY ALA ALA LYS ILE ALA GLU MET
SEQRES 4 A 227 LEU ARG TRP CYS HIS GLU ALA GLY ILE GLU LEU ALA THR
SEQRES 5 A 227 VAL TYR LEU LEU SER THR GLU ASN LEU GLN ARG ASP PRO
SEQRES 6 A 227 ASP GLU LEU ALA ALA LEU ILE GLU ILE ILE THR ASP VAL
SEQRES 7 A 227 VAL GLU GLU ILE CYS ALA PRO ALA ASN HIS TRP SER VAL
SEQRES 8 A 227 ARG THR VAL GLY ASP LEU GLY LEU ILE GLY GLU GLU PRO
SEQRES 9 A 227 ALA ARG ARG LEU ARG GLY ALA VAL GLU SER THR PRO GLU
SEQRES 10 A 227 VAL ALA SER PHE HIS VAL ASN VAL ALA VAL GLY TYR GLY
SEQRES 11 A 227 GLY ARG ARG GLU ILE VAL ASP ALA VAL ARG ALA LEU LEU
SEQRES 12 A 227 SER LYS GLU LEU ALA ASN GLY ALA THR ALA GLU GLU LEU
SEQRES 13 A 227 VAL ASP ALA VAL THR VAL GLU GLY ILE SER GLU ASN LEU
SEQRES 14 A 227 TYR THR SER GLY GLN PRO ASP PRO ASP LEU VAL ILE ARG
SEQRES 15 A 227 THR SER GLY GLU GLN ARG LEU SER GLY PHE LEU LEU TRP
SEQRES 16 A 227 GLN SER ALA TYR SER GLU MET TRP PHE THR GLU ALA HIS
SEQRES 17 A 227 TRP PRO ALA PHE ARG HIS VAL ASP PHE LEU ARG ALA LEU
SEQRES 18 A 227 ARG ASP TYR SER ALA ARG
SEQRES 1 B 227 ASP LEU PRO ARG HIS ILE ALA VAL LEU CYS ASP GLY ASN
SEQRES 2 B 227 ARG ARG TRP ALA ARG SER ALA GLY TYR ASP ASP VAL SER
SEQRES 3 B 227 TYR GLY TYR ARG MET GLY ALA ALA LYS ILE ALA GLU MET
SEQRES 4 B 227 LEU ARG TRP CYS HIS GLU ALA GLY ILE GLU LEU ALA THR
SEQRES 5 B 227 VAL TYR LEU LEU SER THR GLU ASN LEU GLN ARG ASP PRO
SEQRES 6 B 227 ASP GLU LEU ALA ALA LEU ILE GLU ILE ILE THR ASP VAL
SEQRES 7 B 227 VAL GLU GLU ILE CYS ALA PRO ALA ASN HIS TRP SER VAL
SEQRES 8 B 227 ARG THR VAL GLY ASP LEU GLY LEU ILE GLY GLU GLU PRO
SEQRES 9 B 227 ALA ARG ARG LEU ARG GLY ALA VAL GLU SER THR PRO GLU
SEQRES 10 B 227 VAL ALA SER PHE HIS VAL ASN VAL ALA VAL GLY TYR GLY
SEQRES 11 B 227 GLY ARG ARG GLU ILE VAL ASP ALA VAL ARG ALA LEU LEU
SEQRES 12 B 227 SER LYS GLU LEU ALA ASN GLY ALA THR ALA GLU GLU LEU
SEQRES 13 B 227 VAL ASP ALA VAL THR VAL GLU GLY ILE SER GLU ASN LEU
SEQRES 14 B 227 TYR THR SER GLY GLN PRO ASP PRO ASP LEU VAL ILE ARG
SEQRES 15 B 227 THR SER GLY GLU GLN ARG LEU SER GLY PHE LEU LEU TRP
SEQRES 16 B 227 GLN SER ALA TYR SER GLU MET TRP PHE THR GLU ALA HIS
SEQRES 17 B 227 TRP PRO ALA PHE ARG HIS VAL ASP PHE LEU ARG ALA LEU
SEQRES 18 B 227 ARG ASP TYR SER ALA ARG
HET SO4 A1257 5
HET SO4 B1257 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *10(H2 O)
HELIX 1 1 GLY A 41 GLY A 50 1 10
HELIX 2 2 VAL A 54 GLY A 76 1 23
HELIX 3 3 GLU A 88 ARG A 92 5 5
HELIX 4 4 ASP A 93 CYS A 112 1 20
HELIX 5 5 ASP A 125 ILE A 129 5 5
HELIX 6 6 GLY A 130 GLU A 142 1 13
HELIX 7 7 GLY A 159 ASN A 178 1 20
HELIX 8 8 THR A 181 VAL A 189 1 9
HELIX 9 9 THR A 190 GLU A 196 1 7
HELIX 10 10 HIS A 237 PHE A 241 5 5
HELIX 11 11 ARG A 242 ARG A 256 1 15
HELIX 12 12 GLY B 41 ALA B 49 1 9
HELIX 13 13 VAL B 54 GLY B 76 1 23
HELIX 14 14 GLU B 88 ARG B 92 5 5
HELIX 15 15 ASP B 93 CYS B 112 1 20
HELIX 16 16 ASP B 125 ILE B 129 5 5
HELIX 17 17 GLY B 130 SER B 143 1 14
HELIX 18 18 GLY B 159 ASN B 178 1 20
HELIX 19 19 THR B 181 VAL B 186 1 6
HELIX 20 20 THR B 190 ASN B 197 1 8
HELIX 21 21 HIS B 237 PHE B 241 5 5
HELIX 22 22 ARG B 242 ALA B 255 1 14
SHEET 1 AA 6 SER A 119 VAL A 123 0
SHEET 2 AA 6 HIS A 151 TYR A 158 1 O VAL A 152 N ARG A 121
SHEET 3 AA 6 LEU A 79 SER A 86 1 O ALA A 80 N ASN A 153
SHEET 4 AA 6 HIS A 34 LEU A 38 1 O ILE A 35 N THR A 81
SHEET 5 AA 6 LEU A 208 ARG A 211 1 O LEU A 208 N ALA A 36
SHEET 6 AA 6 GLU A 230 PHE A 233 1 O GLU A 230 N VAL A 209
SHEET 1 BA 6 SER B 119 VAL B 123 0
SHEET 2 BA 6 HIS B 151 ALA B 155 1 O VAL B 152 N ARG B 121
SHEET 3 BA 6 LEU B 79 TYR B 83 1 O ALA B 80 N ASN B 153
SHEET 4 BA 6 HIS B 34 LEU B 38 1 O ILE B 35 N THR B 81
SHEET 5 BA 6 LEU B 208 ARG B 211 1 O LEU B 208 N ALA B 36
SHEET 6 BA 6 GLU B 230 PHE B 233 1 O GLU B 230 N VAL B 209
SITE 1 AC1 4 GLY A 41 ASN A 42 ARG A 43 ARG A 44
SITE 1 AC2 5 GLY B 41 ASN B 42 ARG B 43 ARG B 44
SITE 2 AC2 5 ARG B 92
CRYST1 58.878 73.681 103.227 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 0.016984 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013572 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009687 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
