HEADER OXIDOREDUCTASE 31-MAY-13 4BQP
TITLE MTB INHA COMPLEX WITH METHYL-THIAZOLE COMPOUND 7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ENOYL-ACYL CARRIER PROTEIN REDUCTASE, NADH-DEPENDENT
COMPND 5 ENOYL-ACP REDUCTASE;
COMPND 6 EC: 1.3.1.9;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR
KEYWDS OXIDOREDUCTASE, ACP ENOYL REDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.READ,H.GINGELL,P.MADHAVAPEDDI,P.S.SHIRUDE
REVDAT 2 15-JAN-14 4BQP 1 JRNL
REVDAT 1 11-DEC-13 4BQP 0
JRNL AUTH P.S.SHIRUDE,P.MADHAVAPEDDI,M.NAIK,K.MURUGAN,V.SHINDE,
JRNL AUTH 2 R.NANDISHAIAH,J.BHAT,A.KUMAR,S.HAMEED,G.HOLDGATE,G.DAVIES,
JRNL AUTH 3 H.MCMIKEN,N.HEGDE,A.AMBADY,J.VENKATRAMAN,M.PANDA,
JRNL AUTH 4 B.BANDODKAR,V.K.SAMBANDAMURTHY,J.A.READ
JRNL TITL METHYL-THIAZOLES: A NOVEL MODE OF INHIBITION WITH THE
JRNL TITL 2 POTENTIAL TO DEVELOP NOVEL INHIBITORS TARGETING INHA IN
JRNL TITL 3 MYCOBACTERIUM TUBERCULOSIS.
JRNL REF J.MED.CHEM. V. 56 8533 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 24107081
JRNL DOI 10.1021/JM4012033
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,WOMACK;
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.78
REMARK 3 NUMBER OF REFLECTIONS : 112158
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) : 0.2093
REMARK 3 R VALUE (WORKING SET) : 0.2080
REMARK 3 FREE R VALUE : 0.2334
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.02
REMARK 3 FREE R VALUE TEST SET COUNT : 5629
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.94
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.78
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6008
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2007
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5677
REMARK 3 BIN R VALUE (WORKING SET) : 0.1996
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.51
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 331
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11393
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 895
REMARK 3 SOLVENT ATOMS : 450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.6993
REMARK 3 B22 (A**2) : 0.6895
REMARK 3 B33 (A**2) : -4.3888
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : -1.3546
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.253
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.174
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.147
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.178
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.150
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.8592
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.8246
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12102 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 16560 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 3936 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 219 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 1930 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12102 ; 20.00 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.00 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1657 ; 5.00 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 14429 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.91
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.11
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 57.0305 7.5962 78.7558
REMARK 3 T TENSOR
REMARK 3 T11: -0.1232 T22: -0.0637
REMARK 3 T33: -0.1228 T12: 0.0511
REMARK 3 T13: -0.0069 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 1.1958 L22: 0.3615
REMARK 3 L33: 0.5447 L12: -0.0211
REMARK 3 L13: 0.1310 L23: 0.2536
REMARK 3 S TENSOR
REMARK 3 S11: 0.0275 S12: 0.2483 S13: -0.0802
REMARK 3 S21: -0.0812 S22: -0.0246 S23: -0.0543
REMARK 3 S31: 0.0292 S32: 0.0588 S33: -0.0029
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8440 17.3346 78.6166
REMARK 3 T TENSOR
REMARK 3 T11: -0.1400 T22: -0.0994
REMARK 3 T33: -0.1169 T12: 0.0673
REMARK 3 T13: -0.0462 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 1.0946 L22: 0.2074
REMARK 3 L33: 0.6561 L12: -0.0111
REMARK 3 L13: -0.3625 L23: -0.2460
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: 0.2417 S13: 0.0768
REMARK 3 S21: -0.1142 S22: -0.0004 S23: 0.0198
REMARK 3 S31: -0.0543 S32: -0.0597 S33: -0.0161
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2218 8.0192 11.9901
REMARK 3 T TENSOR
REMARK 3 T11: 0.0539 T22: 0.0029
REMARK 3 T33: -0.0752 T12: 0.0602
REMARK 3 T13: -0.0077 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.0995 L22: 0.2215
REMARK 3 L33: 0.5496 L12: -0.1200
REMARK 3 L13: 0.0670 L23: -0.1719
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: 0.0475 S13: 0.0221
REMARK 3 S21: -0.0306 S22: -0.0240 S23: -0.0150
REMARK 3 S31: 0.0201 S32: 0.0216 S33: 0.0143
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0026 -6.7696 40.4891
REMARK 3 T TENSOR
REMARK 3 T11: 0.0199 T22: 0.0047
REMARK 3 T33: -0.0488 T12: 0.0385
REMARK 3 T13: -0.0272 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.1998 L22: 0.5149
REMARK 3 L33: 0.0872 L12: -0.1774
REMARK 3 L13: -0.1433 L23: 0.1275
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: -0.0383 S13: -0.0536
REMARK 3 S21: 0.0085 S22: 0.0125 S23: 0.0247
REMARK 3 S31: 0.0209 S32: -0.0109 S33: -0.0100
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN E
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8811 -22.2932 48.2868
REMARK 3 T TENSOR
REMARK 3 T11: 0.0159 T22: 0.0314
REMARK 3 T33: -0.0764 T12: 0.0973
REMARK 3 T13: -0.0328 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 0.1995 L22: 0.7096
REMARK 3 L33: 0.3825 L12: 0.0578
REMARK 3 L13: -0.0907 L23: -0.2404
REMARK 3 S TENSOR
REMARK 3 S11: -0.0144 S12: -0.0561 S13: 0.0230
REMARK 3 S21: 0.0288 S22: 0.0175 S23: 0.0300
REMARK 3 S31: 0.0073 S32: -0.0099 S33: -0.0031
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN F
REMARK 3 ORIGIN FOR THE GROUP (A): 62.6427 -5.7613 27.7069
REMARK 3 T TENSOR
REMARK 3 T11: 0.0240 T22: -0.0659
REMARK 3 T33: 0.0236 T12: 0.0409
REMARK 3 T13: -0.0239 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0529 L22: 0.7417
REMARK 3 L33: 0.1447 L12: -0.1558
REMARK 3 L13: -0.2944 L23: 0.3397
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: -0.0052 S13: 0.0809
REMARK 3 S21: -0.0190 S22: -0.0056 S23: -0.0316
REMARK 3 S31: -0.0242 S32: 0.0277 S33: 0.0090
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B OR CHAIN C OR CHAIN D OR CHAIN E OR CHAIN F
REMARK 3 AND RESID 1271 OR CHAIN A AND RESID 1272
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8944 -0.3810 48.1044
REMARK 3 T TENSOR
REMARK 3 T11: 0.0076 T22: -0.0042
REMARK 3 T33: -0.0176 T12: 0.0202
REMARK 3 T13: -0.0104 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.0069 L22: 0.0001
REMARK 3 L33: -0.0007 L12: -0.0302
REMARK 3 L13: -0.0253 L23: -0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: 0.0097 S13: -0.0038
REMARK 3 S21: -0.0192 S22: 0.0187 S23: -0.0007
REMARK 3 S31: 0.0041 S32: -0.0029 S33: -0.0192
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A OR CHAIN B OR CHAIN C OR CHAIN D OR CHAIN E
REMARK 3 OR CHAIN F AND RESID 1270
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9137 -0.3644 50.2092
REMARK 3 T TENSOR
REMARK 3 T11: 0.0034 T22: -0.0121
REMARK 3 T33: 0.0019 T12: 0.0084
REMARK 3 T13: -0.0031 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.0043 L22: 0.0498
REMARK 3 L33: -0.0012 L12: 0.0397
REMARK 3 L13: -0.0066 L23: 0.0264
REMARK 3 S TENSOR
REMARK 3 S11: 0.0047 S12: 0.0265 S13: 0.0064
REMARK 3 S21: -0.0040 S22: -0.0021 S23: -0.0021
REMARK 3 S31: -0.0069 S32: -0.0052 S33: -0.0025
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NA. NUMBER OF
REMARK 3 ATOMS WITH PROPER CCP4 ATOM TYPE=12287. NUMBER WITH APPROX DEFAULT
REMARK 3 CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED CONTACTS=1.
REMARK 4
REMARK 4 4BQP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-13.
REMARK 100 THE PDBE ID CODE IS EBI-57094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-12
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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113532
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.89
REMARK 200 RESOLUTION RANGE LOW (A) : 60.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 3.2
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.14
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.40
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 50.64850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.65200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.64850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.65200
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, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -147.8 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 84.00283
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 188.21111
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.7 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 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -50.64850
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 40.65200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 50.64850
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -40.65200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C2044 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 MET D 1
REMARK 465 MET E 1
REMARK 465 ARG E 43
REMARK 465 LEU E 44
REMARK 465 LEU E 197
REMARK 465 ALA E 198
REMARK 465 MET E 199
REMARK 465 SER E 200
REMARK 465 ALA E 201
REMARK 465 ILE E 202
REMARK 465 VAL E 203
REMARK 465 GLY E 204
REMARK 465 MET F 1
REMARK 465 LEU F 197
REMARK 465 ALA F 198
REMARK 465 MET F 199
REMARK 465 SER F 200
REMARK 465 ALA F 201
REMARK 465 ILE F 202
REMARK 465 VAL F 203
REMARK 465 GLY F 204
REMARK 465 GLY F 205
REMARK 465 ALA F 206
REMARK 465 LEU F 207
REMARK 465 GLY F 208
REMARK 465 GLU F 209
REMARK 465 GLU F 210
REMARK 465 ALA F 211
REMARK 465 GLY F 212
REMARK 465 ALA F 213
REMARK 465 GLN F 214
REMARK 465 ILE F 215
REMARK 465 GLN F 216
REMARK 465 LEU F 217
REMARK 465 LEU F 218
REMARK 465 GLU F 219
REMARK 465 GLU F 220
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 35 CG CD OE1 NE2
REMARK 470 ARG A 45 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 49 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 GLU A 80 CG CD OE1 OE2
REMARK 470 GLN A 100 CD OE1 NE2
REMARK 470 LEU A 197 CG CD1 CD2
REMARK 470 GLU A 210 CD OE1 OE2
REMARK 470 GLN A 216 CD OE1 NE2
REMARK 470 GLU A 220 CD OE1 OE2
REMARK 470 THR B 2 OG1 CG2
REMARK 470 ARG B 49 CD NE CZ NH1 NH2
REMARK 470 ARG B 53 CD NE CZ NH1 NH2
REMARK 470 GLU B 80 CG CD OE1 OE2
REMARK 470 GLN B 100 CG CD OE1 NE2
REMARK 470 SER B 200 OG
REMARK 470 GLU B 210 CG CD OE1 OE2
REMARK 470 THR C 2 OG1 CG2
REMARK 470 ARG C 43 NE CZ NH1 NH2
REMARK 470 ARG C 45 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 53 CD NE CZ NH1 NH2
REMARK 470 LYS C 57 CG CD CE NZ
REMARK 470 GLU C 68 CG CD OE1 OE2
REMARK 470 GLU C 69 CG CD OE1 OE2
REMARK 470 GLU C 80 CG CD OE1 OE2
REMARK 470 GLN C 100 CG CD OE1 NE2
REMARK 470 ILE C 105 CG1 CG2 CD1
REMARK 470 ILE C 202 CG1 CG2 CD1
REMARK 470 VAL C 203 CG1 CG2
REMARK 470 LEU C 207 CG CD1 CD2
REMARK 470 GLU C 209 CG CD OE1 OE2
REMARK 470 GLU C 210 CG CD OE1 OE2
REMARK 470 GLN C 214 CG CD OE1 NE2
REMARK 470 GLU C 220 CG CD OE1 OE2
REMARK 470 LEU C 269 CG CD1 CD2
REMARK 470 ARG D 9 CD NE CZ NH1 NH2
REMARK 470 GLN D 35 CD OE1 NE2
REMARK 470 ASP D 42 CG OD1 OD2
REMARK 470 ARG D 43 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 44 CG CD1 CD2
REMARK 470 ARG D 45 CD NE CZ NH1 NH2
REMARK 470 LEU D 46 CG CD1 CD2
REMARK 470 GLN D 48 CG CD OE1 NE2
REMARK 470 LYS D 57 CG CD CE NZ
REMARK 470 GLU D 68 CG CD OE1 OE2
REMARK 470 GLU D 69 CG CD OE1 OE2
REMARK 470 GLU D 80 CG CD OE1 OE2
REMARK 470 LYS D 87 CG CD CE NZ
REMARK 470 GLN D 100 CD OE1 NE2
REMARK 470 LYS D 181 CG CD CE NZ
REMARK 470 ARG D 195 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 197 CG CD1 CD2
REMARK 470 ILE D 202 CG1 CG2 CD1
REMARK 470 VAL D 203 CG1 CG2
REMARK 470 GLU D 209 CG CD OE1 OE2
REMARK 470 GLU D 210 CG CD OE1 OE2
REMARK 470 GLN D 214 CG CD OE1 NE2
REMARK 470 GLN D 216 CG CD OE1 NE2
REMARK 470 GLU D 219 CD OE1 OE2
REMARK 470 GLU D 220 CG CD OE1 OE2
REMARK 470 GLN D 224 CD OE1 NE2
REMARK 470 LYS D 233 CG CD CE NZ
REMARK 470 LEU D 269 CG CD1 CD2
REMARK 470 ARG E 45 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 46 CG CD1 CD2
REMARK 470 ARG E 49 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 53 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 57 CG CD CE NZ
REMARK 470 GLU E 80 CG CD OE1 OE2
REMARK 470 ARG E 195 CG CD NE CZ NH1 NH2
REMARK 470 THR E 196 OG1 CG2
REMARK 470 GLU E 209 CG CD OE1 OE2
REMARK 470 GLN E 214 CG CD OE1 NE2
REMARK 470 GLN E 216 CG CD OE1 NE2
REMARK 470 GLU E 220 CG CD OE1 OE2
REMARK 470 GLN E 224 CG CD OE1 NE2
REMARK 470 MET E 232 CG SD CE
REMARK 470 THR F 2 OG1 CG2
REMARK 470 GLN F 35 CG CD OE1 NE2
REMARK 470 ASP F 42 CG OD1 OD2
REMARK 470 ARG F 43 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 45 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 48 CG CD OE1 NE2
REMARK 470 ARG F 49 CG CD NE CZ NH1 NH2
REMARK 470 ASP F 52 CG OD1 OD2
REMARK 470 ARG F 53 CD NE CZ NH1 NH2
REMARK 470 LYS F 57 CG CD CE NZ
REMARK 470 GLU F 68 CG CD OE1 OE2
REMARK 470 GLU F 69 CG CD OE1 OE2
REMARK 470 GLU F 80 CG CD OE1 OE2
REMARK 470 GLN F 100 CG CD OE1 NE2
REMARK 470 ARG F 195 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 224 CG CD OE1 NE2
REMARK 470 LYS F 240 CD CE NZ
REMARK 470 LEU F 269 CG CD1 CD2
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 F 2030 O HOH D 2043 1655 2.19
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 42 -74.91 54.22
REMARK 500 ALA A 124 -59.95 -122.35
REMARK 500 ASP A 150 107.10 -34.54
REMARK 500 ALA A 157 -37.22 64.30
REMARK 500 ASN A 159 -114.98 42.88
REMARK 500 ALA A 260 72.14 -105.17
REMARK 500 ASP B 42 -73.71 56.41
REMARK 500 ALA B 124 -58.70 -121.33
REMARK 500 ASP B 150 108.97 -35.39
REMARK 500 ALA B 157 -43.58 59.18
REMARK 500 ASN B 159 -116.75 41.80
REMARK 500 ARG B 195 66.08 -69.48
REMARK 500 ALA B 260 68.73 -110.18
REMARK 500 ASP C 42 -72.44 53.83
REMARK 500 ALA C 124 -59.85 -121.73
REMARK 500 ASP C 150 107.08 -40.89
REMARK 500 ALA C 157 -34.88 59.84
REMARK 500 ASN C 159 -114.66 42.91
REMARK 500 ALA C 260 66.70 -112.03
REMARK 500 PHE D 41 -87.89 -92.46
REMARK 500 ASP D 150 108.43 -34.03
REMARK 500 ALA D 157 -36.10 63.25
REMARK 500 ASN D 159 -110.61 35.32
REMARK 500 ARG D 195 64.74 -67.39
REMARK 500 ALA D 260 67.01 -112.70
REMARK 500 PHE E 41 -85.80 -93.02
REMARK 500 ASP E 150 107.97 -34.36
REMARK 500 ALA E 157 -41.67 67.56
REMARK 500 ASN E 159 -118.25 43.77
REMARK 500 ARG E 195 63.90 -68.62
REMARK 500 ALA E 260 67.75 -109.47
REMARK 500 PHE F 41 -85.19 -91.92
REMARK 500 ALA F 124 -60.02 -122.99
REMARK 500 ASP F 150 107.97 -31.72
REMARK 500 ALA F 157 -42.61 70.53
REMARK 500 ASN F 159 -105.76 39.25
REMARK 500 ARG F 195 74.42 -65.50
REMARK 500 ALA F 260 66.04 -110.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP A 42 23.8 L L OUTSIDE RANGE
REMARK 500 ASP B 42 24.0 L L OUTSIDE RANGE
REMARK 500 TRP B 160 24.9 L L OUTSIDE RANGE
REMARK 500 ASP C 42 24.7 L L OUTSIDE RANGE
REMARK 500 LEU C 134 24.9 L L OUTSIDE RANGE
REMARK 500 PHE D 41 21.0 L L OUTSIDE RANGE
REMARK 500 TYR D 113 24.8 L L OUTSIDE RANGE
REMARK 500 TRP D 249 24.8 L L OUTSIDE RANGE
REMARK 500 PHE E 41 22.1 L L OUTSIDE RANGE
REMARK 500 ALA E 157 24.4 L L OUTSIDE RANGE
REMARK 500 TRP E 249 24.8 L L OUTSIDE RANGE
REMARK 500 PHE F 41 21.9 L L OUTSIDE RANGE
REMARK 500 ILE F 47 23.3 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1271 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2082 O
REMARK 620 2 HOH A2081 O 90.7
REMARK 620 3 HOH A2085 O 101.1 91.5
REMARK 620 4 ASP A 223 O 162.0 95.2 95.8
REMARK 620 5 GLN A 224 O 82.4 80.6 171.5 81.8
REMARK 620 6 ALA A 226 O 86.7 176.2 86.2 88.0 101.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VMY A1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VMY B1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VMY C1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VMY D1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VMY E1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VMY F1271
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BQR RELATED DB: PDB
REMARK 900 MTB INHA COMPLEX WITH METHYL-THIAZOLE COMPOUND 7
DBREF 4BQP A 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 4BQP B 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 4BQP C 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 4BQP D 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 4BQP E 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 4BQP F 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
SEQRES 1 A 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 A 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 A 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 A 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 A 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 A 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 A 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 A 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 A 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 A 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 A 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 A 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 A 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 A 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 A 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 A 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 A 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 A 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 A 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 A 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 A 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 B 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 B 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 B 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 B 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 B 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 B 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 B 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 B 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 B 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 B 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 B 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 B 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 B 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 B 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 B 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 B 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 B 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 B 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 B 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 B 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 B 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 C 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 C 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 C 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 C 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 C 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 C 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 C 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 C 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 C 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 C 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 C 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 C 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 C 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 C 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 C 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 C 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 C 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 C 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 C 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 C 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 C 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 D 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 D 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 D 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 D 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 D 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 D 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 D 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 D 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 D 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 D 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 D 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 D 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 D 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 D 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 D 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 D 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 D 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 D 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 D 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 D 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 D 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 E 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 E 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 E 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 E 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 E 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 E 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 E 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 E 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 E 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 E 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 E 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 E 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 E 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 E 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 E 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 E 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 E 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 E 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 E 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 E 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 E 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 F 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 F 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 F 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 F 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 F 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 F 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 F 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 F 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 F 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 F 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 F 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 F 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 F 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 F 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 F 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 F 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 F 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 F 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 F 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 F 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 F 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
HET NAD A1270 44
HET NAD B1270 44
HET NAD C1270 44
HET NAD F1270 44
HET NAD E1270 44
HET NAD D1270 44
HET NA A1271 1
HET VMY A1272 29
HET VMY B1271 29
HET VMY C1271 29
HET VMY D1271 29
HET VMY E1271 29
HET VMY F1271 29
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM NA SODIUM ION
HETNAM VMY (1S)-1-(5-{[1-(2,6-DIFLUOROBENZYL)-1H-
HETNAM 2 VMY PYRAZOL-3-YL]AMINO}-1,3,4-THIADIAZOL-2-YL)-1-(4-
HETNAM 3 VMY METHYL-1,3-THIAZOL-2-YL)ETHANOL
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM NA SODIUM ION
FORMUL 7 NAD 6(C21 H27 N7 O14 P2)
FORMUL 8 NA NA 1+
FORMUL 9 VMY 6(C18 H16 F2 N6 O S2)
FORMUL 10 HOH *450(H2 O)
HELIX 1 1 SER A 20 GLN A 32 1 13
HELIX 2 2 ARG A 43 ASP A 52 1 10
HELIX 3 3 ASN A 67 GLY A 83 1 17
HELIX 4 4 PRO A 107 ALA A 111 5 5
HELIX 5 5 PRO A 112 ALA A 124 1 13
HELIX 6 6 ALA A 124 LEU A 135 1 12
HELIX 7 7 ASN A 159 LYS A 181 1 23
HELIX 8 8 THR A 196 GLY A 205 1 10
HELIX 9 9 GLY A 208 ALA A 226 1 19
HELIX 10 10 ALA A 235 SER A 247 1 13
HELIX 11 11 GLY A 263 GLN A 267 5 5
HELIX 12 12 SER B 20 GLN B 32 1 13
HELIX 13 13 ARG B 43 ASP B 52 1 10
HELIX 14 14 ASN B 67 GLY B 83 1 17
HELIX 15 15 PRO B 107 ALA B 111 5 5
HELIX 16 16 PRO B 112 ALA B 124 1 13
HELIX 17 17 ALA B 124 LEU B 135 1 12
HELIX 18 18 ASN B 159 LYS B 181 1 23
HELIX 19 19 THR B 196 GLY B 205 1 10
HELIX 20 20 GLY B 208 ALA B 226 1 19
HELIX 21 21 ALA B 235 SER B 247 1 13
HELIX 22 22 GLY B 263 GLN B 267 5 5
HELIX 23 23 SER C 20 GLN C 32 1 13
HELIX 24 24 ARG C 43 ASP C 52 1 10
HELIX 25 25 ASN C 67 GLY C 83 1 17
HELIX 26 26 PRO C 99 MET C 103 5 5
HELIX 27 27 PRO C 107 ALA C 111 5 5
HELIX 28 28 PRO C 112 ALA C 124 1 13
HELIX 29 29 ALA C 124 LEU C 135 1 12
HELIX 30 30 ASN C 159 LYS C 181 1 23
HELIX 31 31 THR C 196 GLY C 205 1 10
HELIX 32 32 GLY C 208 ALA C 226 1 19
HELIX 33 33 ALA C 235 SER C 247 1 13
HELIX 34 34 GLY C 263 GLN C 267 5 5
HELIX 35 35 SER D 20 GLN D 32 1 13
HELIX 36 36 ARG D 43 ASP D 52 1 10
HELIX 37 37 ASN D 67 GLY D 83 1 17
HELIX 38 38 PRO D 107 ALA D 111 5 5
HELIX 39 39 PRO D 112 ALA D 124 1 13
HELIX 40 40 ALA D 124 LEU D 135 1 12
HELIX 41 41 TYR D 158 LYS D 181 1 24
HELIX 42 42 THR D 196 GLY D 205 1 10
HELIX 43 43 GLY D 208 ALA D 226 1 19
HELIX 44 44 ALA D 235 SER D 247 1 13
HELIX 45 45 GLY D 263 GLN D 267 5 5
HELIX 46 46 SER E 20 GLN E 32 1 13
HELIX 47 47 ARG E 45 ASP E 52 1 8
HELIX 48 48 ASN E 67 GLY E 83 1 17
HELIX 49 49 PRO E 107 ALA E 111 5 5
HELIX 50 50 PRO E 112 ALA E 124 1 13
HELIX 51 51 ALA E 124 LEU E 135 1 12
HELIX 52 52 ASN E 159 LYS E 181 1 23
HELIX 53 53 GLY E 208 ALA E 226 1 19
HELIX 54 54 ALA E 235 SER E 247 1 13
HELIX 55 55 GLY E 263 GLN E 267 5 5
HELIX 56 56 SER F 20 GLN F 32 1 13
HELIX 57 57 ARG F 43 ASP F 52 1 10
HELIX 58 58 ASN F 67 GLY F 83 1 17
HELIX 59 59 PRO F 107 ALA F 111 5 5
HELIX 60 60 PRO F 112 ALA F 124 1 13
HELIX 61 61 ALA F 124 LEU F 135 1 12
HELIX 62 62 ASN F 159 LYS F 181 1 23
HELIX 63 63 GLY F 221 ALA F 226 1 6
HELIX 64 64 ALA F 235 SER F 247 1 13
HELIX 65 65 GLY F 263 GLN F 267 5 5
SHEET 1 AA 7 LEU A 60 GLU A 62 0
SHEET 2 AA 7 GLN A 35 GLY A 40 1 O LEU A 38 N LEU A 61
SHEET 3 AA 7 ARG A 9 SER A 13 1 O ILE A 10 N VAL A 37
SHEET 4 AA 7 LEU A 88 HIS A 93 1 N ASP A 89 O ARG A 9
SHEET 5 AA 7 MET A 138 ASP A 148 1 N ASN A 139 O LEU A 88
SHEET 6 AA 7 ARG A 185 ALA A 191 1 O ARG A 185 N ILE A 144
SHEET 7 AA 7 ASP A 256 ALA A 260 1 O ASP A 256 N LEU A 188
SHEET 1 BA 7 LEU B 60 GLU B 62 0
SHEET 2 BA 7 GLN B 35 GLY B 40 1 O LEU B 38 N LEU B 61
SHEET 3 BA 7 ARG B 9 SER B 13 1 O ILE B 10 N VAL B 37
SHEET 4 BA 7 LEU B 88 HIS B 93 1 N ASP B 89 O ARG B 9
SHEET 5 BA 7 MET B 138 ASP B 148 1 N ASN B 139 O LEU B 88
SHEET 6 BA 7 ARG B 185 ALA B 191 1 O ARG B 185 N ILE B 144
SHEET 7 BA 7 ASP B 256 ALA B 260 1 O ASP B 256 N LEU B 188
SHEET 1 CA 7 LEU C 60 GLU C 62 0
SHEET 2 CA 7 GLN C 35 GLY C 40 1 O LEU C 38 N LEU C 61
SHEET 3 CA 7 ARG C 9 SER C 13 1 O ILE C 10 N VAL C 37
SHEET 4 CA 7 LEU C 88 HIS C 93 1 N ASP C 89 O ARG C 9
SHEET 5 CA 7 MET C 138 ASP C 148 1 N ASN C 139 O LEU C 88
SHEET 6 CA 7 ARG C 185 ALA C 191 1 O ARG C 185 N ILE C 144
SHEET 7 CA 7 ASP C 256 ALA C 260 1 O ASP C 256 N LEU C 188
SHEET 1 DA 7 LEU D 60 GLU D 62 0
SHEET 2 DA 7 GLN D 35 GLY D 40 1 O LEU D 38 N LEU D 61
SHEET 3 DA 7 ARG D 9 SER D 13 1 O ILE D 10 N VAL D 37
SHEET 4 DA 7 LEU D 88 HIS D 93 1 N ASP D 89 O ARG D 9
SHEET 5 DA 7 MET D 138 ASP D 148 1 N ASN D 139 O LEU D 88
SHEET 6 DA 7 ARG D 185 ALA D 191 1 O ARG D 185 N ILE D 144
SHEET 7 DA 7 ASP D 256 ALA D 260 1 O ASP D 256 N LEU D 188
SHEET 1 EA 7 LEU E 60 GLU E 62 0
SHEET 2 EA 7 GLN E 35 GLY E 40 1 O LEU E 38 N LEU E 61
SHEET 3 EA 7 ARG E 9 SER E 13 1 O ILE E 10 N VAL E 37
SHEET 4 EA 7 LEU E 88 HIS E 93 1 N ASP E 89 O ARG E 9
SHEET 5 EA 7 MET E 138 ASP E 148 1 N ASN E 139 O LEU E 88
SHEET 6 EA 7 ARG E 185 ALA E 191 1 O ARG E 185 N ILE E 144
SHEET 7 EA 7 ASP E 256 ALA E 260 1 O ASP E 256 N LEU E 188
SHEET 1 FA 7 LEU F 60 GLU F 62 0
SHEET 2 FA 7 GLN F 35 GLY F 40 1 O LEU F 38 N LEU F 61
SHEET 3 FA 7 ARG F 9 SER F 13 1 O ILE F 10 N VAL F 37
SHEET 4 FA 7 LEU F 88 HIS F 93 1 N ASP F 89 O ARG F 9
SHEET 5 FA 7 MET F 138 ASP F 148 1 N ASN F 139 O LEU F 88
SHEET 6 FA 7 ARG F 185 ALA F 191 1 O ARG F 185 N ILE F 144
SHEET 7 FA 7 ASP F 256 ALA F 260 1 O ASP F 256 N LEU F 188
LINK NA NA A1271 O HOH A2082 1555 1555 2.66
LINK NA NA A1271 O HOH A2081 1555 1555 2.27
LINK NA NA A1271 O HOH A2085 1555 1555 2.50
LINK NA NA A1271 O ASP A 223 1555 1555 2.60
LINK NA NA A1271 O GLN A 224 1555 1555 2.74
LINK NA NA A1271 O ALA A 226 1555 1555 2.47
SITE 1 AC1 31 GLY A 14 ILE A 15 ILE A 16 SER A 20
SITE 2 AC1 31 ILE A 21 PHE A 41 LEU A 63 ASP A 64
SITE 3 AC1 31 VAL A 65 SER A 94 ILE A 95 GLY A 96
SITE 4 AC1 31 ILE A 122 MET A 147 ASP A 148 PHE A 149
SITE 5 AC1 31 LYS A 165 ALA A 191 PRO A 193 ILE A 194
SITE 6 AC1 31 THR A 196 VMY A1272 HOH A2005 HOH A2006
SITE 7 AC1 31 HOH A2007 HOH A2008 HOH A2021 HOH A2033
SITE 8 AC1 31 HOH A2062 HOH A2075 HOH A2101
SITE 1 AC2 30 GLY B 14 ILE B 15 ILE B 16 SER B 20
SITE 2 AC2 30 ILE B 21 PHE B 41 LEU B 63 ASP B 64
SITE 3 AC2 30 VAL B 65 SER B 94 ILE B 95 GLY B 96
SITE 4 AC2 30 ILE B 122 MET B 147 ASP B 148 PHE B 149
SITE 5 AC2 30 LYS B 165 ALA B 191 PRO B 193 ILE B 194
SITE 6 AC2 30 THR B 196 MET B 199 VMY B1271 HOH B2004
SITE 7 AC2 30 HOH B2005 HOH B2006 HOH B2007 HOH B2020
SITE 8 AC2 30 HOH B2066 HOH B2101
SITE 1 AC3 29 GLY C 14 ILE C 15 ILE C 16 SER C 20
SITE 2 AC3 29 ILE C 21 PHE C 41 LEU C 63 ASP C 64
SITE 3 AC3 29 VAL C 65 SER C 94 ILE C 95 GLY C 96
SITE 4 AC3 29 ILE C 122 MET C 147 ASP C 148 PHE C 149
SITE 5 AC3 29 LYS C 165 ALA C 191 GLY C 192 PRO C 193
SITE 6 AC3 29 ILE C 194 THR C 196 VMY C1271 HOH C2002
SITE 7 AC3 29 HOH C2003 HOH C2004 HOH C2025 HOH C2026
SITE 8 AC3 29 HOH C2035
SITE 1 AC4 24 GLY F 14 ILE F 15 ILE F 16 SER F 20
SITE 2 AC4 24 ILE F 21 PHE F 41 LEU F 63 ASP F 64
SITE 3 AC4 24 VAL F 65 SER F 94 ILE F 95 GLY F 96
SITE 4 AC4 24 ILE F 122 MET F 147 ASP F 148 PHE F 149
SITE 5 AC4 24 MET F 161 LYS F 165 ALA F 191 GLY F 192
SITE 6 AC4 24 PRO F 193 ILE F 194 THR F 196 VMY F1271
SITE 1 AC5 25 GLY E 14 ILE E 15 ILE E 16 SER E 20
SITE 2 AC5 25 ILE E 21 PHE E 41 LEU E 63 ASP E 64
SITE 3 AC5 25 VAL E 65 SER E 94 ILE E 95 GLY E 96
SITE 4 AC5 25 ILE E 122 MET E 147 ASP E 148 PHE E 149
SITE 5 AC5 25 LYS E 165 GLY E 192 PRO E 193 ILE E 194
SITE 6 AC5 25 THR E 196 VMY E1271 HOH E2004 HOH E2005
SITE 7 AC5 25 HOH E2020
SITE 1 AC6 25 GLY D 14 ILE D 15 ILE D 16 SER D 20
SITE 2 AC6 25 ILE D 21 PHE D 41 LEU D 63 ASP D 64
SITE 3 AC6 25 VAL D 65 SER D 94 ILE D 95 GLY D 96
SITE 4 AC6 25 ILE D 122 MET D 147 ASP D 148 PHE D 149
SITE 5 AC6 25 LYS D 165 ILE D 194 THR D 196 MET D 199
SITE 6 AC6 25 VMY D1271 HOH D2005 HOH D2012 HOH D2052
SITE 7 AC6 25 HOH D2053
SITE 1 AC7 6 ASP A 223 GLN A 224 ALA A 226 HOH A2081
SITE 2 AC7 6 HOH A2082 HOH A2085
SITE 1 AC8 13 GLY A 96 PHE A 97 MET A 98 MET A 103
SITE 2 AC8 13 GLY A 104 TYR A 158 MET A 161 ALA A 198
SITE 3 AC8 13 MET A 199 ILE A 202 LEU A 207 NAD A1270
SITE 4 AC8 13 HOH A2075
SITE 1 AC9 14 GLY B 96 PHE B 97 MET B 98 MET B 103
SITE 2 AC9 14 GLY B 104 PHE B 149 TYR B 158 MET B 161
SITE 3 AC9 14 ALA B 198 MET B 199 ILE B 202 LEU B 207
SITE 4 AC9 14 NAD B1270 HOH B2101
SITE 1 BC1 10 GLY C 96 PHE C 97 MET C 98 MET C 103
SITE 2 BC1 10 GLY C 104 MET C 161 ALA C 198 ILE C 202
SITE 3 BC1 10 ILE C 215 NAD C1270
SITE 1 BC2 11 GLY D 96 PHE D 97 MET D 98 MET D 103
SITE 2 BC2 11 GLY D 104 TYR D 158 MET D 161 ALA D 198
SITE 3 BC2 11 MET D 199 LEU D 207 NAD D1270
SITE 1 BC3 9 GLY E 96 PHE E 97 MET E 98 GLN E 100
SITE 2 BC3 9 MET E 103 GLY E 104 MET E 161 LEU E 207
SITE 3 BC3 9 NAD E1270
SITE 1 BC4 8 GLY F 96 PHE F 97 MET F 98 MET F 103
SITE 2 BC4 8 GLY F 104 ALA F 157 MET F 161 NAD F1270
CRYST1 101.297 81.304 189.004 90.00 95.25 90.00 C 1 2 1 24
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 0.009872 0.000000 0.000907 0.00000
SCALE2 0.000000 0.012300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005313 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
