HEADER OXIDOREDUCTASE 26-OCT-14 4D46
TITLE CRYSTAL STRUCTURE OF E. COLI FABI IN COMPLEX WITH NAD AND 5-BROMO-2-
TITLE 2 (4-CHLORO-2-HYDROXYPHENOXY)BENZONITRILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ENOYL-ACP REDUCTASE;
COMPND 5 EC: 1.3.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 469008;
SOURCE 4 STRAIN: BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS ENOYL-ACP REDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE SUPERFAMILY,
KEYWDS 2 ESCHERICHIA COLI, FATTY ACID BIOSYNTHESIS, LIPID SYNTHESIS, ECFABI,
KEYWDS 3 FABI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TAREILUS,J.SCHIEBEL,A.CHANG,P.J.TONGE,C.A.SOTRIFFER,C.KISKER
REVDAT 3 20-DEC-23 4D46 1 REMARK
REVDAT 2 15-APR-15 4D46 1 JRNL
REVDAT 1 04-MAR-15 4D46 0
JRNL AUTH J.SCHIEBEL,A.CHANG,B.MERGET,G.R.BOMMINENI,W.YU,
JRNL AUTH 2 L.A.SPAGNUOLO,M.V.BAXTER,M.TAREILUS,P.J.TONGE,C.KISKER,
JRNL AUTH 3 C.A.SOTRIFFER
JRNL TITL AN ORDERED WATER CHANNEL IN STAPHYLOCOCCUS AUREUS FABI:
JRNL TITL 2 UNRAVELING THE MECHANISM OF SUBSTRATE RECOGNITION AND
JRNL TITL 3 REDUCTION.
JRNL REF BIOCHEMISTRY V. 54 1943 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 25706582
JRNL DOI 10.1021/BI5014358
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39588
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2099
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2849
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 149
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3604
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.06000
REMARK 3 B22 (A**2) : 2.06000
REMARK 3 B33 (A**2) : -3.08000
REMARK 3 B12 (A**2) : 1.03000
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): 0.139
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.733
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3818 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5181 ; 1.752 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 489 ; 7.234 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 153 ;32.794 ;24.183
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 597 ;14.200 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;19.438 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 582 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3122 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2419 ; 1.616 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3839 ; 2.315 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1399 ; 3.851 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1339 ; 5.590 ; 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 : 8
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 2 A 147
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2434 29.5398 -13.8584
REMARK 3 T TENSOR
REMARK 3 T11: 0.0080 T22: 0.1818
REMARK 3 T33: 0.1062 T12: -0.0240
REMARK 3 T13: 0.0067 T23: -0.1157
REMARK 3 L TENSOR
REMARK 3 L11: 0.8744 L22: 0.3599
REMARK 3 L33: 1.1727 L12: 0.0701
REMARK 3 L13: 0.5019 L23: 0.3965
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: -0.0477 S13: 0.0106
REMARK 3 S21: -0.0130 S22: 0.1760 S23: -0.1004
REMARK 3 S31: -0.0816 S32: 0.3368 S33: -0.1613
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 : A 148 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): -31.6894 28.9298 -20.4672
REMARK 3 T TENSOR
REMARK 3 T11: 0.0197 T22: 0.0759
REMARK 3 T33: 0.0811 T12: -0.0165
REMARK 3 T13: -0.0098 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 0.6811 L22: 0.6520
REMARK 3 L33: 1.9835 L12: 0.1646
REMARK 3 L13: -0.1687 L23: 0.6395
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: -0.0921 S13: 0.0215
REMARK 3 S21: -0.0731 S22: 0.0361 S23: 0.0156
REMARK 3 S31: -0.0969 S32: 0.1263 S33: -0.0580
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 211 A 223
REMARK 3 ORIGIN FOR THE GROUP (A): -33.4161 9.3933 -12.4633
REMARK 3 T TENSOR
REMARK 3 T11: 0.4489 T22: 0.2351
REMARK 3 T33: 0.1869 T12: 0.0835
REMARK 3 T13: 0.0435 T23: 0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 18.3824 L22: 5.1031
REMARK 3 L33: 3.0186 L12: 3.7787
REMARK 3 L13: 3.6461 L23: 2.7025
REMARK 3 S TENSOR
REMARK 3 S11: -0.2027 S12: -1.3484 S13: -0.4901
REMARK 3 S21: 0.4074 S22: -0.0545 S23: 0.2387
REMARK 3 S31: 0.8054 S32: 0.0187 S33: 0.2572
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 224 A 257
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9687 17.1722 -23.0020
REMARK 3 T TENSOR
REMARK 3 T11: 0.0736 T22: 0.0854
REMARK 3 T33: 0.1112 T12: 0.0081
REMARK 3 T13: -0.0391 T23: -0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 0.6838 L22: 1.1002
REMARK 3 L33: 2.3589 L12: 0.5573
REMARK 3 L13: -0.1560 L23: 0.7184
REMARK 3 S TENSOR
REMARK 3 S11: 0.0981 S12: 0.0741 S13: -0.0675
REMARK 3 S21: 0.0365 S22: 0.0269 S23: -0.0342
REMARK 3 S31: 0.1736 S32: -0.0172 S33: -0.1250
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 87
REMARK 3 ORIGIN FOR THE GROUP (A): -55.3732 54.0400 -17.1138
REMARK 3 T TENSOR
REMARK 3 T11: 0.3351 T22: 0.1764
REMARK 3 T33: 0.2159 T12: 0.2313
REMARK 3 T13: -0.2260 T23: -0.1623
REMARK 3 L TENSOR
REMARK 3 L11: 1.2882 L22: 2.2394
REMARK 3 L33: 2.8138 L12: -0.0121
REMARK 3 L13: 0.3998 L23: 1.0630
REMARK 3 S TENSOR
REMARK 3 S11: -0.1901 S12: -0.0926 S13: 0.3671
REMARK 3 S21: -0.3593 S22: -0.3199 S23: 0.2912
REMARK 3 S31: -0.8598 S32: -0.5169 S33: 0.5100
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 88 B 188
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8980 41.2031 -18.9122
REMARK 3 T TENSOR
REMARK 3 T11: 0.1295 T22: 0.0577
REMARK 3 T33: 0.1050 T12: 0.0426
REMARK 3 T13: -0.0587 T23: -0.0695
REMARK 3 L TENSOR
REMARK 3 L11: 1.0753 L22: 0.5821
REMARK 3 L33: 1.3763 L12: -0.1050
REMARK 3 L13: -0.1090 L23: 0.8247
REMARK 3 S TENSOR
REMARK 3 S11: -0.0909 S12: -0.0402 S13: 0.1059
REMARK 3 S21: -0.2211 S22: -0.0704 S23: 0.0563
REMARK 3 S31: -0.3695 S32: -0.1724 S33: 0.1613
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 189 B 203
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3055 49.0374 -34.7352
REMARK 3 T TENSOR
REMARK 3 T11: 1.2829 T22: 0.3555
REMARK 3 T33: 0.5454 T12: 0.0180
REMARK 3 T13: -0.2137 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 6.9982 L22: 3.2054
REMARK 3 L33: 0.7195 L12: 4.7352
REMARK 3 L13: -2.2405 L23: -1.5155
REMARK 3 S TENSOR
REMARK 3 S11: -0.2201 S12: 1.0825 S13: 0.8858
REMARK 3 S21: -0.1171 S22: 0.6277 S23: 0.6083
REMARK 3 S31: 0.0082 S32: -0.3515 S33: -0.4076
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 210 B 257
REMARK 3 ORIGIN FOR THE GROUP (A): -52.9121 36.8469 -32.2917
REMARK 3 T TENSOR
REMARK 3 T11: 0.1685 T22: 0.0817
REMARK 3 T33: 0.1410 T12: 0.0971
REMARK 3 T13: -0.1151 T23: -0.0799
REMARK 3 L TENSOR
REMARK 3 L11: 2.2325 L22: 1.8688
REMARK 3 L33: 3.7065 L12: 0.0839
REMARK 3 L13: 0.6803 L23: 1.3605
REMARK 3 S TENSOR
REMARK 3 S11: -0.1576 S12: -0.1092 S13: 0.1891
REMARK 3 S21: -0.4045 S22: -0.1993 S23: 0.0411
REMARK 3 S31: -0.5738 S32: -0.1252 S33: 0.3569
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. VERY WEAK DENSITY FOR LOOP REGION 193-210 IN SUBUNIT
REMARK 3 A, WHICH WAS NOT INTERPRETED. VERY WEAK DENSITY FOR LOOP REGION
REMARK 3 204-209 IN SUBUNIT B, WHICH WAS NOT INTERPRETED. INHIBITOR
REMARK 3 DENSITY BETTER FOR SUBUNIT A, BUT STILL SUFFICIENT FOR B
REMARK 4
REMARK 4 4D46 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1290057469.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41818
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 46.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.00
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.20
REMARK 200 R MERGE FOR SHELL (I) : 1.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 1QSG
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08 M NH4AC, 0.1 M CAPS PH 10.5, 20%
REMARK 280 PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 107.43867
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 214.87733
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 161.15800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 268.59667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.71933
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 107.43867
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 214.87733
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 268.59667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 161.15800
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 53.71933
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.9 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 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -53.71933
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 A2149 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 ARG A 193
REMARK 465 THR A 194
REMARK 465 LEU A 195
REMARK 465 ALA A 196
REMARK 465 ALA A 197
REMARK 465 SER A 198
REMARK 465 GLY A 199
REMARK 465 ILE A 200
REMARK 465 LYS A 201
REMARK 465 ASP A 202
REMARK 465 PHE A 203
REMARK 465 ARG A 204
REMARK 465 LYS A 205
REMARK 465 MET A 206
REMARK 465 LEU A 207
REMARK 465 ALA A 208
REMARK 465 HIS A 209
REMARK 465 CYS A 210
REMARK 465 GLU A 258
REMARK 465 LEU A 259
REMARK 465 GLU A 260
REMARK 465 LEU A 261
REMARK 465 LYS A 262
REMARK 465 LEU A 263
REMARK 465 GLU A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 MET B 1
REMARK 465 ARG B 204
REMARK 465 LYS B 205
REMARK 465 MET B 206
REMARK 465 LEU B 207
REMARK 465 ALA B 208
REMARK 465 HIS B 209
REMARK 465 ASN B 257
REMARK 465 GLU B 258
REMARK 465 LEU B 259
REMARK 465 GLU B 260
REMARK 465 LEU B 261
REMARK 465 LYS B 262
REMARK 465 LEU B 263
REMARK 465 GLU B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU B 49 O HOH B 2021 1.88
REMARK 500 O HOH A 2089 O HOH A 2101 2.04
REMARK 500 O HOH A 2127 O HOH A 2129 2.07
REMARK 500 OE1 GLU A 67 O HOH A 2069 2.12
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 SER A 121 -57.08 -129.43
REMARK 500 SER A 145 -167.70 -127.99
REMARK 500 ASN A 155 -19.66 66.05
REMARK 500 ASN A 157 -124.38 50.33
REMARK 500 VAL A 247 68.19 -110.11
REMARK 500 SER B 121 -59.71 -125.37
REMARK 500 ASN B 155 -27.06 68.83
REMARK 500 ASN B 157 -131.06 54.11
REMARK 500 VAL B 247 70.45 -112.19
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 NAD A 1258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 1257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J47 A 1259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J47 B 1258
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4D41 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADP AND 5-
REMARK 900 HEXYL-2-(4-NITROPHENOXY)PHENOL
REMARK 900 RELATED ID: 4D42 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADP AND 4-
REMARK 900 FLUORO-5-HEXYL-2-PHENOXYPHENOL
REMARK 900 RELATED ID: 4D43 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADP AND 2-(2-
REMARK 900 CHLORO-4-NITROPHENOXY)-5-ETHYL-4- FLUOROPHENOL
REMARK 900 RELATED ID: 4D44 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADP AND 5-
REMARK 900 ETHYL-4-FLUORO-2-((2-FLUOROPYRIDIN-3-YL )OXY)PHENOL
REMARK 900 RELATED ID: 4D45 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADP AND 5-
REMARK 900 BROMO-2-(4-CHLORO-2-HYDROXYPHENOXY) BENZONITRILE
DBREF 4D46 A 1 262 UNP C6EFU4 C6EFU4_ECOBD 1 262
DBREF 4D46 B 1 262 UNP C6EFU4 C6EFU4_ECOBD 1 262
SEQADV 4D46 LEU A 263 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 GLU A 264 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS A 265 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS A 266 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS A 267 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS A 268 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS A 269 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS A 270 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 LEU B 263 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 GLU B 264 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS B 265 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS B 266 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS B 267 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS B 268 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS B 269 UNP C6EFU4 EXPRESSION TAG
SEQADV 4D46 HIS B 270 UNP C6EFU4 EXPRESSION TAG
SEQRES 1 A 270 MET GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY
SEQRES 2 A 270 VAL ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN
SEQRES 3 A 270 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 A 270 GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 A 270 ALA GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL
SEQRES 6 A 270 ALA GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU
SEQRES 7 A 270 GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER
SEQRES 8 A 270 ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR
SEQRES 9 A 270 VAL ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS
SEQRES 10 A 270 ASP ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA
SEQRES 11 A 270 CYS ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR
SEQRES 12 A 270 LEU SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR
SEQRES 13 A 270 ASN VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN
SEQRES 14 A 270 VAL ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL
SEQRES 15 A 270 ARG VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU
SEQRES 16 A 270 ALA ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA
SEQRES 17 A 270 HIS CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR
SEQRES 18 A 270 ILE GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER
SEQRES 19 A 270 ASP LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL
SEQRES 20 A 270 ASP GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU
SEQRES 21 A 270 LEU LYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 270 MET GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY
SEQRES 2 B 270 VAL ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN
SEQRES 3 B 270 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 B 270 GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 B 270 ALA GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL
SEQRES 6 B 270 ALA GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU
SEQRES 7 B 270 GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER
SEQRES 8 B 270 ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR
SEQRES 9 B 270 VAL ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS
SEQRES 10 B 270 ASP ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA
SEQRES 11 B 270 CYS ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR
SEQRES 12 B 270 LEU SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR
SEQRES 13 B 270 ASN VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN
SEQRES 14 B 270 VAL ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL
SEQRES 15 B 270 ARG VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU
SEQRES 16 B 270 ALA ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA
SEQRES 17 B 270 HIS CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR
SEQRES 18 B 270 ILE GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER
SEQRES 19 B 270 ASP LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL
SEQRES 20 B 270 ASP GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU
SEQRES 21 B 270 LEU LYS LEU GLU HIS HIS HIS HIS HIS HIS
HET NAD A1258 44
HET J47 A1259 18
HET NAD B1257 44
HET J47 B1258 18
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM J47 5-BROMO-2-(4-CHLORO-2-HYDROXYPHENOXY)BENZONITRILE
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 4 J47 2(C13 H7 BR CL N O2)
FORMUL 7 HOH *250(H2 O)
HELIX 1 1 SER A 19 GLU A 31 1 13
HELIX 2 2 ASN A 41 LEU A 55 1 15
HELIX 3 3 GLU A 67 LYS A 80 1 14
HELIX 4 4 PRO A 96 ASP A 101 5 6
HELIX 5 5 ASP A 103 VAL A 108 1 6
HELIX 6 6 THR A 109 SER A 121 1 13
HELIX 7 7 SER A 121 ARG A 132 1 12
HELIX 8 8 TYR A 146 GLU A 150 5 5
HELIX 9 9 ASN A 157 GLY A 178 1 22
HELIX 10 10 THR A 221 CYS A 233 1 13
HELIX 11 11 SER A 234 ALA A 238 5 5
HELIX 12 12 GLY A 250 ALA A 254 5 5
HELIX 13 13 SER B 19 GLU B 31 1 13
HELIX 14 14 ASN B 41 LYS B 43 5 3
HELIX 15 15 LEU B 44 LEU B 55 1 12
HELIX 16 16 GLU B 67 LYS B 80 1 14
HELIX 17 17 PRO B 96 ASP B 101 5 6
HELIX 18 18 ASP B 103 VAL B 108 1 6
HELIX 19 19 THR B 109 SER B 121 1 13
HELIX 20 20 SER B 121 ARG B 132 1 12
HELIX 21 21 TYR B 146 GLU B 150 5 5
HELIX 22 22 ASN B 157 GLY B 178 1 22
HELIX 23 23 THR B 194 SER B 198 5 5
HELIX 24 24 THR B 221 CYS B 233 1 13
HELIX 25 25 SER B 234 ALA B 238 5 5
HELIX 26 26 GLY B 250 ALA B 254 5 5
SHEET 1 AA 7 VAL A 60 GLN A 62 0
SHEET 2 AA 7 GLU A 34 TYR A 39 1 O PHE A 37 N LEU A 61
SHEET 3 AA 7 ARG A 8 VAL A 11 1 O ILE A 9 N ALA A 36
SHEET 4 AA 7 PHE A 85 HIS A 90 1 N ASP A 86 O ARG A 8
SHEET 5 AA 7 LEU A 135 SER A 145 1 N ASN A 136 O PHE A 85
SHEET 6 AA 7 VAL A 182 ALA A 189 1 O ARG A 183 N LEU A 141
SHEET 7 AA 7 VAL A 244 VAL A 247 1 O VAL A 245 N SER A 188
SHEET 1 BA 7 VAL B 60 GLN B 62 0
SHEET 2 BA 7 GLU B 34 TYR B 39 1 O PHE B 37 N LEU B 61
SHEET 3 BA 7 ARG B 8 VAL B 11 1 O ILE B 9 N ALA B 36
SHEET 4 BA 7 PHE B 85 HIS B 90 1 N ASP B 86 O ARG B 8
SHEET 5 BA 7 LEU B 135 SER B 145 1 N ASN B 136 O PHE B 85
SHEET 6 BA 7 VAL B 182 ALA B 189 1 O ARG B 183 N LEU B 141
SHEET 7 BA 7 VAL B 244 VAL B 247 1 O VAL B 245 N SER B 188
SITE 1 AC1 26 GLY A 13 VAL A 14 ALA A 15 SER A 19
SITE 2 AC1 26 ILE A 20 GLN A 40 LEU A 44 CYS A 63
SITE 3 AC1 26 ASP A 64 VAL A 65 SER A 91 ILE A 92
SITE 4 AC1 26 LEU A 144 SER A 145 LYS A 163 ALA A 189
SITE 5 AC1 26 GLY A 190 PRO A 191 ILE A 192 J47 A1259
SITE 6 AC1 26 HOH A2009 HOH A2010 HOH A2012 HOH A2014
SITE 7 AC1 26 HOH A2083 HOH A2156
SITE 1 AC2 25 GLY B 13 ALA B 15 SER B 19 ILE B 20
SITE 2 AC2 25 GLN B 40 CYS B 63 ASP B 64 VAL B 65
SITE 3 AC2 25 SER B 91 ILE B 92 LEU B 144 SER B 145
SITE 4 AC2 25 LYS B 163 ALA B 189 GLY B 190 PRO B 191
SITE 5 AC2 25 ILE B 192 THR B 194 LEU B 195 ALA B 196
SITE 6 AC2 25 J47 B1258 HOH B2006 HOH B2007 HOH B2016
SITE 7 AC2 25 HOH B2037
SITE 1 AC3 6 GLY A 93 ALA A 95 LEU A 100 TYR A 146
SITE 2 AC3 6 TYR A 156 NAD A1258
SITE 1 AC4 7 GLY B 93 ALA B 95 LEU B 100 TYR B 146
SITE 2 AC4 7 TYR B 156 ALA B 196 NAD B1257
CRYST1 79.144 79.144 322.316 90.00 90.00 120.00 P 61 2 2 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 0.012635 0.007295 0.000000 0.00000
SCALE2 0.000000 0.014590 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003103 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
