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HEADER HYDROLASE 03-MAR-18 6FVJ
TITLE TESA A MAJOR THIOESTERASE FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: THIOESTERASE TESA;
COMPND 5 EC: 6.3.2.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: MBTB_1, MBTB_2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TESA, THIOESTERASE, MYCOBACTERIUM TUBERCULOSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CAMBILLAU,V.S.NGUYEN,S.CANAAN
REVDAT 1 24-OCT-18 6FVJ 0
JRNL AUTH P.C.NGUYEN,V.S.NGUYEN,B.P.MARTIN,P.FOURQUET,L.CAMOIN,
JRNL AUTH 2 C.D.SPILLING,J.F.CAVALIER,C.CAMBILLAU,S.CANAAN
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF TESA, A MAJOR
JRNL TITL 2 THIOESTERASE REQUIRED FOR OUTER-ENVELOPE LIPID BIOSYNTHESIS
JRNL TITL 3 IN MYCOBACTERIUM TUBERCULOSIS.
JRNL REF J. MOL. BIOL. 2018
JRNL REFN ESSN 1089-8638
JRNL PMID 30292819
JRNL DOI 10.1016/J.JMB.2018.09.017
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 61125
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3056
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.67
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.64
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4464
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2596
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4241
REMARK 3 BIN R VALUE (WORKING SET) : 0.2596
REMARK 3 BIN FREE R VALUE : 0.2595
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 223
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 : 12935
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 148
REMARK 3 SOLVENT ATOMS : 466
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.39450
REMARK 3 B22 (A**2) : 1.56090
REMARK 3 B33 (A**2) : -0.16640
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.420
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.898
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.313
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.857
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.316
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 : 0.917
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 13427 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 18267 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4310 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 2252 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 13427 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1767 ; 5.000 ; 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 : 15215 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.02
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.13
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.02
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 117.5560 263.9310 -202.3050
REMARK 3 T TENSOR
REMARK 3 T11: -0.0242 T22: 0.0053
REMARK 3 T33: 0.0069 T12: -0.0196
REMARK 3 T13: -0.0110 T23: 0.1431
REMARK 3 L TENSOR
REMARK 3 L11: 1.8020 L22: 1.0694
REMARK 3 L33: 0.8650 L12: 0.2015
REMARK 3 L13: 0.1297 L23: -1.2647
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: 0.0067 S13: -0.0015
REMARK 3 S21: -0.0217 S22: -0.0055 S23: 0.0394
REMARK 3 S31: -0.0068 S32: -0.0065 S33: 0.0089
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 156.0430 263.1630 -204.2580
REMARK 3 T TENSOR
REMARK 3 T11: -0.0491 T22: -0.0403
REMARK 3 T33: 0.0622 T12: -0.0625
REMARK 3 T13: 0.0378 T23: 0.0796
REMARK 3 L TENSOR
REMARK 3 L11: 1.9978 L22: 0.7835
REMARK 3 L33: 0.6584 L12: 0.3904
REMARK 3 L13: -0.2483 L23: -0.6255
REMARK 3 S TENSOR
REMARK 3 S11: 0.0037 S12: 0.0136 S13: 0.0136
REMARK 3 S21: -0.0308 S22: -0.0058 S23: -0.0320
REMARK 3 S31: -0.0047 S32: 0.0040 S33: 0.0021
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 106.3910 242.9930 -182.2160
REMARK 3 T TENSOR
REMARK 3 T11: -0.0536 T22: 0.0991
REMARK 3 T33: -0.0835 T12: -0.0319
REMARK 3 T13: 0.0191 T23: 0.0883
REMARK 3 L TENSOR
REMARK 3 L11: 1.8079 L22: 0.0055
REMARK 3 L33: 1.8434 L12: 0.3494
REMARK 3 L13: -0.9254 L23: -0.4669
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0099 S13: -0.0073
REMARK 3 S21: 0.0017 S22: 0.0068 S23: 0.0073
REMARK 3 S31: 0.0298 S32: 0.0038 S33: -0.0053
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 145.0030 242.2020 -184.0610
REMARK 3 T TENSOR
REMARK 3 T11: -0.0075 T22: 0.0360
REMARK 3 T33: -0.0536 T12: -0.0223
REMARK 3 T13: 0.0082 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 1.4311 L22: 0.4695
REMARK 3 L33: 1.0868 L12: -0.6489
REMARK 3 L13: -0.0147 L23: -0.7413
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.0193 S13: -0.0348
REMARK 3 S21: -0.0005 S22: -0.0030 S23: -0.0075
REMARK 3 S31: 0.0207 S32: 0.0156 S33: 0.0065
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 127.3250 298.1430 -204.2780
REMARK 3 T TENSOR
REMARK 3 T11: -0.0100 T22: -0.0640
REMARK 3 T33: -0.0206 T12: 0.0137
REMARK 3 T13: 0.0159 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.0831 L22: 1.8339
REMARK 3 L33: 0.0000 L12: 1.0814
REMARK 3 L13: -0.3336 L23: -0.1644
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: 0.0144 S13: 0.0129
REMARK 3 S21: 0.0108 S22: 0.0098 S23: -0.0028
REMARK 3 S31: -0.0335 S32: -0.0003 S33: -0.0124
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { F|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 126.2880 264.2870 -238.7320
REMARK 3 T TENSOR
REMARK 3 T11: -0.0274 T22: -0.0927
REMARK 3 T33: 0.0864 T12: 0.0587
REMARK 3 T13: 0.0549 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 0.5496 L22: 1.2059
REMARK 3 L33: 0.0000 L12: -1.2977
REMARK 3 L13: 0.3278 L23: -0.3012
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: -0.0227 S13: 0.0203
REMARK 3 S21: 0.0006 S22: -0.0160 S23: -0.0482
REMARK 3 S31: 0.0097 S32: 0.0116 S33: 0.0177
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { G|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 134.4050 320.1970 -182.2430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0262 T22: -0.0406
REMARK 3 T33: -0.0544 T12: -0.0025
REMARK 3 T13: -0.0378 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 0.1365 L22: 0.2563
REMARK 3 L33: 0.2929 L12: 0.1823
REMARK 3 L13: 0.2456 L23: 1.3015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.0090 S13: -0.0111
REMARK 3 S21: 0.0291 S22: -0.0016 S23: -0.0118
REMARK 3 S31: 0.0259 S32: -0.0103 S33: 0.0010
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { H|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 93.8810 319.3070 -183.5680
REMARK 3 T TENSOR
REMARK 3 T11: -0.0023 T22: -0.0407
REMARK 3 T33: 0.0111 T12: -0.0149
REMARK 3 T13: -0.0892 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 0.0089 L22: 0.1995
REMARK 3 L33: 0.0000 L12: 0.0849
REMARK 3 L13: 1.3380 L23: -0.4530
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: 0.0003 S13: -0.0068
REMARK 3 S21: -0.0117 S22: 0.0017 S23: 0.0038
REMARK 3 S31: -0.0032 S32: 0.0128 S33: -0.0027
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6FVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61244
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 43.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 0.90700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% PEG 600, 0.1 M HEPES PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 111.10500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 111.10500
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 39.53500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 112.29000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.53500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 112.29000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 111.10500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.53500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 112.29000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 111.10500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.53500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 112.29000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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 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 D 478 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 LEU A 2
REMARK 465 ALA A 3
REMARK 465 ARG A 4
REMARK 465 HIS A 5
REMARK 465 GLY A 6
REMARK 465 PRO A 7
REMARK 465 ARG A 8
REMARK 465 TYR A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 SER A 12
REMARK 465 VAL A 13
REMARK 465 ASN A 14
REMARK 465 GLY A 15
REMARK 465 HIS A 16
REMARK 465 SER A 17
REMARK 465 ASP A 18
REMARK 465 ASP A 19
REMARK 465 SER A 20
REMARK 465 SER A 21
REMARK 465 GLY A 22
REMARK 465 ASP A 23
REMARK 465 ALA A 24
REMARK 465 LYS A 25
REMARK 465 GLN A 26
REMARK 465 GLN A 65
REMARK 465 HIS A 66
REMARK 465 ASP A 67
REMARK 465 ARG A 68
REMARK 465 SER A 69
REMARK 465 GLY A 70
REMARK 465 LEU A 71
REMARK 465 PRO A 72
REMARK 465 THR A 156
REMARK 465 ARG A 157
REMARK 465 MET A 158
REMARK 465 THR A 159
REMARK 465 GLY A 160
REMARK 465 MET A 161
REMARK 465 ASN A 162
REMARK 465 PRO A 163
REMARK 465 ASP A 164
REMARK 465 PHE A 165
REMARK 465 PHE A 166
REMARK 465 THR A 167
REMARK 465 ASP A 168
REMARK 465 ASP A 169
REMARK 465 GLU A 170
REMARK 465 PHE A 171
REMARK 465 ARG A 260
REMARK 465 ALA A 261
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 ALA B 3
REMARK 465 ARG B 4
REMARK 465 HIS B 5
REMARK 465 GLY B 6
REMARK 465 PRO B 7
REMARK 465 ARG B 8
REMARK 465 TYR B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 SER B 12
REMARK 465 VAL B 13
REMARK 465 ASN B 14
REMARK 465 GLY B 15
REMARK 465 HIS B 16
REMARK 465 SER B 17
REMARK 465 ASP B 18
REMARK 465 ASP B 19
REMARK 465 SER B 20
REMARK 465 SER B 21
REMARK 465 GLY B 22
REMARK 465 ASP B 23
REMARK 465 ALA B 24
REMARK 465 LYS B 25
REMARK 465 GLN B 26
REMARK 465 GLN B 65
REMARK 465 HIS B 66
REMARK 465 ASP B 67
REMARK 465 ARG B 68
REMARK 465 SER B 69
REMARK 465 GLY B 70
REMARK 465 LEU B 71
REMARK 465 PRO B 72
REMARK 465 PRO B 73
REMARK 465 THR B 159
REMARK 465 GLY B 160
REMARK 465 MET B 161
REMARK 465 ASN B 162
REMARK 465 PRO B 163
REMARK 465 ASP B 164
REMARK 465 PHE B 165
REMARK 465 PHE B 166
REMARK 465 THR B 167
REMARK 465 ASP B 168
REMARK 465 ASP B 169
REMARK 465 GLU B 170
REMARK 465 PHE B 171
REMARK 465 ALA B 261
REMARK 465 MET C 1
REMARK 465 LEU C 2
REMARK 465 ALA C 3
REMARK 465 ARG C 4
REMARK 465 HIS C 5
REMARK 465 GLY C 6
REMARK 465 PRO C 7
REMARK 465 ARG C 8
REMARK 465 TYR C 9
REMARK 465 GLY C 10
REMARK 465 GLY C 11
REMARK 465 SER C 12
REMARK 465 VAL C 13
REMARK 465 ASN C 14
REMARK 465 GLY C 15
REMARK 465 HIS C 16
REMARK 465 SER C 17
REMARK 465 ASP C 18
REMARK 465 ASP C 19
REMARK 465 SER C 20
REMARK 465 SER C 21
REMARK 465 GLY C 22
REMARK 465 ASP C 23
REMARK 465 ALA C 24
REMARK 465 LYS C 25
REMARK 465 GLN C 26
REMARK 465 ALA C 27
REMARK 465 GLN C 65
REMARK 465 HIS C 66
REMARK 465 ASP C 67
REMARK 465 ARG C 68
REMARK 465 SER C 69
REMARK 465 GLY C 70
REMARK 465 LEU C 71
REMARK 465 PRO C 72
REMARK 465 PRO C 73
REMARK 465 ARG C 157
REMARK 465 MET C 158
REMARK 465 THR C 159
REMARK 465 GLY C 160
REMARK 465 MET C 161
REMARK 465 ASN C 162
REMARK 465 PRO C 163
REMARK 465 ASP C 164
REMARK 465 PHE C 165
REMARK 465 PHE C 166
REMARK 465 THR C 167
REMARK 465 ASP C 168
REMARK 465 ASP C 169
REMARK 465 GLU C 170
REMARK 465 PHE C 171
REMARK 465 PHE C 172
REMARK 465 VAL C 173
REMARK 465 ASP C 259
REMARK 465 ARG C 260
REMARK 465 ALA C 261
REMARK 465 MET D 1
REMARK 465 LEU D 2
REMARK 465 ALA D 3
REMARK 465 ARG D 4
REMARK 465 HIS D 5
REMARK 465 GLY D 6
REMARK 465 PRO D 7
REMARK 465 ARG D 8
REMARK 465 TYR D 9
REMARK 465 GLY D 10
REMARK 465 GLY D 11
REMARK 465 SER D 12
REMARK 465 VAL D 13
REMARK 465 ASN D 14
REMARK 465 GLY D 15
REMARK 465 HIS D 16
REMARK 465 SER D 17
REMARK 465 ASP D 18
REMARK 465 ASP D 19
REMARK 465 SER D 20
REMARK 465 SER D 21
REMARK 465 GLY D 22
REMARK 465 ASP D 23
REMARK 465 GLN D 65
REMARK 465 HIS D 66
REMARK 465 ASP D 67
REMARK 465 ARG D 68
REMARK 465 SER D 69
REMARK 465 THR D 159
REMARK 465 GLY D 160
REMARK 465 MET D 161
REMARK 465 ASN D 162
REMARK 465 PRO D 163
REMARK 465 ASP D 164
REMARK 465 PHE D 165
REMARK 465 PHE D 166
REMARK 465 THR D 167
REMARK 465 ALA D 261
REMARK 465 MET E 1
REMARK 465 LEU E 2
REMARK 465 ALA E 3
REMARK 465 ARG E 4
REMARK 465 HIS E 5
REMARK 465 GLY E 6
REMARK 465 PRO E 7
REMARK 465 ARG E 8
REMARK 465 TYR E 9
REMARK 465 GLY E 10
REMARK 465 GLY E 11
REMARK 465 SER E 12
REMARK 465 VAL E 13
REMARK 465 ASN E 14
REMARK 465 GLY E 15
REMARK 465 HIS E 16
REMARK 465 SER E 17
REMARK 465 ASP E 18
REMARK 465 ASP E 19
REMARK 465 SER E 20
REMARK 465 SER E 21
REMARK 465 GLY E 22
REMARK 465 ASP E 23
REMARK 465 ALA E 24
REMARK 465 LYS E 25
REMARK 465 GLN E 26
REMARK 465 ALA E 27
REMARK 465 GLN E 65
REMARK 465 HIS E 66
REMARK 465 ASP E 67
REMARK 465 ARG E 68
REMARK 465 SER E 69
REMARK 465 GLY E 70
REMARK 465 THR E 159
REMARK 465 GLY E 160
REMARK 465 MET E 161
REMARK 465 ASN E 162
REMARK 465 PRO E 163
REMARK 465 ASP E 164
REMARK 465 PHE E 165
REMARK 465 PHE E 166
REMARK 465 THR E 167
REMARK 465 ASP E 168
REMARK 465 ASP E 169
REMARK 465 GLU E 170
REMARK 465 PHE E 171
REMARK 465 ARG E 260
REMARK 465 ALA E 261
REMARK 465 MET F 1
REMARK 465 LEU F 2
REMARK 465 ALA F 3
REMARK 465 ARG F 4
REMARK 465 HIS F 5
REMARK 465 GLY F 6
REMARK 465 PRO F 7
REMARK 465 ARG F 8
REMARK 465 TYR F 9
REMARK 465 GLY F 10
REMARK 465 GLY F 11
REMARK 465 SER F 12
REMARK 465 VAL F 13
REMARK 465 ASN F 14
REMARK 465 GLY F 15
REMARK 465 HIS F 16
REMARK 465 SER F 17
REMARK 465 ASP F 18
REMARK 465 ASP F 19
REMARK 465 SER F 20
REMARK 465 SER F 21
REMARK 465 GLY F 22
REMARK 465 ASP F 23
REMARK 465 ALA F 24
REMARK 465 LYS F 25
REMARK 465 GLN F 26
REMARK 465 GLN F 65
REMARK 465 HIS F 66
REMARK 465 ASP F 67
REMARK 465 ARG F 68
REMARK 465 SER F 69
REMARK 465 GLY F 70
REMARK 465 LEU F 71
REMARK 465 PRO F 72
REMARK 465 PRO F 73
REMARK 465 ARG F 157
REMARK 465 MET F 158
REMARK 465 THR F 159
REMARK 465 GLY F 160
REMARK 465 MET F 161
REMARK 465 ASN F 162
REMARK 465 PRO F 163
REMARK 465 ASP F 164
REMARK 465 PHE F 165
REMARK 465 PHE F 166
REMARK 465 THR F 167
REMARK 465 ASP F 168
REMARK 465 ASP F 169
REMARK 465 GLU F 170
REMARK 465 PHE F 171
REMARK 465 ASP F 259
REMARK 465 ARG F 260
REMARK 465 ALA F 261
REMARK 465 MET G 1
REMARK 465 LEU G 2
REMARK 465 ALA G 3
REMARK 465 ARG G 4
REMARK 465 HIS G 5
REMARK 465 GLY G 6
REMARK 465 PRO G 7
REMARK 465 ARG G 8
REMARK 465 TYR G 9
REMARK 465 GLY G 10
REMARK 465 GLY G 11
REMARK 465 SER G 12
REMARK 465 VAL G 13
REMARK 465 ASN G 14
REMARK 465 GLY G 15
REMARK 465 HIS G 16
REMARK 465 SER G 17
REMARK 465 ASP G 18
REMARK 465 ASP G 19
REMARK 465 SER G 20
REMARK 465 SER G 21
REMARK 465 GLY G 22
REMARK 465 ASP G 23
REMARK 465 ALA G 24
REMARK 465 LYS G 25
REMARK 465 GLN G 26
REMARK 465 ALA G 27
REMARK 465 GLN G 65
REMARK 465 HIS G 66
REMARK 465 ASP G 67
REMARK 465 ARG G 68
REMARK 465 SER G 69
REMARK 465 GLY G 70
REMARK 465 LEU G 71
REMARK 465 PRO G 72
REMARK 465 PRO G 73
REMARK 465 THR G 156
REMARK 465 ARG G 157
REMARK 465 MET G 158
REMARK 465 THR G 159
REMARK 465 GLY G 160
REMARK 465 MET G 161
REMARK 465 ASN G 162
REMARK 465 PRO G 163
REMARK 465 ASP G 164
REMARK 465 PHE G 165
REMARK 465 PHE G 166
REMARK 465 THR G 167
REMARK 465 ASP G 168
REMARK 465 ASP G 169
REMARK 465 GLU G 170
REMARK 465 PHE G 171
REMARK 465 PHE G 172
REMARK 465 ARG G 260
REMARK 465 ALA G 261
REMARK 465 MET H 1
REMARK 465 LEU H 2
REMARK 465 ALA H 3
REMARK 465 ARG H 4
REMARK 465 HIS H 5
REMARK 465 GLY H 6
REMARK 465 PRO H 7
REMARK 465 ARG H 8
REMARK 465 TYR H 9
REMARK 465 GLY H 10
REMARK 465 GLY H 11
REMARK 465 SER H 12
REMARK 465 VAL H 13
REMARK 465 ASN H 14
REMARK 465 GLY H 15
REMARK 465 HIS H 16
REMARK 465 SER H 17
REMARK 465 ASP H 18
REMARK 465 ASP H 19
REMARK 465 SER H 20
REMARK 465 SER H 21
REMARK 465 GLY H 22
REMARK 465 ASP H 23
REMARK 465 ALA H 24
REMARK 465 LYS H 25
REMARK 465 GLN H 26
REMARK 465 ALA H 27
REMARK 465 GLN H 65
REMARK 465 HIS H 66
REMARK 465 ASP H 67
REMARK 465 ARG H 68
REMARK 465 SER H 69
REMARK 465 GLY H 70
REMARK 465 LEU H 71
REMARK 465 PRO H 72
REMARK 465 PRO H 73
REMARK 465 LEU H 74
REMARK 465 GLU H 75
REMARK 465 ARG H 157
REMARK 465 MET H 158
REMARK 465 THR H 159
REMARK 465 GLY H 160
REMARK 465 MET H 161
REMARK 465 ASN H 162
REMARK 465 PRO H 163
REMARK 465 ASP H 164
REMARK 465 PHE H 165
REMARK 465 PHE H 166
REMARK 465 THR H 167
REMARK 465 ASP H 168
REMARK 465 ASP H 169
REMARK 465 GLU H 170
REMARK 465 PHE H 171
REMARK 465 PHE H 172
REMARK 465 ARG H 260
REMARK 465 ALA H 261
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 LYS A 56 CG CD CE NZ
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 GLN A 142 CG CD OE1 NE2
REMARK 470 GLN A 144 CG CD OE1 NE2
REMARK 470 ASP A 145 CG OD1 OD2
REMARK 470 LEU A 146 CG CD1 CD2
REMARK 470 GLU A 150 CG CD OE1 OE2
REMARK 470 MET A 151 CG SD CE
REMARK 470 ASP A 153 CG OD1 OD2
REMARK 470 PHE A 155 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 180 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 252 CG OD1 OD2
REMARK 470 ASP A 259 CG OD1 OD2
REMARK 470 LYS B 42 CD CE NZ
REMARK 470 LEU B 74 CG CD1 CD2
REMARK 470 LYS B 141 CG CD CE NZ
REMARK 470 LEU B 143 CG CD1 CD2
REMARK 470 GLN B 144 CG CD OE1 NE2
REMARK 470 LEU B 146 CG CD1 CD2
REMARK 470 GLU B 150 CG CD OE1 OE2
REMARK 470 LEU B 154 CG CD1 CD2
REMARK 470 PHE B 155 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR B 156 OG1 CG2
REMARK 470 ARG B 157 CG CD NE CZ NH1 NH2
REMARK 470 MET B 158 CG SD CE
REMARK 470 PHE B 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 176 CG CD1 CD2
REMARK 470 ASP B 214 CG OD1 OD2
REMARK 470 LYS C 42 CG CD CE NZ
REMARK 470 ARG C 123 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 139 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 153 CG OD1 OD2
REMARK 470 PHE C 155 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR C 156 OG1 CG2
REMARK 470 ARG C 180 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 42 CD CE NZ
REMARK 470 LEU D 71 CG CD1 CD2
REMARK 470 ASP D 95 CG OD1 OD2
REMARK 470 ARG D 139 CG CD NE CZ NH1 NH2
REMARK 470 TYR D 140 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 141 CG CD CE NZ
REMARK 470 GLN D 144 CG CD OE1 NE2
REMARK 470 ARG D 149 CZ NH1 NH2
REMARK 470 MET D 151 CG SD CE
REMARK 470 PHE D 155 CD2 CE1 CE2 CZ
REMARK 470 MET D 158 CG SD CE
REMARK 470 ASP D 168 CG OD1 OD2
REMARK 470 ASP D 169 CG OD1 OD2
REMARK 470 GLU D 170 CG CD OE1 OE2
REMARK 470 PHE D 171 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE D 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL D 173 CG1 CG2
REMARK 470 ARG D 260 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 42 CD CE NZ
REMARK 470 ILE E 138 CG1 CG2 CD1
REMARK 470 ARG E 139 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 144 CG CD OE1 NE2
REMARK 470 ASP E 148 CG OD1 OD2
REMARK 470 ARG E 149 CG CD NE CZ NH1 NH2
REMARK 470 MET E 158 CG SD CE
REMARK 470 PHE E 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL E 173 CG1 CG2
REMARK 470 ASP E 259 CG OD1 OD2
REMARK 470 LYS F 42 CD CE NZ
REMARK 470 LEU F 74 CG CD1 CD2
REMARK 470 LEU F 146 CG CD1 CD2
REMARK 470 PHE F 155 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE F 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL F 173 CG1 CG2
REMARK 470 LEU F 179 CG CD1 CD2
REMARK 470 GLU F 193 CG CD OE1 OE2
REMARK 470 LYS G 42 CD CE NZ
REMARK 470 ASP G 54 CG OD1 OD2
REMARK 470 GLU G 75 CG CD OE1 OE2
REMARK 470 ARG G 123 CG CD NE CZ NH1 NH2
REMARK 470 LEU G 146 CG CD1 CD2
REMARK 470 GLU G 150 CG CD OE1 OE2
REMARK 470 MET G 151 CG SD CE
REMARK 470 PHE G 155 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL G 173 CG1 CG2
REMARK 470 ARG G 180 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 193 CG CD OE1 OE2
REMARK 470 LYS G 195 CG CD CE NZ
REMARK 470 ASN G 242 CG OD1 ND2
REMARK 470 ASP G 259 CG OD1 OD2
REMARK 470 LYS H 42 CG CD CE NZ
REMARK 470 PHE H 51 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU H 146 CG CD1 CD2
REMARK 470 ASP H 148 CG OD1 OD2
REMARK 470 GLU H 150 CG CD OE1 OE2
REMARK 470 PHE H 155 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR H 156 OG1 CG2
REMARK 470 VAL H 173 CG1 CG2
REMARK 470 LEU H 176 CG CD1 CD2
REMARK 470 ARG H 180 CG CD NE CZ NH1 NH2
REMARK 470 ASP H 259 CG OD1 OD2
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 OD2 ASP C 145 CB ASP C 148 1.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER H 104 CA - CB - OG ANGL. DEV. = 56.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 104 -118.69 56.21
REMARK 500 ALA A 131 52.44 36.44
REMARK 500 LYS A 141 47.66 -77.05
REMARK 500 ASP A 148 42.45 -92.13
REMARK 500 ARG A 149 4.50 -63.57
REMARK 500 PRO A 218 4.57 -65.00
REMARK 500 GLU A 225 -149.06 -100.95
REMARK 500 ASP A 235 -144.64 -91.35
REMARK 500 SER B 104 -119.91 57.15
REMARK 500 ALA B 131 50.80 37.11
REMARK 500 LYS B 141 49.36 -74.88
REMARK 500 ASP B 148 33.45 -98.01
REMARK 500 PRO B 218 4.71 -65.05
REMARK 500 GLU B 225 -148.30 -102.14
REMARK 500 ASP B 235 -144.58 -91.80
REMARK 500 SER C 104 -120.44 56.88
REMARK 500 ALA C 131 50.86 36.45
REMARK 500 ILE C 138 68.21 -27.81
REMARK 500 ARG C 149 37.14 -77.13
REMARK 500 PRO C 218 4.65 -64.73
REMARK 500 GLU C 225 -147.81 -102.27
REMARK 500 ASP C 235 -145.13 -92.10
REMARK 500 ALA D 27 -144.01 -97.30
REMARK 500 LEU D 71 142.87 -174.40
REMARK 500 PRO D 73 102.87 -44.48
REMARK 500 SER D 104 -120.18 57.83
REMARK 500 ALA D 131 51.38 37.02
REMARK 500 HIS D 137 43.92 -98.58
REMARK 500 TYR D 140 48.21 -82.15
REMARK 500 GLN D 142 47.05 -107.45
REMARK 500 ASP D 169 -132.09 54.17
REMARK 500 GLU D 170 178.76 85.57
REMARK 500 PHE D 171 -24.72 89.39
REMARK 500 PRO D 218 4.86 -65.51
REMARK 500 GLU D 225 -150.18 -112.60
REMARK 500 ASP D 235 -145.03 -92.22
REMARK 500 SER E 104 -120.38 56.89
REMARK 500 ALA E 131 50.91 37.52
REMARK 500 ILE E 138 -178.32 -64.65
REMARK 500 GLN E 142 48.66 -153.35
REMARK 500 PRO E 218 5.83 -64.99
REMARK 500 GLU E 225 -153.27 -102.44
REMARK 500 ASP E 235 -145.05 -91.94
REMARK 500 SER F 104 -120.06 57.08
REMARK 500 ALA F 131 51.17 36.49
REMARK 500 HIS F 137 58.08 -104.02
REMARK 500 TYR F 140 56.50 -91.04
REMARK 500 LEU F 143 -129.23 -91.74
REMARK 500 ARG F 149 27.61 -140.45
REMARK 500 ASP F 153 -78.14 -67.69
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 563 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 564 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 565 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A 566 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A 567 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH A 568 DISTANCE = 12.13 ANGSTROMS
REMARK 525 HOH A 569 DISTANCE = 12.75 ANGSTROMS
REMARK 525 HOH B 566 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH B 567 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B 568 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH B 569 DISTANCE = 7.54 ANGSTROMS
REMARK 525 HOH B 570 DISTANCE = 8.31 ANGSTROMS
REMARK 525 HOH B 571 DISTANCE = 9.04 ANGSTROMS
REMARK 525 HOH B 572 DISTANCE = 9.62 ANGSTROMS
REMARK 525 HOH C 457 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH C 458 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH C 459 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH C 460 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH C 461 DISTANCE = 7.61 ANGSTROMS
REMARK 525 HOH C 462 DISTANCE = 8.13 ANGSTROMS
REMARK 525 HOH C 463 DISTANCE = 9.03 ANGSTROMS
REMARK 525 HOH C 464 DISTANCE = 9.09 ANGSTROMS
REMARK 525 HOH C 465 DISTANCE = 9.40 ANGSTROMS
REMARK 525 HOH C 466 DISTANCE = 9.80 ANGSTROMS
REMARK 525 HOH C 467 DISTANCE = 10.29 ANGSTROMS
REMARK 525 HOH C 468 DISTANCE = 11.44 ANGSTROMS
REMARK 525 HOH C 469 DISTANCE = 12.37 ANGSTROMS
REMARK 525 HOH C 470 DISTANCE = 13.51 ANGSTROMS
REMARK 525 HOH C 471 DISTANCE = 14.85 ANGSTROMS
REMARK 525 HOH C 472 DISTANCE = 14.94 ANGSTROMS
REMARK 525 HOH D 477 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH D 478 DISTANCE = 9.04 ANGSTROMS
REMARK 525 HOH D 479 DISTANCE = 9.37 ANGSTROMS
REMARK 525 HOH D 480 DISTANCE = 9.54 ANGSTROMS
REMARK 525 HOH D 481 DISTANCE = 9.81 ANGSTROMS
REMARK 525 HOH D 482 DISTANCE = 13.72 ANGSTROMS
REMARK 525 HOH D 483 DISTANCE = 14.58 ANGSTROMS
REMARK 525 HOH E 445 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH E 446 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH E 447 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH E 448 DISTANCE = 7.73 ANGSTROMS
REMARK 525 HOH E 449 DISTANCE = 9.41 ANGSTROMS
REMARK 525 HOH F 444 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH F 445 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH F 446 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH F 447 DISTANCE = 7.89 ANGSTROMS
REMARK 525 HOH F 448 DISTANCE = 9.18 ANGSTROMS
REMARK 525 HOH F 449 DISTANCE = 11.35 ANGSTROMS
REMARK 525 HOH G 430 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH G 431 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH G 432 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH G 433 DISTANCE = 7.73 ANGSTROMS
REMARK 525 HOH G 434 DISTANCE = 7.87 ANGSTROMS
REMARK 525 HOH G 435 DISTANCE = 8.35 ANGSTROMS
REMARK 525 HOH G 436 DISTANCE = 8.52 ANGSTROMS
REMARK 525 HOH H 431 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH H 432 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH H 433 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH H 434 DISTANCE = 8.01 ANGSTROMS
REMARK 525 HOH H 435 DISTANCE = 10.78 ANGSTROMS
REMARK 525 HOH H 436 DISTANCE = 10.93 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 E9H A 401
REMARK 610 E9H B 401
REMARK 610 E9H C 301
REMARK 610 E9H D 301
REMARK 610 E9H E 301
REMARK 610 E9H F 301
REMARK 610 E9H G 301
REMARK 610 E9H H 301
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 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 50 OE1
REMARK 620 2 ARG D 49 O 153.1
REMARK 620 3 PHE D 51 O 75.4 92.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 409 O
REMARK 620 2 HOH B 553 O 57.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E9H A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD F 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E9H B 401 and SER B
REMARK 800 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E9H C 301 and SER C
REMARK 800 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E9H D 301 and SER D
REMARK 800 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E9H E 301 and SER E
REMARK 800 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E9H F 301 and SER F
REMARK 800 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E9H G 301 and SER G
REMARK 800 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E9H H 301 and SER H
REMARK 800 104
DBREF1 6FVJ A 1 261 UNP A0A045JET3_MYCTX
DBREF2 6FVJ A A0A045JET3 1 261
DBREF1 6FVJ B 1 261 UNP A0A045JET3_MYCTX
DBREF2 6FVJ B A0A045JET3 1 261
DBREF1 6FVJ C 1 261 UNP A0A045JET3_MYCTX
DBREF2 6FVJ C A0A045JET3 1 261
DBREF1 6FVJ D 1 261 UNP A0A045JET3_MYCTX
DBREF2 6FVJ D A0A045JET3 1 261
DBREF1 6FVJ E 1 261 UNP A0A045JET3_MYCTX
DBREF2 6FVJ E A0A045JET3 1 261
DBREF1 6FVJ F 1 261 UNP A0A045JET3_MYCTX
DBREF2 6FVJ F A0A045JET3 1 261
DBREF1 6FVJ G 1 261 UNP A0A045JET3_MYCTX
DBREF2 6FVJ G A0A045JET3 1 261
DBREF1 6FVJ H 1 261 UNP A0A045JET3_MYCTX
DBREF2 6FVJ H A0A045JET3 1 261
SEQRES 1 A 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 A 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 A 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 A 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 A 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 A 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 A 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 A 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 A 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 A 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 A 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 A 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 A 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 A 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 A 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 A 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 A 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 A 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 A 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 A 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 A 261 ALA
SEQRES 1 B 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 B 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 B 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 B 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 B 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 B 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 B 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 B 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 B 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 B 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 B 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 B 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 B 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 B 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 B 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 B 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 B 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 B 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 B 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 B 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 B 261 ALA
SEQRES 1 C 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 C 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 C 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 C 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 C 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 C 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 C 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 C 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 C 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 C 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 C 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 C 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 C 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 C 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 C 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 C 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 C 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 C 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 C 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 C 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 C 261 ALA
SEQRES 1 D 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 D 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 D 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 D 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 D 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 D 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 D 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 D 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 D 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 D 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 D 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 D 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 D 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 D 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 D 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 D 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 D 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 D 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 D 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 D 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 D 261 ALA
SEQRES 1 E 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 E 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 E 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 E 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 E 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 E 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 E 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 E 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 E 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 E 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 E 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 E 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 E 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 E 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 E 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 E 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 E 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 E 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 E 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 E 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 E 261 ALA
SEQRES 1 F 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 F 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 F 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 F 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 F 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 F 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 F 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 F 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 F 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 F 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 F 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 F 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 F 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 F 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 F 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 F 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 F 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 F 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 F 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 F 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 F 261 ALA
SEQRES 1 G 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 G 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 G 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 G 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 G 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 G 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 G 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 G 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 G 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 G 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 G 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 G 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 G 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 G 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 G 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 G 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 G 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 G 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 G 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 G 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 G 261 ALA
SEQRES 1 H 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 H 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 H 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 H 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 H 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 H 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 H 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 H 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 H 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 H 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 H 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 H 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 H 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 H 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 H 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 H 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 H 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 H 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 H 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 H 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 H 261 ALA
HET E9H A 401 7
HET MPD A 402 8
HET MPD A 403 8
HET CA A 404 1
HET E9H B 401 5
HET MPD B 402 8
HET MPD B 403 8
HET E9H C 301 8
HET CA C 302 1
HET MPD C 303 8
HET MPD C 304 8
HET E9H D 301 8
HET MPD D 302 8
HET MPD D 303 8
HET E9H E 301 6
HET MPD E 302 8
HET E9H F 301 5
HET MPD F 302 8
HET MPD F 303 8
HET E9H G 301 5
HET MPD G 302 8
HET E9H H 301 6
HETNAM E9H HEXADECYL DIHYDROGEN PHOSPHATE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM CA CALCIUM ION
FORMUL 9 E9H 8(C16 H35 O4 P)
FORMUL 10 MPD 12(C6 H14 O2)
FORMUL 12 CA 2(CA 2+)
FORMUL 31 HOH *466(H2 O)
HELIX 1 AA1 THR A 40 ASP A 43 5 4
HELIX 2 AA2 TYR A 44 GLU A 50 1 7
HELIX 3 AA3 SER A 76 LYS A 89 1 14
HELIX 4 AA4 PRO A 90 ALA A 92 5 3
HELIX 5 AA5 SER A 104 ALA A 120 1 17
HELIX 6 AA6 ARG A 149 LEU A 154 1 6
HELIX 7 AA7 ALA A 175 GLY A 187 1 13
HELIX 8 AA8 THR A 212 ASP A 217 1 6
HELIX 9 AA9 PRO A 218 THR A 223 5 6
HELIX 10 AB1 PHE A 237 ASP A 241 5 5
HELIX 11 AB2 ASN A 242 HIS A 258 1 17
HELIX 12 AB3 THR B 40 ASP B 43 5 4
HELIX 13 AB4 TYR B 44 GLU B 50 1 7
HELIX 14 AB5 SER B 76 LYS B 89 1 14
HELIX 15 AB6 PRO B 90 ALA B 92 5 3
HELIX 16 AB7 SER B 104 ALA B 120 1 17
HELIX 17 AB8 ARG B 149 ARG B 157 1 9
HELIX 18 AB9 PHE B 172 GLY B 174 5 3
HELIX 19 AC1 ALA B 175 GLY B 187 1 13
HELIX 20 AC2 THR B 212 ASP B 217 1 6
HELIX 21 AC3 PRO B 218 THR B 223 5 6
HELIX 22 AC4 PHE B 237 ASP B 241 5 5
HELIX 23 AC5 ASN B 242 HIS B 258 1 17
HELIX 24 AC6 THR C 40 ASP C 43 5 4
HELIX 25 AC7 TYR C 44 GLU C 50 1 7
HELIX 26 AC8 SER C 76 MET C 87 1 12
HELIX 27 AC9 SER C 104 ALA C 120 1 17
HELIX 28 AD1 ARG C 149 THR C 156 1 8
HELIX 29 AD2 ALA C 175 GLY C 187 1 13
HELIX 30 AD3 THR C 212 ASP C 217 1 6
HELIX 31 AD4 PRO C 218 THR C 223 5 6
HELIX 32 AD5 PHE C 237 ASP C 241 5 5
HELIX 33 AD6 ASN C 242 HIS C 258 1 17
HELIX 34 AD7 THR D 40 ASP D 43 5 4
HELIX 35 AD8 TYR D 44 GLU D 50 1 7
HELIX 36 AD9 SER D 76 LYS D 89 1 14
HELIX 37 AE1 PRO D 90 ALA D 92 5 3
HELIX 38 AE2 SER D 104 ALA D 120 1 17
HELIX 39 AE3 LEU D 146 MET D 158 1 13
HELIX 40 AE4 ALA D 175 GLY D 187 1 13
HELIX 41 AE5 THR D 212 ASP D 217 1 6
HELIX 42 AE6 PRO D 218 THR D 223 5 6
HELIX 43 AE7 PHE D 237 ASP D 241 5 5
HELIX 44 AE8 ASN D 242 ARG D 260 1 19
HELIX 45 AE9 THR E 40 ASP E 43 5 4
HELIX 46 AF1 TYR E 44 GLU E 50 1 7
HELIX 47 AF2 SER E 76 LYS E 89 1 14
HELIX 48 AF3 PRO E 90 ALA E 92 5 3
HELIX 49 AF4 SER E 104 ALA E 120 1 17
HELIX 50 AF5 LEU E 146 MET E 158 1 13
HELIX 51 AF6 ALA E 175 GLY E 187 1 13
HELIX 52 AF7 THR E 212 ASP E 217 1 6
HELIX 53 AF8 PRO E 218 THR E 223 5 6
HELIX 54 AF9 PHE E 237 ASP E 241 5 5
HELIX 55 AG1 ASN E 242 ASP E 259 1 18
HELIX 56 AG2 THR F 40 ASP F 43 5 4
HELIX 57 AG3 TYR F 44 GLU F 50 1 7
HELIX 58 AG4 SER F 76 LYS F 89 1 14
HELIX 59 AG5 PRO F 90 ALA F 92 5 3
HELIX 60 AG6 SER F 104 ALA F 120 1 17
HELIX 61 AG7 ARG F 149 THR F 156 1 8
HELIX 62 AG8 ALA F 175 GLY F 187 1 13
HELIX 63 AG9 THR F 212 ASP F 217 1 6
HELIX 64 AH1 PRO F 218 THR F 223 5 6
HELIX 65 AH2 PHE F 237 ASP F 241 5 5
HELIX 66 AH3 ASN F 242 HIS F 258 1 17
HELIX 67 AH4 THR G 40 ASP G 43 5 4
HELIX 68 AH5 TYR G 44 GLU G 50 1 7
HELIX 69 AH6 SER G 76 LYS G 89 1 14
HELIX 70 AH7 PRO G 90 ALA G 92 5 3
HELIX 71 AH8 SER G 104 ALA G 120 1 17
HELIX 72 AH9 ARG G 149 LEU G 154 1 6
HELIX 73 AI1 ALA G 175 GLY G 187 1 13
HELIX 74 AI2 THR G 212 ASP G 217 1 6
HELIX 75 AI3 PRO G 218 THR G 223 5 6
HELIX 76 AI4 PHE G 237 ASP G 241 5 5
HELIX 77 AI5 ASN G 242 LEU G 255 1 14
HELIX 78 AI6 ALA H 41 ASP H 43 5 3
HELIX 79 AI7 TYR H 44 GLU H 50 1 7
HELIX 80 AI8 ILE H 77 MET H 87 1 11
HELIX 81 AI9 MET H 88 ALA H 92 5 5
HELIX 82 AJ1 SER H 104 ALA H 120 1 17
HELIX 83 AJ2 ARG H 149 THR H 156 1 8
HELIX 84 AJ3 ALA H 175 GLY H 187 1 13
HELIX 85 AJ4 THR H 212 ASP H 217 1 6
HELIX 86 AJ5 PRO H 218 THR H 223 5 6
HELIX 87 AJ6 PHE H 237 ASP H 241 5 5
HELIX 88 AJ7 ASN H 242 ASP H 259 1 18
SHEET 1 AA1 6 LYS A 56 ALA A 59 0
SHEET 2 AA1 6 THR A 30 PHE A 34 1 N LEU A 31 O LYS A 56
SHEET 3 AA1 6 PRO A 97 HIS A 103 1 O PHE A 101 N PHE A 34
SHEET 4 AA1 6 ARG A 123 SER A 130 1 O PHE A 128 N PHE A 100
SHEET 5 AA1 6 ILE A 200 GLY A 205 1 O TYR A 201 N PHE A 127
SHEET 6 AA1 6 PHE A 227 PHE A 232 1 O SER A 228 N ALA A 202
SHEET 1 AA2 6 LYS B 56 ALA B 59 0
SHEET 2 AA2 6 THR B 30 PHE B 34 1 N LEU B 31 O LYS B 56
SHEET 3 AA2 6 PRO B 97 HIS B 103 1 O PHE B 101 N PHE B 34
SHEET 4 AA2 6 ARG B 123 SER B 130 1 O PHE B 128 N PHE B 100
SHEET 5 AA2 6 ILE B 200 GLY B 205 1 O TYR B 201 N PHE B 127
SHEET 6 AA2 6 PHE B 227 PHE B 232 1 O SER B 228 N ALA B 202
SHEET 1 AA3 6 LYS C 56 ALA C 59 0
SHEET 2 AA3 6 THR C 30 PHE C 34 1 N LEU C 31 O LYS C 56
SHEET 3 AA3 6 PRO C 97 HIS C 103 1 O PHE C 101 N PHE C 34
SHEET 4 AA3 6 ARG C 123 SER C 130 1 O PHE C 128 N PHE C 100
SHEET 5 AA3 6 ILE C 200 GLY C 205 1 O TYR C 201 N PHE C 127
SHEET 6 AA3 6 PHE C 227 PHE C 232 1 O SER C 228 N ALA C 202
SHEET 1 AA4 6 LYS D 56 ALA D 59 0
SHEET 2 AA4 6 THR D 30 PHE D 34 1 N LEU D 31 O LYS D 56
SHEET 3 AA4 6 PRO D 97 HIS D 103 1 O PHE D 101 N PHE D 34
SHEET 4 AA4 6 ARG D 123 SER D 130 1 O PHE D 128 N PHE D 100
SHEET 5 AA4 6 ILE D 200 GLY D 205 1 O TYR D 201 N PHE D 127
SHEET 6 AA4 6 PHE D 227 PHE D 232 1 O SER D 228 N ALA D 202
SHEET 1 AA5 6 LYS E 56 ALA E 59 0
SHEET 2 AA5 6 THR E 30 PHE E 34 1 N LEU E 31 O LYS E 56
SHEET 3 AA5 6 PRO E 97 HIS E 103 1 O PHE E 101 N PHE E 34
SHEET 4 AA5 6 ARG E 123 SER E 130 1 O PHE E 128 N PHE E 100
SHEET 5 AA5 6 ILE E 200 GLY E 205 1 O TYR E 201 N PHE E 127
SHEET 6 AA5 6 PHE E 227 PHE E 232 1 O SER E 228 N ALA E 202
SHEET 1 AA6 6 LYS F 56 ALA F 59 0
SHEET 2 AA6 6 THR F 30 PHE F 34 1 N LEU F 31 O LYS F 56
SHEET 3 AA6 6 PRO F 97 HIS F 103 1 O PHE F 101 N PHE F 34
SHEET 4 AA6 6 ARG F 123 SER F 130 1 O PHE F 128 N PHE F 100
SHEET 5 AA6 6 ILE F 200 GLY F 205 1 O TYR F 201 N PHE F 127
SHEET 6 AA6 6 PHE F 227 PHE F 232 1 O SER F 228 N ALA F 202
SHEET 1 AA7 6 LYS G 56 ALA G 59 0
SHEET 2 AA7 6 THR G 30 PHE G 34 1 N LEU G 31 O LYS G 56
SHEET 3 AA7 6 PRO G 97 HIS G 103 1 O PHE G 101 N PHE G 34
SHEET 4 AA7 6 ARG G 123 SER G 130 1 O PHE G 128 N PHE G 100
SHEET 5 AA7 6 ILE G 200 GLY G 205 1 O TYR G 201 N PHE G 127
SHEET 6 AA7 6 PHE G 227 PHE G 232 1 O SER G 228 N ALA G 202
SHEET 1 AA8 6 LYS H 56 ALA H 59 0
SHEET 2 AA8 6 THR H 30 PHE H 34 1 N LEU H 31 O LYS H 56
SHEET 3 AA8 6 PRO H 97 HIS H 103 1 O PHE H 101 N TYR H 32
SHEET 4 AA8 6 ARG H 123 SER H 130 1 O PHE H 128 N PHE H 100
SHEET 5 AA8 6 ILE H 200 GLY H 205 1 O TYR H 201 N PHE H 127
SHEET 6 AA8 6 PHE H 227 PHE H 232 1 O SER H 228 N ALA H 202
LINK OE1 GLU A 50 CA CA A 404 1555 1555 2.70
LINK OG SER A 104 P1 E9H A 401 1555 1555 1.61
LINK OG SER B 104 P1 E9H B 401 1555 1555 1.60
LINK OG SER C 104 P1 E9H C 301 1555 1555 1.61
LINK O ARG D 49 CA CA A 404 1555 1555 2.34
LINK O PHE D 51 CA CA A 404 1555 1555 2.41
LINK OG SER D 104 P1 E9H D 301 1555 1555 1.60
LINK OG SER E 104 P1 E9H E 301 1555 1555 1.61
LINK OG SER F 104 P1 E9H F 301 1555 1555 1.61
LINK OG SER G 104 P1 E9H G 301 1555 1555 1.61
LINK OG SER H 104 P1 E9H H 301 1555 1555 1.61
LINK CA CA C 302 O HOH C 409 1555 1555 2.65
LINK CA CA C 302 O HOH B 553 1555 1455 2.98
SITE 1 AC1 7 HIS A 36 ALA A 37 SER A 104 MET A 105
SITE 2 AC1 7 HIS A 236 MPD A 402 HOH A 511
SITE 1 AC2 7 ALA A 131 CYS A 132 SER A 133 ILE A 185
SITE 2 AC2 7 ILE A 210 E9H A 401 ARG F 139
SITE 1 AC3 4 ASP A 43 PHE A 237 ASN A 240 ARG D 49
SITE 1 AC4 4 GLU A 50 LEU A 243 ARG D 49 PHE D 51
SITE 1 AC5 4 SER B 104 SER B 133 ILE B 210 E9H B 401
SITE 1 AC6 5 HIS B 36 ASP B 43 PHE B 237 ASN B 240
SITE 2 AC6 5 HOH B 507
SITE 1 AC7 3 HOH B 553 ARG C 49 HOH C 409
SITE 1 AC8 4 MET C 108 CYS C 132 SER C 133 E9H C 301
SITE 1 AC9 4 HIS C 36 ASP C 43 ASN C 240 HOH C 412
SITE 1 AD1 6 MET D 108 ALA D 131 SER D 133 ILE D 138
SITE 2 AD1 6 ILE D 210 E9H D 301
SITE 1 AD2 4 ASP D 43 TYR D 44 PHE D 237 ASN D 240
SITE 1 AD3 7 SER E 104 MET E 105 ALA E 131 SER E 133
SITE 2 AD3 7 ARG E 139 ILE E 210 E9H E 301
SITE 1 AD4 7 SER F 104 MET F 108 CYS F 132 SER F 133
SITE 2 AD4 7 ILE F 138 ILE F 185 ILE F 210
SITE 1 AD5 5 HIS F 36 ASP F 43 TYR F 44 PHE F 237
SITE 2 AD5 5 ASN F 240
SITE 1 AD6 4 SER G 104 ALA G 131 SER G 133 ILE G 210
SITE 1 AD7 11 HIS B 36 ALA B 37 HIS B 103 MET B 105
SITE 2 AD7 11 GLY B 106 GLY B 107 SER B 130 ALA B 131
SITE 3 AD7 11 CYS B 132 HIS B 236 MPD B 402
SITE 1 AD8 11 HIS C 36 ALA C 37 HIS C 103 MET C 105
SITE 2 AD8 11 GLY C 106 GLY C 107 SER C 130 ALA C 131
SITE 3 AD8 11 CYS C 132 HIS C 236 MPD C 303
SITE 1 AD9 11 HIS D 36 ALA D 37 HIS D 103 MET D 105
SITE 2 AD9 11 GLY D 106 GLY D 107 SER D 130 ALA D 131
SITE 3 AD9 11 CYS D 132 HIS D 236 MPD D 302
SITE 1 AE1 12 HIS E 36 ALA E 37 HIS E 103 MET E 105
SITE 2 AE1 12 GLY E 106 GLY E 107 SER E 130 ALA E 131
SITE 3 AE1 12 CYS E 132 HIS E 236 MPD E 302 HOH E 405
SITE 1 AE2 12 HIS F 36 ALA F 37 HIS F 103 MET F 105
SITE 2 AE2 12 GLY F 106 GLY F 107 SER F 130 ALA F 131
SITE 3 AE2 12 CYS F 132 HIS F 236 MPD F 302 HOH F 410
SITE 1 AE3 11 HIS G 36 ALA G 37 HIS G 103 MET G 105
SITE 2 AE3 11 GLY G 106 GLY G 107 SER G 130 ALA G 131
SITE 3 AE3 11 CYS G 132 HIS G 236 MPD G 302
SITE 1 AE4 11 ARG D 157 HIS H 36 ALA H 37 HIS H 103
SITE 2 AE4 11 MET H 105 GLY H 106 GLY H 107 SER H 130
SITE 3 AE4 11 ALA H 131 CYS H 132 HIS H 236
CRYST1 79.070 224.580 222.210 90.00 90.00 90.00 C 2 2 21 64
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 0.012647 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004453 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004500 0.00000
TER 1599 ASP A 259
TER 3228 ARG B 260
TER 4819 HIS C 258
TER 6516 ARG D 260
TER 8168 ASP E 259
TER 9785 HIS F 258
TER 11363 ASP G 259
TER 12943 ASP H 259
MASTER 1229 0 22 88 48 0 43 613549 8 160 168
END |