HEADER LIGASE 16-FEB-16 5I6G
TITLE CRYSTAL STRUCTURE OF C-TERMINAL VARIANT 2 OF CHAETOMIUM THERMOPHILUM
TITLE 2 ACETYL-COA CARBOXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COA CARBOXYLASE-LIKE PROTEIN,ACETYL-COA CARBOXYLASE-
COMPND 3 LIKE PROTEIN;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: THE CRYSTALLIZED CONSTRUCT CONTAINS AMINO ACIDS 1114-
COMPND 7 2297 (ALIGNED TO ACCESSION CODE: G0S3L5). DUE TO FORMATTING
COMPND 8 RESTRICTIONS THE SEQRES CARD WAS TRUNCATED C-TERMINALLY TO RESIDUE
COMPND 9 R2261. C-TERMINAL STRETCHES AFTER L2259 IN CHAIN A AND R2261 IN CHAIN
COMPND 10 B COULD NOT BE MODELED UNAMBIGUOUSLY AND WERE INTERPRETED AS POLY-
COMPND 11 ALA/UNK RESIDUES.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHAETOMIUM THERMOPHILUM (STRAIN DSM 1495 / CBS
SOURCE 3 144.50 / IMI 039719), CHAETOMIUM THERMOPHILUM VAR. THERMOPHILUM DSM
SOURCE 4 1495;
SOURCE 5 ORGANISM_TAXID: 759272;
SOURCE 6 GENE: CTHT_0021690;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: SF21
KEYWDS CARBOXYLASE, FATTY ACID METABOLISM, MULTIENZYME, CARRIER PROTEIN-
KEYWDS 2 DEPENDENT ENZYME, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HUNKELER,E.STUTTFELD,A.HAGMANN,S.IMSENG,T.MAIER
REVDAT 3 10-JAN-24 5I6G 1 REMARK
REVDAT 2 27-APR-16 5I6G 1 JRNL
REVDAT 1 20-APR-16 5I6G 0
JRNL AUTH M.HUNKELER,E.STUTTFELD,A.HAGMANN,S.IMSENG,T.MAIER
JRNL TITL THE DYNAMIC ORGANIZATION OF FUNGAL ACETYL-COA CARBOXYLASE.
JRNL REF NAT COMMUN V. 7 11196 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27073141
JRNL DOI 10.1038/NCOMMS11196
REMARK 2
REMARK 2 RESOLUTION. 4.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
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) : 4.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 23340
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.760
REMARK 3 FREE R VALUE TEST SET COUNT : 1112
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 : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 4.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 4.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.61
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2802
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2639
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2686
REMARK 3 BIN R VALUE (WORKING SET) : 0.2644
REMARK 3 BIN FREE R VALUE : 0.2515
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.14
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 116
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 : 16405
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 197.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 275.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -72.16960
REMARK 3 B22 (A**2) : 50.93090
REMARK 3 B33 (A**2) : 21.23860
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) : 0.976
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.885
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 16759 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 22697 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 7813 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 446 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2415 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 16759 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 2148 ; 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 : 18765 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.42
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.43
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|1186 - 1327}
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5088 -62.8207 -14.0368
REMARK 3 T TENSOR
REMARK 3 T11: 0.6227 T22: -0.6390
REMARK 3 T33: -0.6524 T12: -0.2394
REMARK 3 T13: -0.4559 T23: -0.3688
REMARK 3 L TENSOR
REMARK 3 L11: 17.2146 L22: 17.9640
REMARK 3 L33: 13.6440 L12: -0.8977
REMARK 3 L13: 6.7854 L23: -4.5424
REMARK 3 S TENSOR
REMARK 3 S11: 0.0536 S12: 1.2838 S13: -0.2986
REMARK 3 S21: -0.5059 S22: -0.3291 S23: 0.5332
REMARK 3 S31: 0.7536 S32: -0.4577 S33: 0.2755
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|1328 - 1523}
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7034 -39.6867 2.3726
REMARK 3 T TENSOR
REMARK 3 T11: -0.8194 T22: -0.9119
REMARK 3 T33: -0.9119 T12: -0.1526
REMARK 3 T13: 0.4559 T23: -0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 8.2663 L22: 9.3737
REMARK 3 L33: 13.1448 L12: -3.4791
REMARK 3 L13: -2.2703 L23: 0.4146
REMARK 3 S TENSOR
REMARK 3 S11: -0.1256 S12: -0.9046 S13: 0.5701
REMARK 3 S21: -0.8371 S22: 0.3070 S23: -0.9644
REMARK 3 S31: 0.9728 S32: 0.0499 S33: -0.1813
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|1524 - 2259}
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2240 -19.2833 45.3341
REMARK 3 T TENSOR
REMARK 3 T11: 0.3884 T22: -0.4435
REMARK 3 T33: -0.3206 T12: 0.1028
REMARK 3 T13: 0.2757 T23: -0.0891
REMARK 3 L TENSOR
REMARK 3 L11: 0.0791 L22: 3.4873
REMARK 3 L33: 3.6046 L12: 0.0709
REMARK 3 L13: -1.0665 L23: 0.5169
REMARK 3 S TENSOR
REMARK 3 S11: 0.1559 S12: -0.0820 S13: 0.2763
REMARK 3 S21: 1.6134 S22: 0.1680 S23: 0.1469
REMARK 3 S31: -0.4814 S32: 0.2609 S33: -0.3239
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {B|1186 - 1327}
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6485 -4.5518 132.0140
REMARK 3 T TENSOR
REMARK 3 T11: 0.8298 T22: 0.0524
REMARK 3 T33: -0.1846 T12: 0.3243
REMARK 3 T13: 0.3038 T23: -0.3940
REMARK 3 L TENSOR
REMARK 3 L11: 5.1798 L22: 23.1478
REMARK 3 L33: 17.1083 L12: 0.4694
REMARK 3 L13: -2.4155 L23: 8.7312
REMARK 3 S TENSOR
REMARK 3 S11: 0.0221 S12: -0.3192 S13: 0.1959
REMARK 3 S21: 0.0630 S22: -0.4165 S23: 0.3421
REMARK 3 S31: 0.4676 S32: -0.5135 S33: 0.3945
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {B|1328 - 1523}
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3161 -26.4635 112.9170
REMARK 3 T TENSOR
REMARK 3 T11: 0.9119 T22: 0.7586
REMARK 3 T33: 0.3053 T12: 0.4353
REMARK 3 T13: -0.2474 T23: -0.0873
REMARK 3 L TENSOR
REMARK 3 L11: 4.5935 L22: 4.9863
REMARK 3 L33: 5.0672 L12: -0.6930
REMARK 3 L13: -1.2356 L23: -2.1923
REMARK 3 S TENSOR
REMARK 3 S11: 0.2834 S12: 0.1040 S13: -1.1043
REMARK 3 S21: 0.6027 S22: 0.3045 S23: -0.9922
REMARK 3 S31: 0.6727 S32: 0.1735 S33: -0.5878
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {B|1524 - 2261}
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5222 -37.6649 60.5560
REMARK 3 T TENSOR
REMARK 3 T11: 0.9119 T22: -0.0439
REMARK 3 T33: 0.0397 T12: -0.0698
REMARK 3 T13: 0.4559 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 2.5060
REMARK 3 L33: 3.8920 L12: -0.5501
REMARK 3 L13: -0.7470 L23: 0.9928
REMARK 3 S TENSOR
REMARK 3 S11: -0.0914 S12: -0.6989 S13: -0.1027
REMARK 3 S21: 1.6327 S22: 0.0745 S23: 0.0511
REMARK 3 S31: 0.6663 S32: -0.1328 S33: 0.0169
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5I6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218268.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-15
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION MARCH 1, 2015
REMARK 200 DATA SCALING SOFTWARE : XSCALE VERSION MARCH 1, 2015
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23225
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.500
REMARK 200 RESOLUTION RANGE LOW (A) : 130.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.27400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 2.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 5I6F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, TACSIMATE, PEGMME5000, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 50.08500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 124.62000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.72500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 124.62000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.08500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.72500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 90890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A 1113
REMARK 465 ASN A 1114
REMARK 465 LEU A 1115
REMARK 465 ARG A 1116
REMARK 465 GLU A 1117
REMARK 465 VAL A 1118
REMARK 465 ARG A 1119
REMARK 465 TYR A 1120
REMARK 465 HIS A 1121
REMARK 465 ASP A 1122
REMARK 465 GLU A 1123
REMARK 465 GLU A 1124
REMARK 465 ARG A 1125
REMARK 465 PRO A 1126
REMARK 465 TYR A 1127
REMARK 465 PHE A 1128
REMARK 465 ILE A 1129
REMARK 465 ASP A 1130
REMARK 465 TRP A 1131
REMARK 465 ASP A 1132
REMARK 465 PHE A 1133
REMARK 465 ALA A 1134
REMARK 465 LEU A 1135
REMARK 465 ARG A 1136
REMARK 465 LYS A 1137
REMARK 465 SER A 1138
REMARK 465 GLY A 1139
REMARK 465 ALA A 1140
REMARK 465 ASN A 1141
REMARK 465 GLN A 1142
REMARK 465 THR A 1143
REMARK 465 GLU A 1144
REMARK 465 SER A 1145
REMARK 465 SER A 1146
REMARK 465 MET A 1147
REMARK 465 HIS A 1148
REMARK 465 MET A 1149
REMARK 465 GLN A 1150
REMARK 465 SER A 1151
REMARK 465 VAL A 1152
REMARK 465 VAL A 1153
REMARK 465 PRO A 1154
REMARK 465 SER A 1155
REMARK 465 SER A 1156
REMARK 465 PRO A 1157
REMARK 465 ALA A 1158
REMARK 465 THR A 1159
REMARK 465 PRO A 1160
REMARK 465 VAL A 1161
REMARK 465 GLU A 1162
REMARK 465 ASN A 1163
REMARK 465 ASP A 1164
REMARK 465 PHE A 1165
REMARK 465 LYS A 1166
REMARK 465 ARG A 1167
REMARK 465 ILE A 1168
REMARK 465 HIS A 1169
REMARK 465 SER A 1170
REMARK 465 ILE A 1171
REMARK 465 SER A 1172
REMARK 465 ASP A 1173
REMARK 465 MET A 1174
REMARK 465 THR A 1175
REMARK 465 TYR A 1176
REMARK 465 LEU A 1177
REMARK 465 ALA A 1178
REMARK 465 ARG A 1179
REMARK 465 ARG A 1180
REMARK 465 THR A 1181
REMARK 465 ARG A 1182
REMARK 465 ASP A 1183
REMARK 465 GLU A 1184
REMARK 465 PRO A 1185
REMARK 465 LEU A 1213
REMARK 465 ALA A 1214
REMARK 465 HIS A 1215
REMARK 465 LYS A 1216
REMARK 465 GLU A 1217
REMARK 465 THR A 1218
REMARK 465 LYS A 1219
REMARK 465 ASP A 1220
REMARK 465 LYS A 1221
REMARK 465 ASP A 1222
REMARK 465 ARG A 1223
REMARK 465 LYS A 1224
REMARK 465 GLN A 1225
REMARK 465 GLN A 1226
REMARK 465 PRO A 1227
REMARK 465 GLY A 1228
REMARK 465 ILE A 1229
REMARK 465 ALA A 1230
REMARK 465 ALA A 1231
REMARK 465 ASP A 1232
REMARK 465 LEU A 1233
REMARK 465 ALA A 1234
REMARK 465 GLN A 1235
REMARK 465 ARG A 1236
REMARK 465 ARG A 1237
REMARK 465 ARG A 1238
REMARK 465 PRO A 1239
REMARK 465 GLY A 1240
REMARK 465 THR A 1241
REMARK 465 PRO A 1242
REMARK 465 LEU A 1243
REMARK 465 ARG A 1244
REMARK 465 LEU A 1245
REMARK 465 GLU A 1246
REMARK 465 GLY A 1247
REMARK 465 ILE A 1248
REMARK 465 GLY A 1249
REMARK 465 GLU A 1250
REMARK 465 LEU A 1251
REMARK 465 SER A 1252
REMARK 465 ARG A 1380
REMARK 465 ASP A 1381
REMARK 465 GLU A 1382
REMARK 465 ILE A 1383
REMARK 465 SER A 1384
REMARK 465 THR A 1385
REMARK 465 ASP A 1465
REMARK 465 ASN A 1466
REMARK 465 ASN A 1467
REMARK 465 ASP A 1468
REMARK 465 GLY A 2188
REMARK 465 LYS A 2189
REMARK 465 ARG A 2190
REMARK 465 ARG A 2191
REMARK 465 HIS A 2192
REMARK 465 ASP A 2193
REMARK 465 PRO A 2194
REMARK 465 GLU A 2195
REMARK 465 LEU A 2260
REMARK 465 ARG A 2261
REMARK 465 GLY B 1113
REMARK 465 ASN B 1114
REMARK 465 LEU B 1115
REMARK 465 ARG B 1116
REMARK 465 GLU B 1117
REMARK 465 VAL B 1118
REMARK 465 ARG B 1119
REMARK 465 TYR B 1120
REMARK 465 HIS B 1121
REMARK 465 ASP B 1122
REMARK 465 GLU B 1123
REMARK 465 GLU B 1124
REMARK 465 ARG B 1125
REMARK 465 PRO B 1126
REMARK 465 TYR B 1127
REMARK 465 PHE B 1128
REMARK 465 ILE B 1129
REMARK 465 ASP B 1130
REMARK 465 TRP B 1131
REMARK 465 ASP B 1132
REMARK 465 PHE B 1133
REMARK 465 ALA B 1134
REMARK 465 LEU B 1135
REMARK 465 ARG B 1136
REMARK 465 LYS B 1137
REMARK 465 SER B 1138
REMARK 465 GLY B 1139
REMARK 465 ALA B 1140
REMARK 465 ASN B 1141
REMARK 465 GLN B 1142
REMARK 465 THR B 1143
REMARK 465 GLU B 1144
REMARK 465 SER B 1145
REMARK 465 SER B 1146
REMARK 465 MET B 1147
REMARK 465 HIS B 1148
REMARK 465 MET B 1149
REMARK 465 GLN B 1150
REMARK 465 SER B 1151
REMARK 465 VAL B 1152
REMARK 465 VAL B 1153
REMARK 465 PRO B 1154
REMARK 465 SER B 1155
REMARK 465 SER B 1156
REMARK 465 PRO B 1157
REMARK 465 ALA B 1158
REMARK 465 THR B 1159
REMARK 465 PRO B 1160
REMARK 465 VAL B 1161
REMARK 465 GLU B 1162
REMARK 465 ASN B 1163
REMARK 465 ASP B 1164
REMARK 465 PHE B 1165
REMARK 465 LYS B 1166
REMARK 465 ARG B 1167
REMARK 465 ILE B 1168
REMARK 465 HIS B 1169
REMARK 465 SER B 1170
REMARK 465 ILE B 1171
REMARK 465 SER B 1172
REMARK 465 ASP B 1173
REMARK 465 MET B 1174
REMARK 465 THR B 1175
REMARK 465 TYR B 1176
REMARK 465 LEU B 1177
REMARK 465 ALA B 1178
REMARK 465 ARG B 1179
REMARK 465 ARG B 1180
REMARK 465 THR B 1181
REMARK 465 ARG B 1182
REMARK 465 ASP B 1183
REMARK 465 GLU B 1184
REMARK 465 PRO B 1185
REMARK 465 LEU B 1213
REMARK 465 ALA B 1214
REMARK 465 HIS B 1215
REMARK 465 LYS B 1216
REMARK 465 GLU B 1217
REMARK 465 THR B 1218
REMARK 465 LYS B 1219
REMARK 465 ASP B 1220
REMARK 465 LYS B 1221
REMARK 465 ASP B 1222
REMARK 465 ARG B 1223
REMARK 465 LYS B 1224
REMARK 465 GLN B 1225
REMARK 465 GLN B 1226
REMARK 465 PRO B 1227
REMARK 465 GLY B 1228
REMARK 465 ILE B 1229
REMARK 465 ALA B 1230
REMARK 465 ALA B 1231
REMARK 465 ASP B 1232
REMARK 465 LEU B 1233
REMARK 465 ALA B 1234
REMARK 465 GLN B 1235
REMARK 465 ARG B 1236
REMARK 465 ARG B 1237
REMARK 465 ARG B 1238
REMARK 465 PRO B 1239
REMARK 465 GLY B 1240
REMARK 465 THR B 1241
REMARK 465 PRO B 1242
REMARK 465 LEU B 1243
REMARK 465 ARG B 1244
REMARK 465 LEU B 1245
REMARK 465 GLU B 1246
REMARK 465 GLY B 1247
REMARK 465 ILE B 1248
REMARK 465 GLY B 1249
REMARK 465 GLU B 1250
REMARK 465 LEU B 1251
REMARK 465 SER B 1252
REMARK 465 ARG B 1380
REMARK 465 ASP B 1381
REMARK 465 GLU B 1382
REMARK 465 ILE B 1383
REMARK 465 SER B 1384
REMARK 465 THR B 1385
REMARK 465 ASP B 1465
REMARK 465 ASN B 1466
REMARK 465 ASN B 1467
REMARK 465 ASP B 1468
REMARK 465 GLY B 2188
REMARK 465 LYS B 2189
REMARK 465 ARG B 2190
REMARK 465 ARG B 2191
REMARK 465 HIS B 2192
REMARK 465 ASP B 2193
REMARK 465 PRO B 2194
REMARK 465 GLU B 2195
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 OG1 THR B 1917 OG SER B 1969 2.14
REMARK 500 CA SER B 1515 O SER B 1599 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 VAL A1210 44.04 -100.71
REMARK 500 ALA A1262 47.84 -83.38
REMARK 500 GLU A1268 -47.76 70.49
REMARK 500 SER A1281 46.34 -100.26
REMARK 500 TYR A1315 67.30 60.12
REMARK 500 GLU A1317 103.95 69.51
REMARK 500 HIS A1323 28.07 48.32
REMARK 500 GLU A1333 -101.52 80.86
REMARK 500 LEU A1334 -29.90 67.48
REMARK 500 LYS A1339 34.21 -81.99
REMARK 500 GLU A1387 32.04 -81.19
REMARK 500 ASN A1410 -121.79 49.52
REMARK 500 THR A1424 46.12 -97.14
REMARK 500 SER A1483 37.87 89.81
REMARK 500 VAL A1486 -72.67 -40.98
REMARK 500 ILE A1487 24.87 39.11
REMARK 500 TYR A1492 -165.42 -100.33
REMARK 500 GLU A1498 -27.41 84.31
REMARK 500 ALA A1511 35.50 71.00
REMARK 500 LYS A1512 -7.22 56.13
REMARK 500 MET A1516 102.45 62.69
REMARK 500 PRO A1524 46.74 -95.65
REMARK 500 TYR A1525 73.40 28.49
REMARK 500 SER A1570 -67.22 58.67
REMARK 500 LEU A1571 83.84 -69.35
REMARK 500 ALA A1572 -2.96 -163.16
REMARK 500 ALA A1577 -165.90 80.15
REMARK 500 GLN A1592 42.71 -106.40
REMARK 500 LEU A1595 135.14 -38.98
REMARK 500 ILE A1638 23.34 38.82
REMARK 500 ALA A1668 81.71 -163.46
REMARK 500 SER A1670 43.27 -140.43
REMARK 500 PHE A1711 -78.74 -115.02
REMARK 500 GLU A1712 -48.58 65.58
REMARK 500 ASP A1761 -68.18 -106.87
REMARK 500 ARG A1771 120.55 -38.81
REMARK 500 GLN A1784 -67.45 53.48
REMARK 500 GLU A1790 -49.35 -25.21
REMARK 500 LEU A1817 -10.80 -142.70
REMARK 500 GLN A1853 -160.57 -117.09
REMARK 500 ARG A1854 -77.32 -82.80
REMARK 500 SER A1864 -92.38 44.33
REMARK 500 ASP A1869 47.80 -84.34
REMARK 500 LYS A1879 -78.68 -68.50
REMARK 500 HIS A2033 -21.36 77.36
REMARK 500 ALA A2086 26.29 -75.05
REMARK 500 ARG A2087 -53.12 -132.98
REMARK 500 GLU A2102 -147.76 60.21
REMARK 500 SER A2105 -178.00 -62.52
REMARK 500 GLN A2117 32.62 -76.53
REMARK 500
REMARK 500 THIS ENTRY HAS 113 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I6E RELATED DB: PDB
REMARK 900 RELATED ID: 5I6F RELATED DB: PDB
REMARK 900 RELATED ID: 5I6H RELATED DB: PDB
REMARK 900 RELATED ID: 5I6I RELATED DB: PDB
REMARK 900 RELATED ID: 5I87 RELATED DB: PDB
DBREF 5I6G A 1114 2261 UNP G0S3L5 G0S3L5_CHATD 1114 2261
DBREF 5I6G A 2300 2311 PDB 5I6G 5I6G 2300 2311
DBREF 5I6G B 1114 2261 UNP G0S3L5 G0S3L5_CHATD 1114 2261
DBREF 5I6G B 2300 2311 PDB 5I6G 5I6G 2300 2311
SEQADV 5I6G GLY A 1113 UNP G0S3L5 EXPRESSION TAG
SEQADV 5I6G GLY B 1113 UNP G0S3L5 EXPRESSION TAG
SEQRES 1 A 1161 GLY ASN LEU ARG GLU VAL ARG TYR HIS ASP GLU GLU ARG
SEQRES 2 A 1161 PRO TYR PHE ILE ASP TRP ASP PHE ALA LEU ARG LYS SER
SEQRES 3 A 1161 GLY ALA ASN GLN THR GLU SER SER MET HIS MET GLN SER
SEQRES 4 A 1161 VAL VAL PRO SER SER PRO ALA THR PRO VAL GLU ASN ASP
SEQRES 5 A 1161 PHE LYS ARG ILE HIS SER ILE SER ASP MET THR TYR LEU
SEQRES 6 A 1161 ALA ARG ARG THR ARG ASP GLU PRO ILE ARG LYS GLY VAL
SEQRES 7 A 1161 ILE VAL PRO CYS LYS ASP LEU LEU ASP ALA GLU GLU ALA
SEQRES 8 A 1161 LEU SER ARG ALA LEU GLU VAL LEU PRO LEU ALA HIS LYS
SEQRES 9 A 1161 GLU THR LYS ASP LYS ASP ARG LYS GLN GLN PRO GLY ILE
SEQRES 10 A 1161 ALA ALA ASP LEU ALA GLN ARG ARG ARG PRO GLY THR PRO
SEQRES 11 A 1161 LEU ARG LEU GLU GLY ILE GLY GLU LEU SER ALA VAL VAL
SEQRES 12 A 1161 ASN VAL ALA VAL ARG ASP ALA GLU GLY LYS ASN ASP GLU
SEQRES 13 A 1161 GLU ILE LEU ALA LEU ILE LYS PRO TRP VAL GLN ASN SER
SEQRES 14 A 1161 LYS ALA ASP LEU LEU ALA ARG ARG VAL ARG ARG LEU THR
SEQRES 15 A 1161 PHE ILE CYS GLY ARG ASN ASP GLY SER TYR PRO SER TYR
SEQRES 16 A 1161 TYR THR PHE ARG GLY PRO ASP TYR ALA GLU ASP ASP SER
SEQRES 17 A 1161 ILE ARG HIS ILE GLU PRO SER LEU ALA PHE GLN LEU GLU
SEQRES 18 A 1161 LEU GLY ARG LEU SER LYS PHE LYS LEU THR PRO VAL PHE
SEQRES 19 A 1161 THR GLN ASN LYS ASN ILE HIS VAL TYR GLU ALA VAL GLY
SEQRES 20 A 1161 ARG GLY VAL GLU THR ASP ARG ARG TYR PHE THR ARG ALA
SEQRES 21 A 1161 VAL VAL ARG PRO GLY ARG LEU ARG ASP GLU ILE SER THR
SEQRES 22 A 1161 ALA GLU TYR LEU ILE SER GLU ALA ASP ARG VAL VAL ASN
SEQRES 23 A 1161 ASP ILE PHE ASP ALA LEU GLU ILE ILE GLY THR ASN LYS
SEQRES 24 A 1161 THR ASP LEU ASN HIS MET PHE ILE ASN PHE SER HIS THR
SEQRES 25 A 1161 PHE GLN VAL THR ALA ASP GLU VAL ALA GLU SER LEU GLN
SEQRES 26 A 1161 GLY PHE LEU ASP ARG PHE GLY PRO ARG GLY TRP ARG LEU
SEQRES 27 A 1161 ARG VAL HIS GLN VAL GLU ILE ARG ILE ASN CYS MET ARG
SEQRES 28 A 1161 SER ASP ASN ASN ASP GLU ASN ASP THR MET PRO LEU ARG
SEQRES 29 A 1161 VAL ILE ILE THR ASN THR SER GLY PHE VAL ILE GLN ILE
SEQRES 30 A 1161 GLU LEU TYR GLU GLU LYS LEU SER GLU LYS GLY GLU TRP
SEQRES 31 A 1161 VAL TYR TYR TYR VAL SER GLY ASN ALA LYS ILE GLY SER
SEQRES 32 A 1161 MET HIS LEU LEU PRO VAL SER THR PRO TYR PRO THR LYS
SEQRES 33 A 1161 ASN TRP LEU GLN PRO LYS ARG TYR LYS ALA HIS ILE LEU
SEQRES 34 A 1161 GLY THR GLN TYR VAL TYR ASP PHE PRO GLU LEU PHE ARG
SEQRES 35 A 1161 GLN ALA ILE GLN ASN SER TRP THR GLU ALA VAL LYS LYS
SEQRES 36 A 1161 ILE PRO SER LEU ALA ALA LYS GLN PRO ALA ILE GLY GLU
SEQRES 37 A 1161 CYS ILE ASP TYR ASN GLU LEU VAL LEU GLY ASP GLN ASP
SEQRES 38 A 1161 ASN LEU ALA GLU VAL SER ARG GLU PRO GLY MET ASN SER
SEQRES 39 A 1161 THR GLY MET VAL GLY TRP LEU ILE ASN ALA ARG THR PRO
SEQRES 40 A 1161 GLU TYR PRO ASP GLY ARG LYS PHE ILE VAL VAL ALA ASN
SEQRES 41 A 1161 ASP ILE THR PHE LYS ILE GLY SER PHE GLY PRO LYS GLU
SEQRES 42 A 1161 ASP THR PHE PHE PHE LYS CYS THR GLU LEU ALA ARG LYS
SEQRES 43 A 1161 MET GLY ILE PRO ARG ILE TYR LEU SER ALA ASN SER GLY
SEQRES 44 A 1161 ALA ARG LEU GLY LEU ALA GLU GLU LEU MET PRO HIS PHE
SEQRES 45 A 1161 ASN VAL ALA TRP ASN ASP PRO ALA LYS PRO GLU ALA GLY
SEQRES 46 A 1161 PHE LYS TYR LEU TYR LEU SER ASP GLU ALA LYS ARG ARG
SEQRES 47 A 1161 PHE GLU ASN GLU VAL ILE THR GLU GLU ILE VAL GLU ASP
SEQRES 48 A 1161 GLY GLU LYS ARG HIS LYS ILE ILE THR ILE VAL GLY ALA
SEQRES 49 A 1161 GLU GLU GLY LEU GLY VAL GLU CYS LEU ARG GLY SER GLY
SEQRES 50 A 1161 LEU ILE ALA GLY ALA THR SER ARG ALA TYR ASN ASP ILE
SEQRES 51 A 1161 PHE THR CYS THR LEU VAL THR CYS ARG SER VAL GLY ILE
SEQRES 52 A 1161 GLY ALA TYR LEU VAL ARG LEU GLY GLN ARG ALA VAL GLN
SEQRES 53 A 1161 VAL GLU GLY GLN PRO ILE ILE LEU THR GLY ALA PRO ALA
SEQRES 54 A 1161 LEU ASN SER LEU LEU GLY ARG GLU VAL TYR THR SER ASN
SEQRES 55 A 1161 LEU GLN LEU GLY GLY THR GLN ILE MET TYR ARG ASN GLY
SEQRES 56 A 1161 VAL SER HIS LEU THR ALA LYS ASP ASP PHE ASP GLY VAL
SEQRES 57 A 1161 THR LYS ILE VAL GLN TRP LEU SER PHE ILE PRO ASP GLN
SEQRES 58 A 1161 ARG ASN ASN PRO LEU PRO ILE LEU SER PRO SER PRO ASP
SEQRES 59 A 1161 PRO TRP ASP ARG ASP VAL VAL TYR THR PRO PRO TYR LYS
SEQRES 60 A 1161 GLN THR TYR ASP VAL ARG TRP MET ILE ALA GLY LYS GLU
SEQRES 61 A 1161 ASP GLU ASP GLY PHE GLN PRO GLY LEU PHE ASP LYS ASP
SEQRES 62 A 1161 SER PHE VAL GLU THR LEU GLY GLY TRP ALA ARG THR VAL
SEQRES 63 A 1161 VAL VAL GLY ARG ALA ARG LEU GLY GLY ILE PRO MET GLY
SEQRES 64 A 1161 VAL ILE ALA VAL GLU THR ARG THR ILE GLU ASN ILE THR
SEQRES 65 A 1161 PRO ALA ASP PRO ALA ASN PRO ASP SER ILE GLU GLN VAL
SEQRES 66 A 1161 THR ASN GLU ALA GLY GLY VAL TRP TYR PRO ASN SER ALA
SEQRES 67 A 1161 PHE LYS THR ALA GLN ALA ILE ASN ASP PHE ASN TYR GLY
SEQRES 68 A 1161 GLU GLN LEU PRO LEU MET ILE LEU ALA ASN TRP ARG GLY
SEQRES 69 A 1161 PHE SER GLY GLY GLN ARG ASP MET TYR ASN GLU VAL LEU
SEQRES 70 A 1161 LYS TYR GLY SER PHE ILE VAL ASP ALA LEU THR ARG PHE
SEQRES 71 A 1161 GLU LYS PRO ILE PHE ILE TYR ILE PRO PRO HIS GLY GLU
SEQRES 72 A 1161 LEU ARG GLY GLY SER TRP VAL VAL VAL ASP PRO THR ILE
SEQRES 73 A 1161 ASN PRO ALA SER MET GLU MET TYR ALA ASP GLU GLU ALA
SEQRES 74 A 1161 ARG GLY GLY VAL LEU GLU PRO GLU GLY ILE ILE PRO ILE
SEQRES 75 A 1161 LYS TYR LYS LYS ASP LYS GLN LEU GLU THR MET ALA ARG
SEQRES 76 A 1161 LEU ASP PRO VAL TYR ARG SER LEU LYS LYS GLU MET ALA
SEQRES 77 A 1161 LYS GLU GLY LEU SER LYS GLU GLU SER ASP ASN ILE LYS
SEQRES 78 A 1161 LYS LYS MET GLN GLN ARG GLU GLU LEU LEU LEU PRO ILE
SEQRES 79 A 1161 TYR HIS GLN ILE CYS VAL GLN PHE ALA ASP LEU HIS ASP
SEQRES 80 A 1161 ARG ALA GLY ARG MET LYS ALA LYS GLY VAL ILE ARG GLN
SEQRES 81 A 1161 SER LEU GLN TRP ARG GLN SER ARG ARG PHE PHE TYR TRP
SEQRES 82 A 1161 ARG VAL ARG ARG ARG LEU ILE GLU ASP ASP ILE LEU ARG
SEQRES 83 A 1161 ARG ILE GLU GLU ALA ILE ASN PRO ALA GLY LYS ARG ARG
SEQRES 84 A 1161 HIS ASP PRO GLU ASN THR SER LEU ALA ALA SER PRO GLU
SEQRES 85 A 1161 THR ARG SER PRO HIS LEU VAL GLN LEU GLU SER TRP VAL
SEQRES 86 A 1161 GLY ILE PRO GLY PHE LYS THR ASN ASP ARG GLU VAL VAL
SEQRES 87 A 1161 GLU TRP TYR GLU GLN ASN GLN ASP ARG ILE ASN GLU LYS
SEQRES 88 A 1161 LEU GLU LYS LEU LYS LYS GLU SER ILE ALA ASP GLN MET
SEQRES 89 A 1161 ARG GLU LEU LEU ARG UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 90 A 1161 UNK UNK UNK UNK
SEQRES 1 B 1161 GLY ASN LEU ARG GLU VAL ARG TYR HIS ASP GLU GLU ARG
SEQRES 2 B 1161 PRO TYR PHE ILE ASP TRP ASP PHE ALA LEU ARG LYS SER
SEQRES 3 B 1161 GLY ALA ASN GLN THR GLU SER SER MET HIS MET GLN SER
SEQRES 4 B 1161 VAL VAL PRO SER SER PRO ALA THR PRO VAL GLU ASN ASP
SEQRES 5 B 1161 PHE LYS ARG ILE HIS SER ILE SER ASP MET THR TYR LEU
SEQRES 6 B 1161 ALA ARG ARG THR ARG ASP GLU PRO ILE ARG LYS GLY VAL
SEQRES 7 B 1161 ILE VAL PRO CYS LYS ASP LEU LEU ASP ALA GLU GLU ALA
SEQRES 8 B 1161 LEU SER ARG ALA LEU GLU VAL LEU PRO LEU ALA HIS LYS
SEQRES 9 B 1161 GLU THR LYS ASP LYS ASP ARG LYS GLN GLN PRO GLY ILE
SEQRES 10 B 1161 ALA ALA ASP LEU ALA GLN ARG ARG ARG PRO GLY THR PRO
SEQRES 11 B 1161 LEU ARG LEU GLU GLY ILE GLY GLU LEU SER ALA VAL VAL
SEQRES 12 B 1161 ASN VAL ALA VAL ARG ASP ALA GLU GLY LYS ASN ASP GLU
SEQRES 13 B 1161 GLU ILE LEU ALA LEU ILE LYS PRO TRP VAL GLN ASN SER
SEQRES 14 B 1161 LYS ALA ASP LEU LEU ALA ARG ARG VAL ARG ARG LEU THR
SEQRES 15 B 1161 PHE ILE CYS GLY ARG ASN ASP GLY SER TYR PRO SER TYR
SEQRES 16 B 1161 TYR THR PHE ARG GLY PRO ASP TYR ALA GLU ASP ASP SER
SEQRES 17 B 1161 ILE ARG HIS ILE GLU PRO SER LEU ALA PHE GLN LEU GLU
SEQRES 18 B 1161 LEU GLY ARG LEU SER LYS PHE LYS LEU THR PRO VAL PHE
SEQRES 19 B 1161 THR GLN ASN LYS ASN ILE HIS VAL TYR GLU ALA VAL GLY
SEQRES 20 B 1161 ARG GLY VAL GLU THR ASP ARG ARG TYR PHE THR ARG ALA
SEQRES 21 B 1161 VAL VAL ARG PRO GLY ARG LEU ARG ASP GLU ILE SER THR
SEQRES 22 B 1161 ALA GLU TYR LEU ILE SER GLU ALA ASP ARG VAL VAL ASN
SEQRES 23 B 1161 ASP ILE PHE ASP ALA LEU GLU ILE ILE GLY THR ASN LYS
SEQRES 24 B 1161 THR ASP LEU ASN HIS MET PHE ILE ASN PHE SER HIS THR
SEQRES 25 B 1161 PHE GLN VAL THR ALA ASP GLU VAL ALA GLU SER LEU GLN
SEQRES 26 B 1161 GLY PHE LEU ASP ARG PHE GLY PRO ARG GLY TRP ARG LEU
SEQRES 27 B 1161 ARG VAL HIS GLN VAL GLU ILE ARG ILE ASN CYS MET ARG
SEQRES 28 B 1161 SER ASP ASN ASN ASP GLU ASN ASP THR MET PRO LEU ARG
SEQRES 29 B 1161 VAL ILE ILE THR ASN THR SER GLY PHE VAL ILE GLN ILE
SEQRES 30 B 1161 GLU LEU TYR GLU GLU LYS LEU SER GLU LYS GLY GLU TRP
SEQRES 31 B 1161 VAL TYR TYR TYR VAL SER GLY ASN ALA LYS ILE GLY SER
SEQRES 32 B 1161 MET HIS LEU LEU PRO VAL SER THR PRO TYR PRO THR LYS
SEQRES 33 B 1161 ASN TRP LEU GLN PRO LYS ARG TYR LYS ALA HIS ILE LEU
SEQRES 34 B 1161 GLY THR GLN TYR VAL TYR ASP PHE PRO GLU LEU PHE ARG
SEQRES 35 B 1161 GLN ALA ILE GLN ASN SER TRP THR GLU ALA VAL LYS LYS
SEQRES 36 B 1161 ILE PRO SER LEU ALA ALA LYS GLN PRO ALA ILE GLY GLU
SEQRES 37 B 1161 CYS ILE ASP TYR ASN GLU LEU VAL LEU GLY ASP GLN ASP
SEQRES 38 B 1161 ASN LEU ALA GLU VAL SER ARG GLU PRO GLY MET ASN SER
SEQRES 39 B 1161 THR GLY MET VAL GLY TRP LEU ILE ASN ALA ARG THR PRO
SEQRES 40 B 1161 GLU TYR PRO ASP GLY ARG LYS PHE ILE VAL VAL ALA ASN
SEQRES 41 B 1161 ASP ILE THR PHE LYS ILE GLY SER PHE GLY PRO LYS GLU
SEQRES 42 B 1161 ASP THR PHE PHE PHE LYS CYS THR GLU LEU ALA ARG LYS
SEQRES 43 B 1161 MET GLY ILE PRO ARG ILE TYR LEU SER ALA ASN SER GLY
SEQRES 44 B 1161 ALA ARG LEU GLY LEU ALA GLU GLU LEU MET PRO HIS PHE
SEQRES 45 B 1161 ASN VAL ALA TRP ASN ASP PRO ALA LYS PRO GLU ALA GLY
SEQRES 46 B 1161 PHE LYS TYR LEU TYR LEU SER ASP GLU ALA LYS ARG ARG
SEQRES 47 B 1161 PHE GLU ASN GLU VAL ILE THR GLU GLU ILE VAL GLU ASP
SEQRES 48 B 1161 GLY GLU LYS ARG HIS LYS ILE ILE THR ILE VAL GLY ALA
SEQRES 49 B 1161 GLU GLU GLY LEU GLY VAL GLU CYS LEU ARG GLY SER GLY
SEQRES 50 B 1161 LEU ILE ALA GLY ALA THR SER ARG ALA TYR ASN ASP ILE
SEQRES 51 B 1161 PHE THR CYS THR LEU VAL THR CYS ARG SER VAL GLY ILE
SEQRES 52 B 1161 GLY ALA TYR LEU VAL ARG LEU GLY GLN ARG ALA VAL GLN
SEQRES 53 B 1161 VAL GLU GLY GLN PRO ILE ILE LEU THR GLY ALA PRO ALA
SEQRES 54 B 1161 LEU ASN SER LEU LEU GLY ARG GLU VAL TYR THR SER ASN
SEQRES 55 B 1161 LEU GLN LEU GLY GLY THR GLN ILE MET TYR ARG ASN GLY
SEQRES 56 B 1161 VAL SER HIS LEU THR ALA LYS ASP ASP PHE ASP GLY VAL
SEQRES 57 B 1161 THR LYS ILE VAL GLN TRP LEU SER PHE ILE PRO ASP GLN
SEQRES 58 B 1161 ARG ASN ASN PRO LEU PRO ILE LEU SER PRO SER PRO ASP
SEQRES 59 B 1161 PRO TRP ASP ARG ASP VAL VAL TYR THR PRO PRO TYR LYS
SEQRES 60 B 1161 GLN THR TYR ASP VAL ARG TRP MET ILE ALA GLY LYS GLU
SEQRES 61 B 1161 ASP GLU ASP GLY PHE GLN PRO GLY LEU PHE ASP LYS ASP
SEQRES 62 B 1161 SER PHE VAL GLU THR LEU GLY GLY TRP ALA ARG THR VAL
SEQRES 63 B 1161 VAL VAL GLY ARG ALA ARG LEU GLY GLY ILE PRO MET GLY
SEQRES 64 B 1161 VAL ILE ALA VAL GLU THR ARG THR ILE GLU ASN ILE THR
SEQRES 65 B 1161 PRO ALA ASP PRO ALA ASN PRO ASP SER ILE GLU GLN VAL
SEQRES 66 B 1161 THR ASN GLU ALA GLY GLY VAL TRP TYR PRO ASN SER ALA
SEQRES 67 B 1161 PHE LYS THR ALA GLN ALA ILE ASN ASP PHE ASN TYR GLY
SEQRES 68 B 1161 GLU GLN LEU PRO LEU MET ILE LEU ALA ASN TRP ARG GLY
SEQRES 69 B 1161 PHE SER GLY GLY GLN ARG ASP MET TYR ASN GLU VAL LEU
SEQRES 70 B 1161 LYS TYR GLY SER PHE ILE VAL ASP ALA LEU THR ARG PHE
SEQRES 71 B 1161 GLU LYS PRO ILE PHE ILE TYR ILE PRO PRO HIS GLY GLU
SEQRES 72 B 1161 LEU ARG GLY GLY SER TRP VAL VAL VAL ASP PRO THR ILE
SEQRES 73 B 1161 ASN PRO ALA SER MET GLU MET TYR ALA ASP GLU GLU ALA
SEQRES 74 B 1161 ARG GLY GLY VAL LEU GLU PRO GLU GLY ILE ILE PRO ILE
SEQRES 75 B 1161 LYS TYR LYS LYS ASP LYS GLN LEU GLU THR MET ALA ARG
SEQRES 76 B 1161 LEU ASP PRO VAL TYR ARG SER LEU LYS LYS GLU MET ALA
SEQRES 77 B 1161 LYS GLU GLY LEU SER LYS GLU GLU SER ASP ASN ILE LYS
SEQRES 78 B 1161 LYS LYS MET GLN GLN ARG GLU GLU LEU LEU LEU PRO ILE
SEQRES 79 B 1161 TYR HIS GLN ILE CYS VAL GLN PHE ALA ASP LEU HIS ASP
SEQRES 80 B 1161 ARG ALA GLY ARG MET LYS ALA LYS GLY VAL ILE ARG GLN
SEQRES 81 B 1161 SER LEU GLN TRP ARG GLN SER ARG ARG PHE PHE TYR TRP
SEQRES 82 B 1161 ARG VAL ARG ARG ARG LEU ILE GLU ASP ASP ILE LEU ARG
SEQRES 83 B 1161 ARG ILE GLU GLU ALA ILE ASN PRO ALA GLY LYS ARG ARG
SEQRES 84 B 1161 HIS ASP PRO GLU ASN THR SER LEU ALA ALA SER PRO GLU
SEQRES 85 B 1161 THR ARG SER PRO HIS LEU VAL GLN LEU GLU SER TRP VAL
SEQRES 86 B 1161 GLY ILE PRO GLY PHE LYS THR ASN ASP ARG GLU VAL VAL
SEQRES 87 B 1161 GLU TRP TYR GLU GLN ASN GLN ASP ARG ILE ASN GLU LYS
SEQRES 88 B 1161 LEU GLU LYS LEU LYS LYS GLU SER ILE ALA ASP GLN MET
SEQRES 89 B 1161 ARG GLU LEU LEU ARG UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 90 B 1161 UNK UNK UNK UNK
HELIX 1 AA1 LEU A 1198 ALA A 1200 5 3
HELIX 2 AA2 GLU A 1201 ARG A 1206 1 6
HELIX 3 AA3 ALA A 1207 VAL A 1210 5 4
HELIX 4 AA4 ILE A 1274 SER A 1281 1 8
HELIX 5 AA5 ALA A 1283 ARG A 1288 1 6
HELIX 6 AA6 GLU A 1325 GLU A 1333 1 9
HELIX 7 AA7 GLU A 1387 GLY A 1408 1 22
HELIX 8 AA8 THR A 1428 LEU A 1450 1 23
HELIX 9 AA9 LEU A 1531 ILE A 1540 1 10
HELIX 10 AB1 TYR A 1545 TYR A 1547 5 3
HELIX 11 AB2 ASP A 1548 ILE A 1568 1 21
HELIX 12 AB3 THR A 1635 SER A 1640 5 6
HELIX 13 AB4 GLY A 1642 GLY A 1660 1 19
HELIX 14 AB5 ALA A 1677 MET A 1681 5 5
HELIX 15 AB6 SER A 1704 ARG A 1709 1 6
HELIX 16 AB7 GLY A 1741 ASN A 1760 1 20
HELIX 17 AB8 GLY A 1774 GLY A 1783 1 10
HELIX 18 AB9 GLY A 1798 GLY A 1807 1 10
HELIX 19 AC1 ASN A 1814 GLY A 1819 1 6
HELIX 20 AC2 GLY A 1819 TYR A 1824 1 6
HELIX 21 AC3 ASP A 1835 ILE A 1850 1 16
HELIX 22 AC4 VAL A 1884 ALA A 1889 1 6
HELIX 23 AC5 TYR A 1966 TYR A 1982 1 17
HELIX 24 AC6 GLY A 2000 ASN A 2006 1 7
HELIX 25 AC7 GLU A 2007 PHE A 2022 1 16
HELIX 26 AC8 ARG A 2037 VAL A 2043 1 7
HELIX 27 AC9 GLU A 2067 TYR A 2076 1 10
HELIX 28 AD1 LYS A 2077 ASP A 2089 1 13
HELIX 29 AD2 ASP A 2089 LYS A 2101 1 13
HELIX 30 AD3 SER A 2105 ARG A 2140 1 36
HELIX 31 AD4 ARG A 2140 LYS A 2147 1 8
HELIX 32 AD5 GLN A 2155 ARG A 2157 5 3
HELIX 33 AD6 GLN A 2158 ASN A 2185 1 28
HELIX 34 AD7 SER A 2202 ARG A 2206 5 5
HELIX 35 AD8 VAL A 2211 GLY A 2218 1 8
HELIX 36 AD9 ASN A 2225 ASN A 2236 1 12
HELIX 37 AE1 ASN A 2236 LEU A 2259 1 24
HELIX 38 AE2 UNK A 2301 UNK A 2311 1 11
HELIX 39 AE3 LEU B 1198 ALA B 1200 5 3
HELIX 40 AE4 GLU B 1201 ARG B 1206 1 6
HELIX 41 AE5 ALA B 1207 VAL B 1210 5 4
HELIX 42 AE6 ILE B 1274 SER B 1281 1 8
HELIX 43 AE7 ALA B 1283 ARG B 1288 1 6
HELIX 44 AE8 SER B 1327 GLU B 1333 5 7
HELIX 45 AE9 GLU B 1387 GLY B 1408 1 22
HELIX 46 AF1 THR B 1428 LEU B 1450 1 23
HELIX 47 AF2 TRP B 1530 ILE B 1540 1 11
HELIX 48 AF3 TYR B 1545 TYR B 1547 5 3
HELIX 49 AF4 ASP B 1548 ILE B 1568 1 21
HELIX 50 AF5 THR B 1635 SER B 1640 5 6
HELIX 51 AF6 GLY B 1642 GLY B 1660 1 19
HELIX 52 AF7 ALA B 1677 MET B 1681 5 5
HELIX 53 AF8 SER B 1704 ARG B 1709 1 6
HELIX 54 AF9 GLY B 1741 ASN B 1760 1 20
HELIX 55 AG1 GLY B 1774 GLY B 1783 1 10
HELIX 56 AG2 GLY B 1798 GLY B 1807 1 10
HELIX 57 AG3 ASN B 1814 GLY B 1819 1 6
HELIX 58 AG4 GLY B 1819 TYR B 1824 1 6
HELIX 59 AG5 ASP B 1835 ILE B 1850 1 16
HELIX 60 AG6 VAL B 1884 ALA B 1889 1 6
HELIX 61 AG7 TYR B 1966 TYR B 1982 1 17
HELIX 62 AG8 GLY B 2000 ASN B 2006 1 7
HELIX 63 AG9 GLU B 2007 PHE B 2022 1 16
HELIX 64 AH1 ARG B 2037 VAL B 2043 1 7
HELIX 65 AH2 GLU B 2067 TYR B 2076 1 10
HELIX 66 AH3 LYS B 2077 ASP B 2089 1 13
HELIX 67 AH4 ASP B 2089 LYS B 2101 1 13
HELIX 68 AH5 SER B 2105 ARG B 2140 1 36
HELIX 69 AH6 ARG B 2140 LYS B 2147 1 8
HELIX 70 AH7 GLN B 2155 ARG B 2157 5 3
HELIX 71 AH8 GLN B 2158 ASN B 2185 1 28
HELIX 72 AH9 SER B 2202 ARG B 2206 5 5
HELIX 73 AI1 VAL B 2211 GLY B 2218 1 8
HELIX 74 AI2 ASN B 2225 ASN B 2236 1 12
HELIX 75 AI3 ASN B 2236 ARG B 2261 1 26
HELIX 76 AI4 UNK B 2301 UNK B 2311 1 11
SHEET 1 AA1 4 GLY A1189 PRO A1193 0
SHEET 2 AA1 4 VAL A1254 VAL A1259 1 O ALA A1258 N VAL A1192
SHEET 3 AA1 4 ARG A1292 CYS A1297 1 O THR A1294 N VAL A1255
SHEET 4 AA1 4 THR A1309 ARG A1311 -1 O PHE A1310 N LEU A1293
SHEET 1 AA2 7 PHE A1340 VAL A1345 0
SHEET 2 AA2 7 ILE A1352 GLY A1359 -1 O GLU A1356 N THR A1343
SHEET 3 AA2 7 ARG A1367 VAL A1374 -1 O ARG A1367 N ALA A1357
SHEET 4 AA2 7 ASN A1415 PHE A1421 1 O ASN A1420 N VAL A1374
SHEET 5 AA2 7 GLN A1454 ILE A1459 1 O GLU A1456 N ILE A1419
SHEET 6 AA2 7 LEU A1475 THR A1480 -1 O VAL A1477 N ILE A1457
SHEET 7 AA2 7 ILE A1489 LEU A1491 -1 O GLU A1490 N ILE A1478
SHEET 1 AA3 2 GLU A1494 LEU A1496 0
SHEET 2 AA3 2 TRP A1502 TYR A1504 -1 O VAL A1503 N LYS A1495
SHEET 1 AA4 8 ALA A1596 VAL A1598 0
SHEET 2 AA4 8 TYR A1584 VAL A1588 -1 N GLU A1586 O VAL A1598
SHEET 3 AA4 8 MET A1609 ALA A1616 -1 O GLY A1611 N LEU A1587
SHEET 4 AA4 8 ARG A1625 ASN A1632 -1 O ALA A1631 N VAL A1610
SHEET 5 AA4 8 ARG A1663 SER A1667 1 O ILE A1664 N VAL A1630
SHEET 6 AA4 8 THR A1764 VAL A1768 1 O CYS A1765 N TYR A1665
SHEET 7 AA4 8 ALA A1786 VAL A1789 1 O VAL A1787 N VAL A1768
SHEET 8 AA4 8 LEU A1831 ALA A1833 1 O LEU A1831 N GLN A1788
SHEET 1 AA5 4 ASN A1685 TRP A1688 0
SHEET 2 AA5 4 PHE A1698 LEU A1703 -1 O TYR A1702 N ASN A1685
SHEET 3 AA5 4 GLU A1725 ILE A1733 -1 O ILE A1730 N LEU A1701
SHEET 4 AA5 4 VAL A1715 GLU A1722 -1 N ILE A1716 O THR A1732
SHEET 1 AA6 2 SER A1772 VAL A1773 0
SHEET 2 AA6 2 ILE A1794 ILE A1795 1 O ILE A1795 N SER A1772
SHEET 1 AA7 2 GLY A1890 GLU A1892 0
SHEET 2 AA7 2 PHE A1897 PRO A1899 -1 O GLN A1898 N LYS A1891
SHEET 1 AA8 7 VAL A1908 THR A1910 0
SHEET 2 AA8 7 VAL A1918 LEU A1925 -1 O ARG A1922 N VAL A1908
SHEET 3 AA8 7 ILE A1928 VAL A1935 -1 O VAL A1932 N GLY A1921
SHEET 4 AA8 7 LEU A1988 LEU A1991 1 O MET A1989 N GLY A1931
SHEET 5 AA8 7 ILE A2026 ILE A2030 1 O PHE A2027 N ILE A1990
SHEET 6 AA8 7 MET A2053 ASP A2058 1 O TYR A2056 N ILE A2028
SHEET 7 AA8 7 SER A2153 LEU A2154 1 O LEU A2154 N ALA A2057
SHEET 1 AA9 2 ILE A1940 THR A1944 0
SHEET 2 AA9 2 GLN A1956 GLU A1960 -1 O GLN A1956 N THR A1944
SHEET 1 AB1 4 GLY B1189 ILE B1191 0
SHEET 2 AB1 4 VAL B1254 VAL B1259 1 O ASN B1256 N VAL B1190
SHEET 3 AB1 4 ARG B1292 CYS B1297 1 O THR B1294 N VAL B1255
SHEET 4 AB1 4 SER B1306 TYR B1307 -1 O SER B1306 N CYS B1297
SHEET 1 AB2 4 GLY B1189 ILE B1191 0
SHEET 2 AB2 4 VAL B1254 VAL B1259 1 O ASN B1256 N VAL B1190
SHEET 3 AB2 4 ARG B1292 CYS B1297 1 O THR B1294 N VAL B1255
SHEET 4 AB2 4 PHE B1310 ARG B1311 -1 O PHE B1310 N LEU B1293
SHEET 1 AB3 8 PHE B1340 VAL B1345 0
SHEET 2 AB3 8 ILE B1352 GLY B1359 -1 O GLU B1356 N THR B1343
SHEET 3 AB3 8 ARG B1366 VAL B1374 -1 O ARG B1367 N ALA B1357
SHEET 4 AB3 8 ASN B1415 PHE B1421 1 O HIS B1416 N THR B1370
SHEET 5 AB3 8 GLN B1454 CYS B1461 1 O GLU B1456 N ILE B1419
SHEET 6 AB3 8 MET B1473 THR B1480 -1 O LEU B1475 N ILE B1459
SHEET 7 AB3 8 ILE B1489 LEU B1496 -1 O TYR B1492 N ARG B1476
SHEET 8 AB3 8 TRP B1502 TYR B1506 -1 O VAL B1503 N LYS B1495
SHEET 1 AB4 8 ALA B1596 VAL B1598 0
SHEET 2 AB4 8 TYR B1584 VAL B1588 -1 N GLU B1586 O VAL B1598
SHEET 3 AB4 8 MET B1609 ALA B1616 -1 O GLY B1611 N LEU B1587
SHEET 4 AB4 8 ARG B1625 ASN B1632 -1 O ALA B1631 N VAL B1610
SHEET 5 AB4 8 ARG B1663 SER B1667 1 O LEU B1666 N VAL B1630
SHEET 6 AB4 8 THR B1764 VAL B1768 1 O CYS B1765 N TYR B1665
SHEET 7 AB4 8 ARG B1785 VAL B1789 1 O VAL B1787 N VAL B1768
SHEET 8 AB4 8 LEU B1831 ALA B1833 1 O LEU B1831 N GLN B1788
SHEET 1 AB5 4 ASN B1685 TRP B1688 0
SHEET 2 AB5 4 PHE B1698 LEU B1703 -1 O TYR B1702 N ASN B1685
SHEET 3 AB5 4 GLU B1725 ILE B1733 -1 O ILE B1730 N LEU B1701
SHEET 4 AB5 4 VAL B1715 GLU B1722 -1 N ILE B1716 O THR B1732
SHEET 1 AB6 2 SER B1772 VAL B1773 0
SHEET 2 AB6 2 ILE B1794 ILE B1795 1 O ILE B1795 N SER B1772
SHEET 1 AB7 2 GLY B1890 GLU B1892 0
SHEET 2 AB7 2 PHE B1897 PRO B1899 -1 O GLN B1898 N LYS B1891
SHEET 1 AB8 7 VAL B1908 THR B1910 0
SHEET 2 AB8 7 VAL B1918 LEU B1925 -1 O ARG B1922 N VAL B1908
SHEET 3 AB8 7 ILE B1928 VAL B1935 -1 O ALA B1934 N VAL B1919
SHEET 4 AB8 7 LEU B1988 LEU B1991 1 O MET B1989 N GLY B1931
SHEET 5 AB8 7 ILE B2026 ILE B2030 1 O PHE B2027 N ILE B1990
SHEET 6 AB8 7 MET B2053 ASP B2058 1 O TYR B2056 N ILE B2028
SHEET 7 AB8 7 SER B2153 LEU B2154 1 O LEU B2154 N ALA B2057
SHEET 1 AB9 2 ILE B1940 THR B1944 0
SHEET 2 AB9 2 GLN B1956 GLU B1960 -1 O GLN B1956 N THR B1944
LINK C UNK A2300 N UNK A2301 1555 1555 1.36
LINK C UNK A2301 N UNK A2302 1555 1555 1.35
LINK C UNK A2302 N UNK A2303 1555 1555 1.36
LINK C UNK A2303 N UNK A2304 1555 1555 1.35
LINK C UNK A2304 N UNK A2305 1555 1555 1.36
LINK C UNK A2305 N UNK A2306 1555 1555 1.36
LINK C UNK A2306 N UNK A2307 1555 1555 1.34
LINK C UNK A2307 N UNK A2308 1555 1555 1.37
LINK C UNK A2308 N UNK A2309 1555 1555 1.36
LINK C UNK A2309 N UNK A2310 1555 1555 1.35
LINK C UNK A2310 N UNK A2311 1555 1555 1.36
LINK C UNK B2300 N UNK B2301 1555 1555 1.37
LINK C UNK B2301 N UNK B2302 1555 1555 1.36
LINK C UNK B2302 N UNK B2303 1555 1555 1.37
LINK C UNK B2303 N UNK B2304 1555 1555 1.35
LINK C UNK B2304 N UNK B2305 1555 1555 1.36
LINK C UNK B2305 N UNK B2306 1555 1555 1.36
LINK C UNK B2306 N UNK B2307 1555 1555 1.34
LINK C UNK B2307 N UNK B2308 1555 1555 1.36
LINK C UNK B2308 N UNK B2309 1555 1555 1.35
LINK C UNK B2309 N UNK B2310 1555 1555 1.35
LINK C UNK B2310 N UNK B2311 1555 1555 1.35
CRYST1 100.170 153.450 249.240 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009983 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006517 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004012 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
