HEADER TRANSCRIPTION/DNA/RNA 29-SEP-15 5E17
TITLE T. THERMOPHILUS TRANSCRIPTION INITIATION COMPLEX HAVING A RRR
TITLE 2 DISCRIMINATOR SEQUENCE AND A NONTEMPLATE-STRAND LENGTH CORRESPONDING
TITLE 3 TO TSS SELECTION AT POSITION 7 (RPO-GGG-7)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RNAP SUBUNIT ALPHA,RNA POLYMERASE SUBUNIT ALPHA,
COMPND 5 TRANSCRIPTASE SUBUNIT ALPHA;
COMPND 6 EC: 2.7.7.6;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND 9 CHAIN: C;
COMPND 10 SYNONYM: RNAP SUBUNIT BETA,RNA POLYMERASE SUBUNIT BETA,TRANSCRIPTASE
COMPND 11 SUBUNIT BETA;
COMPND 12 EC: 2.7.7.6;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA';
COMPND 15 CHAIN: D;
COMPND 16 SYNONYM: RNAP SUBUNIT BETA',RNA POLYMERASE SUBUNIT BETA',
COMPND 17 TRANSCRIPTASE SUBUNIT BETA';
COMPND 18 EC: 2.7.7.6;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA;
COMPND 21 CHAIN: E;
COMPND 22 SYNONYM: RNAP OMEGA SUBUNIT,RNA POLYMERASE OMEGA SUBUNIT,
COMPND 23 TRANSCRIPTASE SUBUNIT OMEGA;
COMPND 24 EC: 2.7.7.6;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: RNA POLYMERASE SIGMA FACTOR SIGA;
COMPND 27 CHAIN: F;
COMPND 28 ENGINEERED: YES;
COMPND 29 MOL_ID: 6;
COMPND 30 MOLECULE: DNA (5'-
COMPND 31 D(*CP*CP*T*GP*CP*AP*TP*CP*CP*GP*TP*GP*AP*GP*TP*CP*GP*AP*GP*GP*G)-3');
COMPND 32 CHAIN: G;
COMPND 33 ENGINEERED: YES;
COMPND 34 MOL_ID: 7;
COMPND 35 MOLECULE: DNA (27-MER);
COMPND 36 CHAIN: H;
COMPND 37 ENGINEERED: YES;
COMPND 38 MOL_ID: 8;
COMPND 39 MOLECULE: RNA (5'-R(*CP*CP*CP*UP*CP*GP*A)-3');
COMPND 40 CHAIN: I;
COMPND 41 ENGINEERED: YES;
COMPND 42 OTHER_DETAILS: RNA -6+1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS (STRAIN HB8 / ATCC 27634 /
SOURCE 6 DSM 579);
SOURCE 7 ORGANISM_TAXID: 300852;
SOURCE 8 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS (STRAIN HB8 / ATCC 27634 /
SOURCE 11 DSM 579);
SOURCE 12 ORGANISM_TAXID: 300852;
SOURCE 13 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 14 MOL_ID: 4;
SOURCE 15 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS (STRAIN HB8 / ATCC 27634 /
SOURCE 16 DSM 579);
SOURCE 17 ORGANISM_TAXID: 300852;
SOURCE 18 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 19 MOL_ID: 5;
SOURCE 20 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS (STRAIN HB8 / ATCC 27634 /
SOURCE 21 DSM 579);
SOURCE 22 ORGANISM_TAXID: 300852;
SOURCE 23 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 24 GENE: SIGA, TTHA0532;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 27 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 30 MOL_ID: 6;
SOURCE 31 SYNTHETIC: YES;
SOURCE 32 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 33 ORGANISM_TAXID: 274;
SOURCE 34 MOL_ID: 7;
SOURCE 35 SYNTHETIC: YES;
SOURCE 36 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 37 ORGANISM_TAXID: 274;
SOURCE 38 MOL_ID: 8;
SOURCE 39 SYNTHETIC: YES;
SOURCE 40 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 41 ORGANISM_TAXID: 274
KEYWDS DNA, SINGLE-STRANDED, DNA-DIRECTED RNA POLYMERASES, GENE EXPRESSION
KEYWDS 2 REGULATION, BACTERIAL, PROMOTER REGIONS, PROTEIN CONFORMATION, SIGMA
KEYWDS 3 FACTOR, THERMUS THERMOPHILUS, TRANSCRIPTION INITIATION, START SITE
KEYWDS 4 SELECTION, PROMOTER ESCAPE, INITIAL TRANSCRIPT, ABORTIVE PRODUCT,
KEYWDS 5 SIGMA FINGER, TRANSCRIPTION-DNA-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,R.H.EBRIGHT
REVDAT 3 27-SEP-23 5E17 1 JRNL REMARK LINK
REVDAT 2 16-MAR-16 5E17 1 JRNL
REVDAT 1 09-MAR-16 5E17 0
JRNL AUTH J.T.WINKELMAN,I.O.VVEDENSKAYA,Y.ZHANG,Y.ZHANG,J.G.BIRD,
JRNL AUTH 2 D.M.TAYLOR,R.L.GOURSE,R.H.EBRIGHT,B.E.NICKELS
JRNL TITL MULTIPLEXED PROTEIN-DNA CROSS-LINKING: SCRUNCHING IN
JRNL TITL 2 TRANSCRIPTION START SITE SELECTION.
JRNL REF SCIENCE V. 351 1090 2016
JRNL REFN ESSN 1095-9203
JRNL PMID 26941320
JRNL DOI 10.1126/SCIENCE.AAD6881
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 85533
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.8205 - 9.8337 0.99 3031 157 0.2409 0.2362
REMARK 3 2 9.8337 - 7.8247 1.00 2957 153 0.1934 0.2403
REMARK 3 3 7.8247 - 6.8413 1.00 2969 142 0.2295 0.2539
REMARK 3 4 6.8413 - 6.2184 1.00 2897 163 0.2272 0.2683
REMARK 3 5 6.2184 - 5.7741 1.00 2928 156 0.2269 0.2994
REMARK 3 6 5.7741 - 5.4346 1.00 2918 154 0.2046 0.2772
REMARK 3 7 5.4346 - 5.1630 1.00 2904 155 0.1944 0.2111
REMARK 3 8 5.1630 - 4.9387 1.00 2914 157 0.1790 0.2276
REMARK 3 9 4.9387 - 4.7489 0.99 2857 138 0.1735 0.2149
REMARK 3 10 4.7489 - 4.5852 0.98 2864 151 0.1714 0.1935
REMARK 3 11 4.5852 - 4.4421 0.97 2826 147 0.1734 0.2077
REMARK 3 12 4.4421 - 4.3152 0.95 2753 141 0.1729 0.2206
REMARK 3 13 4.3152 - 4.2018 0.93 2701 143 0.1845 0.2216
REMARK 3 14 4.2018 - 4.0994 0.93 2689 145 0.1885 0.2478
REMARK 3 15 4.0994 - 4.0062 0.91 2623 139 0.1929 0.2368
REMARK 3 16 4.0062 - 3.9211 0.91 2656 127 0.1976 0.2805
REMARK 3 17 3.9211 - 3.8427 0.90 2587 151 0.2132 0.2446
REMARK 3 18 3.8427 - 3.7702 0.90 2587 149 0.2174 0.2940
REMARK 3 19 3.7702 - 3.7030 0.89 2613 131 0.2177 0.2667
REMARK 3 20 3.7030 - 3.6402 0.91 2605 136 0.2285 0.2526
REMARK 3 21 3.6402 - 3.5815 0.89 2567 134 0.2317 0.3148
REMARK 3 22 3.5815 - 3.5265 0.90 2609 147 0.2407 0.2920
REMARK 3 23 3.5265 - 3.4746 0.89 2555 132 0.2575 0.3546
REMARK 3 24 3.4746 - 3.4257 0.90 2618 131 0.2640 0.3378
REMARK 3 25 3.4257 - 3.3795 0.90 2592 140 0.2613 0.3359
REMARK 3 26 3.3795 - 3.3356 0.89 2546 129 0.2792 0.3308
REMARK 3 27 3.3356 - 3.2939 0.91 2635 143 0.2808 0.3400
REMARK 3 28 3.2939 - 3.2542 0.88 2554 154 0.2894 0.3599
REMARK 3 29 3.2542 - 3.2164 0.90 2593 109 0.2934 0.3251
REMARK 3 30 3.2164 - 3.1803 0.73 2119 112 0.3007 0.3683
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 29265
REMARK 3 ANGLE : 0.825 39783
REMARK 3 CHIRALITY : 0.032 4484
REMARK 3 PLANARITY : 0.004 5044
REMARK 3 DIHEDRAL : 13.864 11387
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5E17 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000214120.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 HKL2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85564
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.18500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.86300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4G7H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 8.4, 200 MM
REMARK 280 POTASSIUM CHLORIDE, 50 MM MAGNESIUM CHLORIDE, 9.5% PEG4000,,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 91.50350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.78300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.50350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.78300
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: NONAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 53930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 143120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -238.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I
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 MET A 1
REMARK 465 LEU A 2
REMARK 465 ASP A 3
REMARK 465 ALA A 235
REMARK 465 PRO A 236
REMARK 465 GLU A 237
REMARK 465 GLU A 238
REMARK 465 ALA A 239
REMARK 465 LYS A 240
REMARK 465 GLU A 241
REMARK 465 PRO A 242
REMARK 465 GLU A 243
REMARK 465 ALA A 244
REMARK 465 PRO A 245
REMARK 465 PRO A 246
REMARK 465 GLU A 247
REMARK 465 GLN A 248
REMARK 465 GLU A 249
REMARK 465 GLU A 250
REMARK 465 GLU A 251
REMARK 465 LEU A 252
REMARK 465 ASP A 253
REMARK 465 LEU A 254
REMARK 465 PRO A 255
REMARK 465 LEU A 256
REMARK 465 GLU A 257
REMARK 465 GLU A 258
REMARK 465 LEU A 259
REMARK 465 GLY A 260
REMARK 465 LEU A 261
REMARK 465 SER A 262
REMARK 465 THR A 263
REMARK 465 ARG A 264
REMARK 465 VAL A 265
REMARK 465 LEU A 266
REMARK 465 HIS A 267
REMARK 465 SER A 268
REMARK 465 LEU A 269
REMARK 465 LYS A 270
REMARK 465 GLU A 271
REMARK 465 GLU A 272
REMARK 465 GLY A 273
REMARK 465 ILE A 274
REMARK 465 GLU A 275
REMARK 465 SER A 276
REMARK 465 VAL A 277
REMARK 465 ARG A 278
REMARK 465 ALA A 279
REMARK 465 LEU A 280
REMARK 465 LEU A 281
REMARK 465 ALA A 282
REMARK 465 LEU A 283
REMARK 465 ASN A 284
REMARK 465 LEU A 285
REMARK 465 LYS A 286
REMARK 465 ASP A 287
REMARK 465 LEU A 288
REMARK 465 LYS A 289
REMARK 465 ASN A 290
REMARK 465 ILE A 291
REMARK 465 PRO A 292
REMARK 465 GLY A 293
REMARK 465 ILE A 294
REMARK 465 GLY A 295
REMARK 465 GLU A 296
REMARK 465 ARG A 297
REMARK 465 SER A 298
REMARK 465 LEU A 299
REMARK 465 GLU A 300
REMARK 465 GLU A 301
REMARK 465 ILE A 302
REMARK 465 LYS A 303
REMARK 465 GLU A 304
REMARK 465 ALA A 305
REMARK 465 LEU A 306
REMARK 465 GLU A 307
REMARK 465 LYS A 308
REMARK 465 LYS A 309
REMARK 465 GLY A 310
REMARK 465 PHE A 311
REMARK 465 THR A 312
REMARK 465 LEU A 313
REMARK 465 LYS A 314
REMARK 465 GLU A 315
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 ASP B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 ASN B 91
REMARK 465 GLN B 229
REMARK 465 ALA B 230
REMARK 465 ALA B 231
REMARK 465 ALA B 232
REMARK 465 VAL B 233
REMARK 465 ALA B 234
REMARK 465 ALA B 235
REMARK 465 PRO B 236
REMARK 465 GLU B 237
REMARK 465 GLU B 238
REMARK 465 ALA B 239
REMARK 465 LYS B 240
REMARK 465 GLU B 241
REMARK 465 PRO B 242
REMARK 465 GLU B 243
REMARK 465 ALA B 244
REMARK 465 PRO B 245
REMARK 465 PRO B 246
REMARK 465 GLU B 247
REMARK 465 GLN B 248
REMARK 465 GLU B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 LEU B 252
REMARK 465 ASP B 253
REMARK 465 LEU B 254
REMARK 465 PRO B 255
REMARK 465 LEU B 256
REMARK 465 GLU B 257
REMARK 465 GLU B 258
REMARK 465 LEU B 259
REMARK 465 GLY B 260
REMARK 465 LEU B 261
REMARK 465 SER B 262
REMARK 465 THR B 263
REMARK 465 ARG B 264
REMARK 465 VAL B 265
REMARK 465 LEU B 266
REMARK 465 HIS B 267
REMARK 465 SER B 268
REMARK 465 LEU B 269
REMARK 465 LYS B 270
REMARK 465 GLU B 271
REMARK 465 GLU B 272
REMARK 465 GLY B 273
REMARK 465 ILE B 274
REMARK 465 GLU B 275
REMARK 465 SER B 276
REMARK 465 VAL B 277
REMARK 465 ARG B 278
REMARK 465 ALA B 279
REMARK 465 LEU B 280
REMARK 465 LEU B 281
REMARK 465 ALA B 282
REMARK 465 LEU B 283
REMARK 465 ASN B 284
REMARK 465 LEU B 285
REMARK 465 LYS B 286
REMARK 465 ASP B 287
REMARK 465 LEU B 288
REMARK 465 LYS B 289
REMARK 465 ASN B 290
REMARK 465 ILE B 291
REMARK 465 PRO B 292
REMARK 465 GLY B 293
REMARK 465 ILE B 294
REMARK 465 GLY B 295
REMARK 465 GLU B 296
REMARK 465 ARG B 297
REMARK 465 SER B 298
REMARK 465 LEU B 299
REMARK 465 GLU B 300
REMARK 465 GLU B 301
REMARK 465 ILE B 302
REMARK 465 LYS B 303
REMARK 465 GLU B 304
REMARK 465 ALA B 305
REMARK 465 LEU B 306
REMARK 465 GLU B 307
REMARK 465 LYS B 308
REMARK 465 LYS B 309
REMARK 465 GLY B 310
REMARK 465 PHE B 311
REMARK 465 THR B 312
REMARK 465 LEU B 313
REMARK 465 LYS B 314
REMARK 465 GLU B 315
REMARK 465 GLU C 57
REMARK 465 ASP C 58
REMARK 465 LYS C 59
REMARK 465 GLY C 60
REMARK 465 LYS C 61
REMARK 465 GLY C 62
REMARK 465 ARG C 1119
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 MET D 1238
REMARK 465 ARG D 1239
REMARK 465 THR D 1240
REMARK 465 PHE D 1241
REMARK 465 HIS D 1242
REMARK 465 THR D 1243
REMARK 465 GLY D 1244
REMARK 465 GLY D 1245
REMARK 465 VAL D 1246
REMARK 465 ALA D 1247
REMARK 465 GLY D 1248
REMARK 465 ALA D 1249
REMARK 465 ALA D 1250
REMARK 465 ASP D 1251
REMARK 465 VAL D 1503
REMARK 465 GLU D 1504
REMARK 465 ALA D 1505
REMARK 465 LYS D 1506
REMARK 465 GLU D 1507
REMARK 465 ARG D 1508
REMARK 465 PRO D 1509
REMARK 465 ALA D 1510
REMARK 465 ALA D 1511
REMARK 465 ARG D 1512
REMARK 465 ARG D 1513
REMARK 465 GLY D 1514
REMARK 465 VAL D 1515
REMARK 465 LYS D 1516
REMARK 465 ARG D 1517
REMARK 465 GLU D 1518
REMARK 465 GLN D 1519
REMARK 465 PRO D 1520
REMARK 465 GLY D 1521
REMARK 465 LYS D 1522
REMARK 465 GLN D 1523
REMARK 465 ALA D 1524
REMARK 465 MET E 1
REMARK 465 GLU E 96
REMARK 465 ARG E 97
REMARK 465 GLU E 98
REMARK 465 GLU E 99
REMARK 465 MET F -19
REMARK 465 GLY F -18
REMARK 465 SER F -17
REMARK 465 SER F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 HIS F -10
REMARK 465 SER F -9
REMARK 465 SER F -8
REMARK 465 GLY F -7
REMARK 465 LEU F -6
REMARK 465 VAL F -5
REMARK 465 PRO F -4
REMARK 465 ARG F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 LYS F 3
REMARK 465 SER F 4
REMARK 465 LYS F 5
REMARK 465 ARG F 6
REMARK 465 LYS F 7
REMARK 465 ASN F 8
REMARK 465 ALA F 9
REMARK 465 GLN F 10
REMARK 465 ALA F 11
REMARK 465 GLN F 12
REMARK 465 GLU F 13
REMARK 465 ALA F 14
REMARK 465 GLN F 15
REMARK 465 GLU F 16
REMARK 465 THR F 17
REMARK 465 GLU F 18
REMARK 465 VAL F 19
REMARK 465 LEU F 20
REMARK 465 VAL F 21
REMARK 465 GLN F 22
REMARK 465 GLU F 23
REMARK 465 GLU F 24
REMARK 465 ALA F 25
REMARK 465 GLU F 26
REMARK 465 GLU F 27
REMARK 465 LEU F 28
REMARK 465 PRO F 29
REMARK 465 GLU F 30
REMARK 465 PHE F 31
REMARK 465 PRO F 32
REMARK 465 GLU F 33
REMARK 465 GLY F 34
REMARK 465 GLU F 35
REMARK 465 PRO F 36
REMARK 465 ASP F 37
REMARK 465 PRO F 38
REMARK 465 ASP F 39
REMARK 465 LEU F 40
REMARK 465 GLU F 41
REMARK 465 ASP F 42
REMARK 465 PRO F 43
REMARK 465 ASP F 44
REMARK 465 LEU F 45
REMARK 465 THR F 46
REMARK 465 LEU F 47
REMARK 465 GLU F 48
REMARK 465 ASP F 49
REMARK 465 ASP F 50
REMARK 465 LEU F 51
REMARK 465 LEU F 52
REMARK 465 ASP F 53
REMARK 465 LEU F 54
REMARK 465 PRO F 55
REMARK 465 GLU F 56
REMARK 465 GLU F 57
REMARK 465 GLY F 58
REMARK 465 GLU F 59
REMARK 465 GLY F 60
REMARK 465 LEU F 61
REMARK 465 ASP F 62
REMARK 465 LEU F 63
REMARK 465 GLU F 64
REMARK 465 GLU F 65
REMARK 465 GLU F 66
REMARK 465 GLU F 67
REMARK 465 GLU F 68
REMARK 465 ASP F 69
REMARK 465 LEU F 70
REMARK 465 PRO F 71
REMARK 465 ILE F 72
REMARK 465 PRO F 73
REMARK 465 LYS F 74
REMARK 465 ILE F 75
REMARK 465 SER F 76
REMARK 465 THR F 77
REMARK 465 PRO F 320
REMARK 465 ILE F 321
REMARK 465 GLY F 322
REMARK 465 ASP F 323
REMARK 465 GLU F 324
REMARK 465 LYS F 325
REMARK 465 ASP F 326
REMARK 465 SER F 327
REMARK 465 PHE F 328
REMARK 465 DC G 1
REMARK 465 DC G 2
REMARK 465 DT G 3
REMARK 465 DA H 25
REMARK 465 DG H 26
REMARK 465 DG H 27
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 VAL E 95 CB CG1 CG2
REMARK 470 DG G 4 P OP1 OP2
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 O ALA D 918 N GLY D 923 1.80
REMARK 500 O ASP B 74 O HOH B 2101 2.02
REMARK 500 OD1 ASP D 739 OD1 ASP D 741 2.06
REMARK 500 O PHE D 1071 OG SER D 1074 2.13
REMARK 500 N SER D 449 O HOH D 2101 2.13
REMARK 500 OH TYR D 128 OD2 ASP D 579 2.14
REMARK 500 O GLN C 884 OG1 THR C 888 2.15
REMARK 500 N ILE B 78 O HOH B 2101 2.15
REMARK 500 OG1 THR C 768 OE1 GLU C 771 2.16
REMARK 500 O TYR D 432 O HOH D 2101 2.16
REMARK 500 OD1 ASP C 223 OG SER C 225 2.16
REMARK 500 OD1 ASP D 741 OD1 ASP D 743 2.16
REMARK 500 OH TYR C 615 OH TYR C 623 2.17
REMARK 500 O GLN D 1184 O HOH D 2102 2.17
REMARK 500 OG1 THR B 51 O VAL B 87 2.19
REMARK 500 OG SER D 1190 OE1 GLU D 1369 2.19
REMARK 500 N2 DG G 12 O2 DC H 16 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN D 917 C GLN D 917 O 0.115
REMARK 500 ARG D 921 C ARG D 921 O 0.173
REMARK 500 GLY D 923 CA GLY D 923 C -0.121
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 MET D 924 C - N - CA ANGL. DEV. = -15.0 DEGREES
REMARK 500 GLU D 925 C - N - CA ANGL. DEV. = -18.5 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 46 -67.24 -101.38
REMARK 500 ALA B 8 174.43 72.39
REMARK 500 SER B 46 -63.34 -127.00
REMARK 500 ILE B 129 -63.00 -96.84
REMARK 500 LYS B 155 -62.82 -93.19
REMARK 500 SER B 226 -68.00 -139.72
REMARK 500 LEU C 69 -70.11 -98.51
REMARK 500 GLU C 216 -7.99 68.07
REMARK 500 GLU C 301 -64.20 -128.69
REMARK 500 GLU C 421 -15.08 73.88
REMARK 500 VAL C 441 -62.69 -95.08
REMARK 500 THR C 443 153.26 175.93
REMARK 500 ASN C 609 -62.84 -103.21
REMARK 500 MET C 677 145.52 179.83
REMARK 500 ASP C 686 -3.66 71.10
REMARK 500 PHE C 906 -15.49 68.85
REMARK 500 TYR C 925 -73.60 -49.12
REMARK 500 THR C 979 -61.90 -98.94
REMARK 500 SER C1009 -70.85 -89.33
REMARK 500 THR C1054 -75.41 -123.91
REMARK 500 SER C1057 -82.53 -124.38
REMARK 500 THR D 31 -75.46 -109.44
REMARK 500 ILE D 49 -64.09 -90.78
REMARK 500 GLU D 275 -137.27 53.62
REMARK 500 ILE D 367 -65.20 -99.92
REMARK 500 LEU D 421 -67.61 -104.26
REMARK 500 GLU D 515 -64.64 -101.93
REMARK 500 PRO D 563 -179.14 -62.21
REMARK 500 LEU D 751 -62.07 -95.16
REMARK 500 SER D 774 -60.31 -108.60
REMARK 500 LEU D 778 -60.28 -93.09
REMARK 500 ARG D 783 -118.97 50.67
REMARK 500 ALA D 807 -67.90 -94.22
REMARK 500 ALA D 830 -134.97 55.00
REMARK 500 LEU D 920 -70.74 -50.52
REMARK 500 ARG D 921 -70.89 -96.73
REMARK 500 LYS D 926 -8.97 -56.89
REMARK 500 LEU D1144 -58.85 -122.82
REMARK 500 TYR D1198 -2.01 68.08
REMARK 500 PRO D1232 49.19 -87.29
REMARK 500 ALA D1338 -71.61 -85.86
REMARK 500 GLN D1441 174.82 176.56
REMARK 500 VAL E 80 140.17 -176.69
REMARK 500 GLN F 254 -59.12 -120.85
REMARK 500 ILE F 376 -74.01 -106.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU D 922 GLY D 923 128.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 183 OD1
REMARK 620 2 ASP B 191 O 107.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2105 O
REMARK 620 2 HOH B2110 O 165.2
REMARK 620 3 LYS D 840 O 113.5 73.4
REMARK 620 4 HOH D2117 O 79.4 92.6 65.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1603 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 58 SG
REMARK 620 2 CYS D 60 SG 103.1
REMARK 620 3 CYS D 73 SG 152.9 103.7
REMARK 620 4 CYS D 76 SG 107.3 71.0 77.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 739 OD1
REMARK 620 2 ASP D 741 OD1 60.3
REMARK 620 3 ASP D 741 OD2 69.2 54.2
REMARK 620 4 ASP D 743 OD1 79.4 63.1 117.3
REMARK 620 5 ASP D 743 OD2 75.5 104.7 144.6 50.5
REMARK 620 6 HOH D2104 O 98.2 110.3 56.2 173.4 135.1
REMARK 620 7 HOH D2105 O 79.5 138.8 121.4 103.1 52.7 82.4
REMARK 620 8 A I 7 O3' 137.4 133.6 153.2 77.7 62.2 107.8 71.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1112 SG
REMARK 620 2 CYS D1194 SG 119.1
REMARK 620 3 CYS D1201 SG 112.8 89.1
REMARK 620 4 CYS D1204 SG 132.4 98.4 94.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA F 292 O
REMARK 620 2 GLY F 296 O 91.6
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 MG B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E18 RELATED DB: PDB
DBREF 5E17 A 1 315 UNP Q9Z9H6 RPOA_THETH 1 315
DBREF 5E17 B 1 315 UNP Q9Z9H6 RPOA_THETH 1 315
DBREF 5E17 C 1 1119 UNP Q8RQE9 RPOB_THET8 1 1119
DBREF 5E17 D 1 1524 UNP Q8RQE8 RPOC_THET8 1 1524
DBREF 5E17 E 1 99 UNP Q8RQE7 RPOZ_THET8 1 99
DBREF 5E17 F 1 423 UNP Q5SKW1 Q5SKW1_THET8 1 423
DBREF 5E17 G 1 21 PDB 5E17 5E17 1 21
DBREF 5E17 H 1 27 PDB 5E17 5E17 1 27
DBREF 5E17 I 1 7 PDB 5E17 5E17 1 7
SEQADV 5E17 MET F -19 UNP Q5SKW1 INITIATING METHIONINE
SEQADV 5E17 GLY F -18 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 SER F -17 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 SER F -16 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 HIS F -15 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 HIS F -14 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 HIS F -13 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 HIS F -12 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 HIS F -11 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 HIS F -10 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 SER F -9 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 SER F -8 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 GLY F -7 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 LEU F -6 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 VAL F -5 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 PRO F -4 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 ARG F -3 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 GLY F -2 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 SER F -1 UNP Q5SKW1 EXPRESSION TAG
SEQADV 5E17 HIS F 0 UNP Q5SKW1 EXPRESSION TAG
SEQRES 1 A 315 MET LEU ASP SER LYS LEU LYS ALA PRO VAL PHE THR VAL
SEQRES 2 A 315 ARG THR GLN GLY ARG GLU TYR GLY GLU PHE VAL LEU GLU
SEQRES 3 A 315 PRO LEU GLU ARG GLY PHE GLY VAL THR LEU GLY ASN PRO
SEQRES 4 A 315 LEU ARG ARG ILE LEU LEU SER SER ILE PRO GLY THR ALA
SEQRES 5 A 315 VAL THR SER VAL TYR ILE GLU ASP VAL LEU HIS GLU PHE
SEQRES 6 A 315 SER THR ILE PRO GLY VAL LYS GLU ASP VAL VAL GLU ILE
SEQRES 7 A 315 ILE LEU ASN LEU LYS GLU LEU VAL VAL ARG PHE LEU ASN
SEQRES 8 A 315 PRO SER LEU GLN THR VAL THR LEU LEU LEU LYS ALA GLU
SEQRES 9 A 315 GLY PRO LYS GLU VAL LYS ALA ARG ASP PHE LEU PRO VAL
SEQRES 10 A 315 ALA ASP VAL GLU ILE MET ASN PRO ASP LEU HIS ILE ALA
SEQRES 11 A 315 THR LEU GLU GLU GLY GLY ARG LEU ASN MET GLU VAL ARG
SEQRES 12 A 315 VAL ASP ARG GLY VAL GLY TYR VAL PRO ALA GLU LYS HIS
SEQRES 13 A 315 GLY ILE LYS ASP ARG ILE ASN ALA ILE PRO VAL ASP ALA
SEQRES 14 A 315 VAL PHE SER PRO VAL ARG ARG VAL ALA PHE GLN VAL GLU
SEQRES 15 A 315 ASP THR ARG LEU GLY GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 16 A 315 THR LEU ARG ILE TRP THR ASP GLY SER VAL THR PRO LEU
SEQRES 17 A 315 GLU ALA LEU ASN GLN ALA VAL GLU ILE LEU ARG GLU HIS
SEQRES 18 A 315 LEU THR TYR PHE SER ASN PRO GLN ALA ALA ALA VAL ALA
SEQRES 19 A 315 ALA PRO GLU GLU ALA LYS GLU PRO GLU ALA PRO PRO GLU
SEQRES 20 A 315 GLN GLU GLU GLU LEU ASP LEU PRO LEU GLU GLU LEU GLY
SEQRES 21 A 315 LEU SER THR ARG VAL LEU HIS SER LEU LYS GLU GLU GLY
SEQRES 22 A 315 ILE GLU SER VAL ARG ALA LEU LEU ALA LEU ASN LEU LYS
SEQRES 23 A 315 ASP LEU LYS ASN ILE PRO GLY ILE GLY GLU ARG SER LEU
SEQRES 24 A 315 GLU GLU ILE LYS GLU ALA LEU GLU LYS LYS GLY PHE THR
SEQRES 25 A 315 LEU LYS GLU
SEQRES 1 B 315 MET LEU ASP SER LYS LEU LYS ALA PRO VAL PHE THR VAL
SEQRES 2 B 315 ARG THR GLN GLY ARG GLU TYR GLY GLU PHE VAL LEU GLU
SEQRES 3 B 315 PRO LEU GLU ARG GLY PHE GLY VAL THR LEU GLY ASN PRO
SEQRES 4 B 315 LEU ARG ARG ILE LEU LEU SER SER ILE PRO GLY THR ALA
SEQRES 5 B 315 VAL THR SER VAL TYR ILE GLU ASP VAL LEU HIS GLU PHE
SEQRES 6 B 315 SER THR ILE PRO GLY VAL LYS GLU ASP VAL VAL GLU ILE
SEQRES 7 B 315 ILE LEU ASN LEU LYS GLU LEU VAL VAL ARG PHE LEU ASN
SEQRES 8 B 315 PRO SER LEU GLN THR VAL THR LEU LEU LEU LYS ALA GLU
SEQRES 9 B 315 GLY PRO LYS GLU VAL LYS ALA ARG ASP PHE LEU PRO VAL
SEQRES 10 B 315 ALA ASP VAL GLU ILE MET ASN PRO ASP LEU HIS ILE ALA
SEQRES 11 B 315 THR LEU GLU GLU GLY GLY ARG LEU ASN MET GLU VAL ARG
SEQRES 12 B 315 VAL ASP ARG GLY VAL GLY TYR VAL PRO ALA GLU LYS HIS
SEQRES 13 B 315 GLY ILE LYS ASP ARG ILE ASN ALA ILE PRO VAL ASP ALA
SEQRES 14 B 315 VAL PHE SER PRO VAL ARG ARG VAL ALA PHE GLN VAL GLU
SEQRES 15 B 315 ASP THR ARG LEU GLY GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 16 B 315 THR LEU ARG ILE TRP THR ASP GLY SER VAL THR PRO LEU
SEQRES 17 B 315 GLU ALA LEU ASN GLN ALA VAL GLU ILE LEU ARG GLU HIS
SEQRES 18 B 315 LEU THR TYR PHE SER ASN PRO GLN ALA ALA ALA VAL ALA
SEQRES 19 B 315 ALA PRO GLU GLU ALA LYS GLU PRO GLU ALA PRO PRO GLU
SEQRES 20 B 315 GLN GLU GLU GLU LEU ASP LEU PRO LEU GLU GLU LEU GLY
SEQRES 21 B 315 LEU SER THR ARG VAL LEU HIS SER LEU LYS GLU GLU GLY
SEQRES 22 B 315 ILE GLU SER VAL ARG ALA LEU LEU ALA LEU ASN LEU LYS
SEQRES 23 B 315 ASP LEU LYS ASN ILE PRO GLY ILE GLY GLU ARG SER LEU
SEQRES 24 B 315 GLU GLU ILE LYS GLU ALA LEU GLU LYS LYS GLY PHE THR
SEQRES 25 B 315 LEU LYS GLU
SEQRES 1 C 1119 MET GLU ILE LYS ARG PHE GLY ARG ILE ARG GLU VAL ILE
SEQRES 2 C 1119 PRO LEU PRO PRO LEU THR GLU ILE GLN VAL GLU SER TYR
SEQRES 3 C 1119 ARG ARG ALA LEU GLN ALA ASP VAL PRO PRO GLU LYS ARG
SEQRES 4 C 1119 GLU ASN VAL GLY ILE GLN ALA ALA PHE ARG GLU THR PHE
SEQRES 5 C 1119 PRO ILE GLU GLU GLU ASP LYS GLY LYS GLY GLY LEU VAL
SEQRES 6 C 1119 LEU ASP PHE LEU GLU TYR ARG LEU GLY GLU PRO PRO PHE
SEQRES 7 C 1119 PRO GLN ASP GLU CYS ARG GLU LYS ASP LEU THR TYR GLN
SEQRES 8 C 1119 ALA PRO LEU TYR ALA ARG LEU GLN LEU ILE HIS LYS ASP
SEQRES 9 C 1119 THR GLY LEU ILE LYS GLU ASP GLU VAL PHE LEU GLY HIS
SEQRES 10 C 1119 ILE PRO LEU MET THR GLU ASP GLY SER PHE ILE ILE ASN
SEQRES 11 C 1119 GLY ALA ASP ARG VAL ILE VAL SER GLN ILE HIS ARG SER
SEQRES 12 C 1119 PRO GLY VAL TYR PHE THR PRO ASP PRO ALA ARG PRO GLY
SEQRES 13 C 1119 ARG TYR ILE ALA SER ILE ILE PRO LEU PRO LYS ARG GLY
SEQRES 14 C 1119 PRO TRP ILE ASP LEU GLU VAL GLU PRO ASN GLY VAL VAL
SEQRES 15 C 1119 SER MET LYS VAL ASN LYS ARG LYS PHE PRO LEU VAL LEU
SEQRES 16 C 1119 LEU LEU ARG VAL LEU GLY TYR ASP GLN GLU THR LEU ALA
SEQRES 17 C 1119 ARG GLU LEU GLY ALA TYR GLY GLU LEU VAL GLN GLY LEU
SEQRES 18 C 1119 MET ASP GLU SER VAL PHE ALA MET ARG PRO GLU GLU ALA
SEQRES 19 C 1119 LEU ILE ARG LEU PHE THR LEU LEU ARG PRO GLY ASP PRO
SEQRES 20 C 1119 PRO LYS ARG ASP LYS ALA VAL ALA TYR VAL TYR GLY LEU
SEQRES 21 C 1119 ILE ALA ASP PRO ARG ARG TYR ASP LEU GLY GLU ALA GLY
SEQRES 22 C 1119 ARG TYR LYS ALA GLU GLU LYS LEU GLY ILE ARG LEU SER
SEQRES 23 C 1119 GLY ARG THR LEU ALA ARG PHE GLU ASP GLY GLU PHE LYS
SEQRES 24 C 1119 ASP GLU VAL PHE LEU PRO THR LEU ARG TYR LEU PHE ALA
SEQRES 25 C 1119 LEU THR ALA GLY VAL PRO GLY HIS GLU VAL ASP ASP ILE
SEQRES 26 C 1119 ASP HIS LEU GLY ASN ARG ARG ILE ARG THR VAL GLY GLU
SEQRES 27 C 1119 LEU MET THR ASP GLN PHE ARG VAL GLY LEU ALA ARG LEU
SEQRES 28 C 1119 ALA ARG GLY VAL ARG GLU ARG MET LEU MET GLY SER GLU
SEQRES 29 C 1119 ASP SER LEU THR PRO ALA LYS LEU VAL ASN SER ARG PRO
SEQRES 30 C 1119 LEU GLU ALA ALA ILE ARG GLU PHE PHE SER ARG SER GLN
SEQRES 31 C 1119 LEU SER GLN PHE LYS ASP GLU THR ASN PRO LEU SER SER
SEQRES 32 C 1119 LEU ARG HIS LYS ARG ARG ILE SER ALA LEU GLY PRO GLY
SEQRES 33 C 1119 GLY LEU THR ARG GLU ARG ALA GLY PHE ASP VAL ARG ASP
SEQRES 34 C 1119 VAL HIS ARG THR HIS TYR GLY ARG ILE CYS PRO VAL GLU
SEQRES 35 C 1119 THR PRO GLU GLY ALA ASN ILE GLY LEU ILE THR SER LEU
SEQRES 36 C 1119 ALA ALA TYR ALA ARG VAL ASP GLU LEU GLY PHE ILE ARG
SEQRES 37 C 1119 THR PRO TYR ARG ARG VAL VAL GLY GLY VAL VAL THR ASP
SEQRES 38 C 1119 GLU VAL VAL TYR MET THR ALA THR GLU GLU ASP ARG TYR
SEQRES 39 C 1119 THR ILE ALA GLN ALA ASN THR PRO LEU GLU GLY ASN ARG
SEQRES 40 C 1119 ILE ALA ALA GLU ARG VAL VAL ALA ARG ARG LYS GLY GLU
SEQRES 41 C 1119 PRO VAL ILE VAL SER PRO GLU GLU VAL GLU PHE MET ASP
SEQRES 42 C 1119 VAL SER PRO LYS GLN VAL PHE SER VAL ASN THR ASN LEU
SEQRES 43 C 1119 ILE PRO PHE LEU GLU HIS ASP ASP ALA ASN ARG ALA LEU
SEQRES 44 C 1119 MET GLY SER ASN MET GLN THR GLN ALA VAL PRO LEU ILE
SEQRES 45 C 1119 ARG ALA GLN ALA PRO VAL VAL MET THR GLY LEU GLU GLU
SEQRES 46 C 1119 ARG VAL VAL ARG ASP SER LEU ALA ALA LEU TYR ALA GLU
SEQRES 47 C 1119 GLU ASP GLY GLU VAL ALA LYS VAL ASP GLY ASN ARG ILE
SEQRES 48 C 1119 VAL VAL ARG TYR GLU ASP GLY ARG LEU VAL GLU TYR PRO
SEQRES 49 C 1119 LEU ARG ARG PHE TYR ARG SER ASN GLN GLY THR ALA LEU
SEQRES 50 C 1119 ASP GLN ARG PRO ARG VAL VAL VAL GLY GLN ARG VAL ARG
SEQRES 51 C 1119 LYS GLY ASP LEU LEU ALA ASP GLY PRO ALA SER GLU ASN
SEQRES 52 C 1119 GLY PHE LEU ALA LEU GLY GLN ASN VAL LEU VAL ALA ILE
SEQRES 53 C 1119 MET PRO PHE ASP GLY TYR ASN PHE GLU ASP ALA ILE VAL
SEQRES 54 C 1119 ILE SER GLU GLU LEU LEU LYS ARG ASP PHE TYR THR SER
SEQRES 55 C 1119 ILE HIS ILE GLU ARG TYR GLU ILE GLU ALA ARG ASP THR
SEQRES 56 C 1119 LYS LEU GLY PRO GLU ARG ILE THR ARG ASP ILE PRO HIS
SEQRES 57 C 1119 LEU SER GLU ALA ALA LEU ARG ASP LEU ASP GLU GLU GLY
SEQRES 58 C 1119 VAL VAL ARG ILE GLY ALA GLU VAL LYS PRO GLY ASP ILE
SEQRES 59 C 1119 LEU VAL GLY ARG THR SER PHE LYS GLY GLU SER GLU PRO
SEQRES 60 C 1119 THR PRO GLU GLU ARG LEU LEU ARG SER ILE PHE GLY GLU
SEQRES 61 C 1119 LYS ALA ARG ASP VAL LYS ASP THR SER LEU ARG VAL PRO
SEQRES 62 C 1119 PRO GLY GLU GLY GLY ILE VAL VAL ARG THR VAL ARG LEU
SEQRES 63 C 1119 ARG ARG GLY ASP PRO GLY VAL GLU LEU LYS PRO GLY VAL
SEQRES 64 C 1119 ARG GLU VAL VAL ARG VAL TYR VAL ALA GLN LYS ARG LYS
SEQRES 65 C 1119 LEU GLN VAL GLY ASP LYS LEU ALA ASN ARG HIS GLY ASN
SEQRES 66 C 1119 LYS GLY VAL VAL ALA LYS ILE LEU PRO VAL GLU ASP MET
SEQRES 67 C 1119 PRO HIS LEU PRO ASP GLY THR PRO VAL ASP VAL ILE LEU
SEQRES 68 C 1119 ASN PRO LEU GLY VAL PRO SER ARG MET ASN LEU GLY GLN
SEQRES 69 C 1119 ILE LEU GLU THR HIS LEU GLY LEU ALA GLY TYR PHE LEU
SEQRES 70 C 1119 GLY GLN ARG TYR ILE SER PRO ILE PHE ASP GLY ALA LYS
SEQRES 71 C 1119 GLU PRO GLU ILE LYS GLU LEU LEU ALA GLN ALA PHE GLU
SEQRES 72 C 1119 VAL TYR PHE GLY LYS ARG LYS GLY GLU GLY PHE GLY VAL
SEQRES 73 C 1119 ASP LYS ARG GLU VAL GLU VAL LEU ARG ARG ALA GLU LYS
SEQRES 74 C 1119 LEU GLY LEU VAL THR PRO GLY LYS THR PRO GLU GLU GLN
SEQRES 75 C 1119 LEU LYS GLU LEU PHE LEU GLN GLY LYS VAL VAL LEU TYR
SEQRES 76 C 1119 ASP GLY ARG THR GLY GLU PRO ILE GLU GLY PRO ILE VAL
SEQRES 77 C 1119 VAL GLY GLN MET PHE ILE MET LYS LEU TYR HIS MET VAL
SEQRES 78 C 1119 GLU ASP LYS MET HIS ALA ARG SER THR GLY PRO TYR SER
SEQRES 79 C 1119 LEU ILE THR GLN GLN PRO LEU GLY GLY LYS ALA GLN PHE
SEQRES 80 C 1119 GLY GLY GLN ARG PHE GLY GLU MET GLU VAL TRP ALA LEU
SEQRES 81 C 1119 GLU ALA TYR GLY ALA ALA HIS THR LEU GLN GLU MET LEU
SEQRES 82 C 1119 THR LEU LYS SER ASP ASP ILE GLU GLY ARG ASN ALA ALA
SEQRES 83 C 1119 TYR GLU ALA ILE ILE LYS GLY GLU ASP VAL PRO GLU PRO
SEQRES 84 C 1119 SER VAL PRO GLU SER PHE ARG VAL LEU VAL LYS GLU LEU
SEQRES 85 C 1119 GLN ALA LEU ALA LEU ASP VAL GLN THR LEU ASP GLU LYS
SEQRES 86 C 1119 ASP ASN PRO VAL ASP ILE PHE GLU GLY LEU ALA SER LYS
SEQRES 87 C 1119 ARG
SEQRES 1 D 1524 MET LYS LYS GLU VAL ARG LYS VAL ARG ILE ALA LEU ALA
SEQRES 2 D 1524 SER PRO GLU LYS ILE ARG SER TRP SER TYR GLY GLU VAL
SEQRES 3 D 1524 GLU LYS PRO GLU THR ILE ASN TYR ARG THR LEU LYS PRO
SEQRES 4 D 1524 GLU ARG ASP GLY LEU PHE ASP GLU ARG ILE PHE GLY PRO
SEQRES 5 D 1524 ILE LYS ASP TYR GLU CYS ALA CYS GLY LYS TYR LYS ARG
SEQRES 6 D 1524 GLN ARG PHE GLU GLY LYS VAL CYS GLU ARG CYS GLY VAL
SEQRES 7 D 1524 GLU VAL THR LYS SER ILE VAL ARG ARG TYR ARG MET GLY
SEQRES 8 D 1524 HIS ILE GLU LEU ALA THR PRO ALA ALA HIS ILE TRP PHE
SEQRES 9 D 1524 VAL LYS ASP VAL PRO SER LYS ILE GLY THR LEU LEU ASP
SEQRES 10 D 1524 LEU SER ALA THR GLU LEU GLU GLN VAL LEU TYR PHE SER
SEQRES 11 D 1524 LYS TYR ILE VAL LEU ASP PRO LYS GLY ALA ILE LEU ASN
SEQRES 12 D 1524 GLY VAL PRO VAL GLU LYS ARG GLN LEU LEU THR ASP GLU
SEQRES 13 D 1524 GLU TYR ARG GLU LEU ARG TYR GLY LYS GLN GLU THR TYR
SEQRES 14 D 1524 PRO LEU PRO PRO GLY VAL ASP ALA LEU VAL LYS ASP GLY
SEQRES 15 D 1524 GLU GLU VAL VAL LYS GLY GLN GLU LEU ALA PRO GLY VAL
SEQRES 16 D 1524 VAL SER ARG LEU ASP GLY VAL ALA LEU TYR ARG PHE PRO
SEQRES 17 D 1524 ARG ARG VAL ARG VAL GLU TYR VAL LYS LYS GLU ARG ALA
SEQRES 18 D 1524 GLY LEU ARG LEU PRO LEU ALA ALA TRP VAL GLU LYS GLU
SEQRES 19 D 1524 ALA TYR LYS PRO GLY GLU ILE LEU ALA GLU LEU PRO GLU
SEQRES 20 D 1524 PRO TYR LEU PHE ARG ALA GLU GLU GLU GLY VAL VAL GLU
SEQRES 21 D 1524 LEU LYS GLU LEU GLU GLU GLY ALA PHE LEU VAL LEU ARG
SEQRES 22 D 1524 ARG GLU ASP GLU PRO VAL ALA THR TYR PHE LEU PRO VAL
SEQRES 23 D 1524 GLY MET THR PRO LEU VAL VAL HIS GLY GLU ILE VAL GLU
SEQRES 24 D 1524 LYS GLY GLN PRO LEU ALA GLU ALA LYS GLY LEU LEU ARG
SEQRES 25 D 1524 MET PRO ARG GLN VAL ARG ALA ALA GLN VAL GLU ALA GLU
SEQRES 26 D 1524 GLU GLU GLY GLU THR VAL TYR LEU THR LEU PHE LEU GLU
SEQRES 27 D 1524 TRP THR GLU PRO LYS ASP TYR ARG VAL GLN PRO HIS MET
SEQRES 28 D 1524 ASN VAL VAL VAL PRO GLU GLY ALA ARG VAL GLU ALA GLY
SEQRES 29 D 1524 ASP LYS ILE VAL ALA ALA ILE ASP PRO GLU GLU GLU VAL
SEQRES 30 D 1524 ILE ALA GLU ALA GLU GLY VAL VAL HIS LEU HIS GLU PRO
SEQRES 31 D 1524 ALA SER ILE LEU VAL VAL LYS ALA ARG VAL TYR PRO PHE
SEQRES 32 D 1524 GLU ASP ASP VAL GLU VAL SER THR GLY ASP ARG VAL ALA
SEQRES 33 D 1524 PRO GLY ASP VAL LEU ALA ASP GLY GLY LYS VAL LYS SER
SEQRES 34 D 1524 ASP VAL TYR GLY ARG VAL GLU VAL ASP LEU VAL ARG ASN
SEQRES 35 D 1524 VAL VAL ARG VAL VAL GLU SER TYR ASP ILE ASP ALA ARG
SEQRES 36 D 1524 MET GLY ALA GLU ALA ILE GLN GLN LEU LEU LYS GLU LEU
SEQRES 37 D 1524 ASP LEU GLU ALA LEU GLU LYS GLU LEU LEU GLU GLU MET
SEQRES 38 D 1524 LYS HIS PRO SER ARG ALA ARG ARG ALA LYS ALA ARG LYS
SEQRES 39 D 1524 ARG LEU GLU VAL VAL ARG ALA PHE LEU ASP SER GLY ASN
SEQRES 40 D 1524 ARG PRO GLU TRP MET ILE LEU GLU ALA VAL PRO VAL LEU
SEQRES 41 D 1524 PRO PRO ASP LEU ARG PRO MET VAL GLN VAL ASP GLY GLY
SEQRES 42 D 1524 ARG PHE ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG
SEQRES 43 D 1524 LEU ILE ASN ARG ASN ASN ARG LEU LYS LYS LEU LEU ALA
SEQRES 44 D 1524 GLN GLY ALA PRO GLU ILE ILE ILE ARG ASN GLU LYS ARG
SEQRES 45 D 1524 MET LEU GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY
SEQRES 46 D 1524 ARG ARG GLY ALA PRO VAL THR ASN PRO GLY SER ASP ARG
SEQRES 47 D 1524 PRO LEU ARG SER LEU THR ASP ILE LEU SER GLY LYS GLN
SEQRES 48 D 1524 GLY ARG PHE ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP
SEQRES 49 D 1524 TYR SER GLY ARG SER VAL ILE VAL VAL GLY PRO GLN LEU
SEQRES 50 D 1524 LYS LEU HIS GLN CYS GLY LEU PRO LYS ARG MET ALA LEU
SEQRES 51 D 1524 GLU LEU PHE LYS PRO PHE LEU LEU LYS LYS MET GLU GLU
SEQRES 52 D 1524 LYS GLY ILE ALA PRO ASN VAL LYS ALA ALA ARG ARG MET
SEQRES 53 D 1524 LEU GLU ARG GLN ARG ASP ILE LYS ASP GLU VAL TRP ASP
SEQRES 54 D 1524 ALA LEU GLU GLU VAL ILE HIS GLY LYS VAL VAL LEU LEU
SEQRES 55 D 1524 ASN ARG ALA PRO THR LEU HIS ARG LEU GLY ILE GLN ALA
SEQRES 56 D 1524 PHE GLN PRO VAL LEU VAL GLU GLY GLN SER ILE GLN LEU
SEQRES 57 D 1524 HIS PRO LEU VAL CYS GLU ALA PHE ASN ALA ASP PHE ASP
SEQRES 58 D 1524 GLY ASP GLN MET ALA VAL HIS VAL PRO LEU SER SER PHE
SEQRES 59 D 1524 ALA GLN ALA GLU ALA ARG ILE GLN MET LEU SER ALA HIS
SEQRES 60 D 1524 ASN LEU LEU SER PRO ALA SER GLY GLU PRO LEU ALA LYS
SEQRES 61 D 1524 PRO SER ARG ASP ILE ILE LEU GLY LEU TYR TYR ILE THR
SEQRES 62 D 1524 GLN VAL ARG LYS GLU LYS LYS GLY ALA GLY LEU GLU PHE
SEQRES 63 D 1524 ALA THR PRO GLU GLU ALA LEU ALA ALA HIS GLU ARG GLY
SEQRES 64 D 1524 GLU VAL ALA LEU ASN ALA PRO ILE LYS VAL ALA GLY ARG
SEQRES 65 D 1524 GLU THR SER VAL GLY ARG LEU LYS TYR VAL PHE ALA ASN
SEQRES 66 D 1524 PRO ASP GLU ALA LEU LEU ALA VAL ALA HIS GLY ILE VAL
SEQRES 67 D 1524 ASP LEU GLN ASP VAL VAL THR VAL ARG TYR MET GLY LYS
SEQRES 68 D 1524 ARG LEU GLU THR SER PRO GLY ARG ILE LEU PHE ALA ARG
SEQRES 69 D 1524 ILE VAL ALA GLU ALA VAL GLU ASP GLU LYS VAL ALA TRP
SEQRES 70 D 1524 GLU LEU ILE GLN LEU ASP VAL PRO GLN GLU LYS ASN SER
SEQRES 71 D 1524 LEU LYS ASP LEU VAL TYR GLN ALA PHE LEU ARG LEU GLY
SEQRES 72 D 1524 MET GLU LYS THR ALA ARG LEU LEU ASP ALA LEU LYS TYR
SEQRES 73 D 1524 TYR GLY PHE THR PHE SER THR THR SER GLY ILE THR ILE
SEQRES 74 D 1524 GLY ILE ASP ASP ALA VAL ILE PRO GLU GLU LYS LYS GLN
SEQRES 75 D 1524 TYR LEU GLU GLU ALA ASP ARG LYS LEU LEU GLN ILE GLU
SEQRES 76 D 1524 GLN ALA TYR GLU MET GLY PHE LEU THR ASP ARG GLU ARG
SEQRES 77 D 1524 TYR ASP GLN ILE LEU GLN LEU TRP THR GLU THR THR GLU
SEQRES 78 D 1524 LYS VAL THR GLN ALA VAL PHE LYS ASN PHE GLU GLU ASN
SEQRES 79 D 1524 TYR PRO PHE ASN PRO LEU TYR VAL MET ALA GLN SER GLY
SEQRES 80 D 1524 ALA ARG GLY ASN PRO GLN GLN ILE ARG GLN LEU CYS GLY
SEQRES 81 D 1524 LEU ARG GLY LEU MET GLN LYS PRO SER GLY GLU THR PHE
SEQRES 82 D 1524 GLU VAL PRO VAL ARG SER SER PHE ARG GLU GLY LEU THR
SEQRES 83 D 1524 VAL LEU GLU TYR PHE ILE SER SER HIS GLY ALA ARG LYS
SEQRES 84 D 1524 GLY GLY ALA ASP THR ALA LEU ARG THR ALA ASP SER GLY
SEQRES 85 D 1524 TYR LEU THR ARG LYS LEU VAL ASP VAL THR HIS GLU ILE
SEQRES 86 D 1524 VAL VAL ARG GLU ALA ASP CYS GLY THR THR ASN TYR ILE
SEQRES 87 D 1524 SER VAL PRO LEU PHE GLN PRO ASP GLU VAL THR ARG SER
SEQRES 88 D 1524 LEU ARG LEU ARG LYS ARG ALA ASP ILE GLU ALA GLY LEU
SEQRES 89 D 1524 TYR GLY ARG VAL LEU ALA ARG GLU VAL GLU VAL LEU GLY
SEQRES 90 D 1524 VAL ARG LEU GLU GLU GLY ARG TYR LEU SER MET ASP ASP
SEQRES 91 D 1524 VAL HIS LEU LEU ILE LYS ALA ALA GLU ALA GLY GLU ILE
SEQRES 92 D 1524 GLN GLU VAL PRO VAL ARG SER PRO LEU THR CYS GLN THR
SEQRES 93 D 1524 ARG TYR GLY VAL CYS GLN LYS CYS TYR GLY TYR ASP LEU
SEQRES 94 D 1524 SER MET ALA ARG PRO VAL SER ILE GLY GLU ALA VAL GLY
SEQRES 95 D 1524 ILE VAL ALA ALA GLN SER ILE GLY GLU PRO GLY THR GLN
SEQRES 96 D 1524 LEU THR MET ARG THR PHE HIS THR GLY GLY VAL ALA GLY
SEQRES 97 D 1524 ALA ALA ASP ILE THR GLN GLY LEU PRO ARG VAL ILE GLU
SEQRES 98 D 1524 LEU PHE GLU ALA ARG ARG PRO LYS ALA LYS ALA VAL ILE
SEQRES 99 D 1524 SER GLU ILE ASP GLY VAL VAL ARG ILE GLU GLU THR GLU
SEQRES 100 D 1524 GLU LYS LEU SER VAL PHE VAL GLU SER GLU GLY PHE SER
SEQRES 101 D 1524 LYS GLU TYR LYS LEU PRO LYS GLU ALA ARG LEU LEU VAL
SEQRES 102 D 1524 LYS ASP GLY ASP TYR VAL GLU ALA GLY GLN PRO LEU THR
SEQRES 103 D 1524 ARG GLY ALA ILE ASP PRO HIS GLN LEU LEU GLU ALA LYS
SEQRES 104 D 1524 GLY PRO GLU ALA VAL GLU ARG TYR LEU VAL GLU GLU ILE
SEQRES 105 D 1524 GLN LYS VAL TYR ARG ALA GLN GLY VAL LYS LEU HIS ASP
SEQRES 106 D 1524 LYS HIS ILE GLU ILE VAL VAL ARG GLN MET MET LYS TYR
SEQRES 107 D 1524 VAL GLU VAL THR ASP PRO GLY ASP SER ARG LEU LEU GLU
SEQRES 108 D 1524 GLY GLN VAL LEU GLU LYS TRP ASP VAL GLU ALA LEU ASN
SEQRES 109 D 1524 GLU ARG LEU ILE ALA GLU GLY LYS THR PRO VAL ALA TRP
SEQRES 110 D 1524 LYS PRO LEU LEU MET GLY VAL THR LYS SER ALA LEU SER
SEQRES 111 D 1524 THR LYS SER TRP LEU SER ALA ALA SER PHE GLN ASN THR
SEQRES 112 D 1524 THR HIS VAL LEU THR GLU ALA ALA ILE ALA GLY LYS LYS
SEQRES 113 D 1524 ASP GLU LEU ILE GLY LEU LYS GLU ASN VAL ILE LEU GLY
SEQRES 114 D 1524 ARG LEU ILE PRO ALA GLY THR GLY SER ASP PHE VAL ARG
SEQRES 115 D 1524 PHE THR GLN VAL VAL ASP GLN LYS THR LEU LYS ALA ILE
SEQRES 116 D 1524 GLU GLU ALA ARG LYS GLU ALA VAL GLU ALA LYS GLU ARG
SEQRES 117 D 1524 PRO ALA ALA ARG ARG GLY VAL LYS ARG GLU GLN PRO GLY
SEQRES 118 D 1524 LYS GLN ALA
SEQRES 1 E 99 MET ALA GLU PRO GLY ILE ASP LYS LEU PHE GLY MET VAL
SEQRES 2 E 99 ASP SER LYS TYR ARG LEU THR VAL VAL VAL ALA LYS ARG
SEQRES 3 E 99 ALA GLN GLN LEU LEU ARG HIS GLY PHE LYS ASN THR VAL
SEQRES 4 E 99 LEU GLU PRO GLU GLU ARG PRO LYS MET GLN THR LEU GLU
SEQRES 5 E 99 GLY LEU PHE ASP ASP PRO ASN ALA VAL THR TRP ALA MET
SEQRES 6 E 99 LYS GLU LEU LEU THR GLY ARG LEU VAL PHE GLY GLU ASN
SEQRES 7 E 99 LEU VAL PRO GLU ASP ARG LEU GLN LYS GLU MET GLU ARG
SEQRES 8 E 99 LEU TYR PRO VAL GLU ARG GLU GLU
SEQRES 1 F 443 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 443 LEU VAL PRO ARG GLY SER HIS MET LYS LYS SER LYS ARG
SEQRES 3 F 443 LYS ASN ALA GLN ALA GLN GLU ALA GLN GLU THR GLU VAL
SEQRES 4 F 443 LEU VAL GLN GLU GLU ALA GLU GLU LEU PRO GLU PHE PRO
SEQRES 5 F 443 GLU GLY GLU PRO ASP PRO ASP LEU GLU ASP PRO ASP LEU
SEQRES 6 F 443 THR LEU GLU ASP ASP LEU LEU ASP LEU PRO GLU GLU GLY
SEQRES 7 F 443 GLU GLY LEU ASP LEU GLU GLU GLU GLU GLU ASP LEU PRO
SEQRES 8 F 443 ILE PRO LYS ILE SER THR SER ASP PRO VAL ARG GLN TYR
SEQRES 9 F 443 LEU HIS GLU ILE GLY GLN VAL PRO LEU LEU THR LEU GLU
SEQRES 10 F 443 GLU GLU VAL GLU LEU ALA ARG LYS VAL GLU GLU GLY MET
SEQRES 11 F 443 GLU ALA ILE LYS LYS LEU SER GLU ILE THR GLY LEU ASP
SEQRES 12 F 443 PRO ASP LEU ILE ARG GLU VAL VAL ARG ALA LYS ILE LEU
SEQRES 13 F 443 GLY SER ALA ARG VAL ARG HIS ILE PRO GLY LEU LYS GLU
SEQRES 14 F 443 THR LEU ASP PRO LYS THR VAL GLU GLU ILE ASP GLN LYS
SEQRES 15 F 443 LEU LYS SER LEU PRO LYS GLU HIS LYS ARG TYR LEU HIS
SEQRES 16 F 443 ILE ALA ARG GLU GLY GLU ALA ALA ARG GLN HIS LEU ILE
SEQRES 17 F 443 GLU ALA ASN LEU ARG LEU VAL VAL SER ILE ALA LYS LYS
SEQRES 18 F 443 TYR THR GLY ARG GLY LEU SER PHE LEU ASP LEU ILE GLN
SEQRES 19 F 443 GLU GLY ASN GLN GLY LEU ILE ARG ALA VAL GLU LYS PHE
SEQRES 20 F 443 GLU TYR LYS ARG ARG PHE LYS PHE SER THR TYR ALA THR
SEQRES 21 F 443 TRP TRP ILE ARG GLN ALA ILE ASN ARG ALA ILE ALA ASP
SEQRES 22 F 443 GLN ALA ARG THR ILE ARG ILE PRO VAL HIS MET VAL GLU
SEQRES 23 F 443 THR ILE ASN LYS LEU SER ARG THR ALA ARG GLN LEU GLN
SEQRES 24 F 443 GLN GLU LEU GLY ARG GLU PRO THR TYR GLU GLU ILE ALA
SEQRES 25 F 443 GLU ALA MET GLY PRO GLY TRP ASP ALA LYS ARG VAL GLU
SEQRES 26 F 443 GLU THR LEU LYS ILE ALA GLN GLU PRO VAL SER LEU GLU
SEQRES 27 F 443 THR PRO ILE GLY ASP GLU LYS ASP SER PHE TYR GLY ASP
SEQRES 28 F 443 PHE ILE PRO ASP GLU HIS LEU PRO SER PRO VAL ASP ALA
SEQRES 29 F 443 ALA THR GLN SER LEU LEU SER GLU GLU LEU GLU LYS ALA
SEQRES 30 F 443 LEU SER LYS LEU SER GLU ARG GLU ALA MET VAL LEU LYS
SEQRES 31 F 443 LEU ARG LYS GLY LEU ILE ASP GLY ARG GLU HIS THR LEU
SEQRES 32 F 443 GLU GLU VAL GLY ALA PHE PHE GLY VAL THR ARG GLU ARG
SEQRES 33 F 443 ILE ARG GLN ILE GLU ASN LYS ALA LEU ARG LYS LEU LYS
SEQRES 34 F 443 TYR HIS GLU SER ARG THR ARG LYS LEU ARG ASP PHE LEU
SEQRES 35 F 443 ASP
SEQRES 1 G 21 DC DC DT DG DC DA DT DC DC DG DT DG DA
SEQRES 2 G 21 DG DT DC DG DA DG DG DG
SEQRES 1 H 27 DT DA DT DA DA DT DG DG DG DA DG DC DT
SEQRES 2 H 27 DG DT DC DA DC DG DG DA DT DG DC DA DG
SEQRES 3 H 27 DG
SEQRES 1 I 7 C C C U C G A
HET MG B2001 1
HET MG D1601 1
HET ZN D1602 1
HET ZN D1603 1
HET MG D1604 1
HET MG F2001 1
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
FORMUL 10 MG 4(MG 2+)
FORMUL 12 ZN 2(ZN 2+)
FORMUL 16 HOH *159(H2 O)
HELIX 1 AA1 GLY A 31 ILE A 48 1 18
HELIX 2 AA2 ASP A 74 GLU A 84 1 11
HELIX 3 AA3 ARG A 112 PHE A 114 5 3
HELIX 4 AA4 PRO A 152 GLY A 157 1 6
HELIX 5 AA5 THR A 206 PHE A 225 1 20
HELIX 6 AA6 GLY B 31 LEU B 45 1 15
HELIX 7 AA7 ASP B 74 GLU B 84 1 11
HELIX 8 AA8 ARG B 112 PHE B 114 5 3
HELIX 9 AA9 PRO B 152 GLY B 157 1 6
HELIX 10 AB1 THR B 206 THR B 223 1 18
HELIX 11 AB2 THR C 19 GLN C 31 1 13
HELIX 12 AB3 PRO C 35 ARG C 39 5 5
HELIX 13 AB4 GLY C 43 PHE C 52 1 10
HELIX 14 AB5 PRO C 79 LYS C 86 1 8
HELIX 15 AB6 LEU C 193 LEU C 200 1 8
HELIX 16 AB7 ASP C 203 GLY C 212 1 10
HELIX 17 AB8 LEU C 217 LEU C 221 5 5
HELIX 18 AB9 ASP C 223 ALA C 228 1 6
HELIX 19 AC1 ARG C 230 ARG C 243 1 14
HELIX 20 AC2 LYS C 249 ILE C 261 1 13
HELIX 21 AC3 GLY C 270 GLY C 282 1 13
HELIX 22 AC4 VAL C 302 GLY C 316 1 15
HELIX 23 AC5 THR C 335 MET C 361 1 27
HELIX 24 AC6 THR C 368 VAL C 373 1 6
HELIX 25 AC7 SER C 375 SER C 389 1 15
HELIX 26 AC8 ASN C 399 ARG C 408 1 10
HELIX 27 AC9 GLY C 424 ASP C 429 1 6
HELIX 28 AD1 HIS C 431 TYR C 435 5 5
HELIX 29 AD2 THR C 487 ARG C 493 1 7
HELIX 30 AD3 SER C 525 VAL C 529 5 5
HELIX 31 AD4 SER C 535 PHE C 540 5 6
HELIX 32 AD5 ASN C 543 ILE C 547 5 5
HELIX 33 AD6 PHE C 549 ASP C 553 5 5
HELIX 34 AD7 ASP C 554 GLN C 567 1 14
HELIX 35 AD8 LEU C 583 SER C 591 1 9
HELIX 36 AD9 ASN C 683 ALA C 687 5 5
HELIX 37 AE1 GLU C 692 ARG C 697 1 6
HELIX 38 AE2 SER C 730 ARG C 735 1 6
HELIX 39 AE3 THR C 768 GLY C 779 1 12
HELIX 40 AE4 PRO C 854 MET C 858 5 5
HELIX 41 AE5 LEU C 874 MET C 880 1 7
HELIX 42 AE6 LEU C 882 GLY C 898 1 17
HELIX 43 AE7 LYS C 910 GLU C 932 1 23
HELIX 44 AE8 ASP C 937 LEU C 950 1 14
HELIX 45 AE9 THR C 958 GLN C 969 1 12
HELIX 46 AF1 MET C 1000 MET C 1005 1 6
HELIX 47 AF2 GLY C 1033 GLY C 1044 1 12
HELIX 48 AF3 ALA C 1045 THR C 1054 1 10
HELIX 49 AF4 ASP C 1059 GLY C 1073 1 15
HELIX 50 AF5 PRO C 1082 ALA C 1094 1 13
HELIX 51 AF6 SER D 14 SER D 22 1 9
HELIX 52 AF7 ASP D 46 GLY D 51 1 6
HELIX 53 AF8 ILE D 84 ARG D 89 1 6
HELIX 54 AF9 HIS D 101 ASP D 107 1 7
HELIX 55 AG1 SER D 110 LEU D 116 1 7
HELIX 56 AG2 SER D 119 TYR D 128 1 10
HELIX 57 AG3 THR D 154 GLY D 164 1 11
HELIX 58 AG4 ASP D 372 GLU D 376 5 5
HELIX 59 AG5 ASP D 423 LYS D 426 5 4
HELIX 60 AG6 GLY D 457 LEU D 468 1 12
HELIX 61 AG7 ASP D 469 LYS D 482 1 14
HELIX 62 AG8 SER D 485 GLY D 506 1 22
HELIX 63 AG9 ARG D 508 TRP D 511 5 4
HELIX 64 AH1 SER D 538 GLN D 560 1 23
HELIX 65 AH2 PRO D 563 ASP D 583 1 21
HELIX 66 AH3 SER D 602 SER D 608 1 7
HELIX 67 AH4 GLY D 612 LEU D 618 1 7
HELIX 68 AH5 LYS D 646 PHE D 653 1 8
HELIX 69 AH6 PHE D 653 LYS D 664 1 12
HELIX 70 AH7 ASN D 669 ARG D 679 1 11
HELIX 71 AH8 GLN D 680 ILE D 683 5 4
HELIX 72 AH9 ASP D 685 ILE D 695 1 11
HELIX 73 AI1 HIS D 709 LEU D 711 5 3
HELIX 74 AI2 VAL D 732 ASN D 737 1 6
HELIX 75 AI3 SER D 752 GLN D 762 1 11
HELIX 76 AI4 ARG D 783 GLN D 794 1 12
HELIX 77 AI5 THR D 808 GLY D 819 1 12
HELIX 78 AI6 SER D 835 TYR D 841 1 7
HELIX 79 AI7 ASN D 845 HIS D 855 1 11
HELIX 80 AI8 SER D 876 GLU D 891 1 16
HELIX 81 AI9 ASP D 892 ILE D 900 1 9
HELIX 82 AJ1 GLU D 907 SER D 945 1 39
HELIX 83 AJ2 GLY D 950 ALA D 954 5 5
HELIX 84 AJ3 GLU D 958 MET D 980 1 23
HELIX 85 AJ4 THR D 984 TYR D 1015 1 32
HELIX 86 AJ5 ASN D 1018 GLY D 1027 1 10
HELIX 87 AJ6 ASN D 1031 GLY D 1040 1 10
HELIX 88 AJ7 THR D 1066 HIS D 1103 1 38
HELIX 89 AJ8 LYS D 1136 TYR D 1145 1 10
HELIX 90 AJ9 SER D 1167 GLY D 1181 1 15
HELIX 91 AK1 GLN D 1202 GLY D 1206 1 5
HELIX 92 AK2 ALA D 1220 GLU D 1231 1 12
HELIX 93 AK3 PRO D 1232 THR D 1234 5 3
HELIX 94 AK4 GLY D 1255 GLU D 1264 1 10
HELIX 95 AK5 ASP D 1331 GLY D 1340 1 10
HELIX 96 AK6 GLY D 1340 GLN D 1359 1 20
HELIX 97 AK7 HIS D 1364 MET D 1376 1 13
HELIX 98 AK8 LYS D 1397 GLU D 1410 1 14
HELIX 99 AK9 GLY D 1423 SER D 1430 1 8
HELIX 100 AL1 SER D 1433 GLN D 1441 1 9
HELIX 101 AL2 ASN D 1442 GLY D 1454 1 13
HELIX 102 AL3 GLY D 1461 LEU D 1468 1 8
HELIX 103 AL4 ALA D 1474 SER D 1478 5 5
HELIX 104 AL5 GLN D 1489 ALA D 1502 1 14
HELIX 105 AL6 GLY E 5 VAL E 13 1 9
HELIX 106 AL7 SER E 15 HIS E 33 1 19
HELIX 107 AL8 ASN E 59 THR E 70 1 12
HELIX 108 AL9 PRO E 81 TYR E 93 1 13
HELIX 109 AM1 ASP F 79 VAL F 91 1 13
HELIX 110 AM2 THR F 95 GLY F 121 1 27
HELIX 111 AM3 ASP F 123 GLY F 137 1 15
HELIX 112 AM4 ASP F 152 SER F 165 1 14
HELIX 113 AM5 PRO F 167 LYS F 201 1 35
HELIX 114 AM6 SER F 208 LYS F 226 1 19
HELIX 115 AM7 GLU F 228 ARG F 232 5 5
HELIX 116 AM8 LYS F 234 ALA F 255 1 22
HELIX 117 AM9 PRO F 261 GLY F 283 1 23
HELIX 118 AN1 THR F 287 MET F 295 1 9
HELIX 119 AN2 ASP F 300 GLN F 312 1 13
HELIX 120 AN3 TYR F 329 ILE F 333 5 5
HELIX 121 AN4 SER F 340 LYS F 360 1 21
HELIX 122 AN5 SER F 362 GLY F 374 1 13
HELIX 123 AN6 THR F 382 PHE F 390 1 9
HELIX 124 AN7 THR F 393 ARG F 416 1 24
HELIX 125 AN8 ARG F 419 ASP F 423 5 5
SHEET 1 AA1 4 VAL A 10 GLN A 16 0
SHEET 2 AA1 4 TYR A 20 LEU A 28 -1 O GLU A 22 N ARG A 14
SHEET 3 AA1 4 ARG A 189 THR A 201 -1 O LEU A 197 N PHE A 23
SHEET 4 AA1 4 VAL A 174 LEU A 186 -1 N ALA A 178 O ARG A 198
SHEET 1 AA2 4 THR A 96 GLU A 104 0
SHEET 2 AA2 4 ARG A 137 VAL A 148 -1 O VAL A 144 N VAL A 97
SHEET 3 AA2 4 PRO A 49 ILE A 58 -1 N GLY A 50 O GLY A 147
SHEET 4 AA2 4 ILE A 165 PRO A 166 -1 O ILE A 165 N VAL A 56
SHEET 1 AA3 2 VAL A 87 PHE A 89 0
SHEET 2 AA3 2 VAL A 120 ILE A 122 -1 O GLU A 121 N ARG A 88
SHEET 1 AA4 2 LYS A 107 LYS A 110 0
SHEET 2 AA4 2 HIS A 128 LEU A 132 -1 O LEU A 132 N LYS A 107
SHEET 1 AA5 2 TYR A 150 VAL A 151 0
SHEET 2 AA5 2 ALA A 169 VAL A 170 -1 O ALA A 169 N VAL A 151
SHEET 1 AA6 5 PRO A 228 ALA A 230 0
SHEET 2 AA6 5 VAL B 10 GLN B 16 1 O VAL B 13 N GLN A 229
SHEET 3 AA6 5 TYR B 20 LEU B 28 -1 O GLU B 22 N ARG B 14
SHEET 4 AA6 5 ASP B 193 THR B 201 -1 O LEU B 197 N PHE B 23
SHEET 5 AA6 5 VAL B 174 ASP B 183 -1 N ALA B 178 O ARG B 198
SHEET 1 AA7 4 THR B 96 GLU B 104 0
SHEET 2 AA7 4 ARG B 137 GLY B 147 -1 O VAL B 142 N LEU B 99
SHEET 3 AA7 4 GLY B 50 ILE B 58 -1 N THR B 54 O ARG B 143
SHEET 4 AA7 4 ILE B 165 PRO B 166 -1 O ILE B 165 N VAL B 56
SHEET 1 AA8 2 VAL B 87 PHE B 89 0
SHEET 2 AA8 2 VAL B 120 ILE B 122 -1 O GLU B 121 N ARG B 88
SHEET 1 AA9 2 LYS B 107 LYS B 110 0
SHEET 2 AA9 2 HIS B 128 LEU B 132 -1 O LEU B 132 N LYS B 107
SHEET 1 AB1 2 TYR B 150 VAL B 151 0
SHEET 2 AB1 2 ALA B 169 VAL B 170 -1 O ALA B 169 N VAL B 151
SHEET 1 AB2 3 GLU C 2 ARG C 5 0
SHEET 2 AB2 3 GLN C 899 ILE C 902 1 O ILE C 902 N LYS C 4
SHEET 3 AB2 3 VAL C 579 MET C 580 1 N MET C 580 O TYR C 901
SHEET 1 AB3 3 VAL C 65 LEU C 73 0
SHEET 2 AB3 3 GLN C 91 ILE C 101 -1 O ILE C 101 N VAL C 65
SHEET 3 AB3 3 ILE C 108 PRO C 119 -1 O GLY C 116 N LEU C 94
SHEET 1 AB4 3 PHE C 127 ILE C 129 0
SHEET 2 AB4 3 ALA C 132 ILE C 136 -1 O ALA C 132 N ILE C 129
SHEET 3 AB4 3 SER C 392 PHE C 394 -1 O GLN C 393 N VAL C 135
SHEET 1 AB5 4 ARG C 331 ARG C 334 0
SHEET 2 AB5 4 SER C 138 ARG C 142 -1 N GLN C 139 O ARG C 334
SHEET 3 AB5 4 ARG C 409 SER C 411 1 O SER C 411 N ILE C 140
SHEET 4 AB5 4 ILE C 452 SER C 454 -1 O THR C 453 N ILE C 410
SHEET 1 AB6 5 GLY C 145 PRO C 150 0
SHEET 2 AB6 5 TYR C 158 ILE C 163 -1 O ILE C 159 N THR C 149
SHEET 3 AB6 5 ILE C 172 VAL C 176 -1 O ILE C 172 N ILE C 162
SHEET 4 AB6 5 VAL C 182 VAL C 186 -1 O SER C 183 N GLU C 175
SHEET 5 AB6 5 LYS C 190 PRO C 192 -1 O PHE C 191 N MET C 184
SHEET 1 AB7 2 ALA C 291 GLU C 294 0
SHEET 2 AB7 2 GLU C 297 ASP C 300 -1 O GLU C 297 N GLU C 294
SHEET 1 AB8 3 ARG C 460 VAL C 461 0
SHEET 2 AB8 3 ILE C 467 VAL C 475 -1 O ARG C 468 N ARG C 460
SHEET 3 AB8 3 VAL C 478 MET C 486 -1 O THR C 480 N ARG C 473
SHEET 1 AB9 6 ARG C 460 VAL C 461 0
SHEET 2 AB9 6 ILE C 467 VAL C 475 -1 O ARG C 468 N ARG C 460
SHEET 3 AB9 6 PHE C 531 ASP C 533 -1 O MET C 532 N ARG C 472
SHEET 4 AB9 6 THR C 495 ALA C 497 1 N ALA C 497 O PHE C 531
SHEET 5 AB9 6 VAL C 513 ARG C 517 -1 O ARG C 516 N ILE C 496
SHEET 6 AB9 6 GLU C 520 VAL C 524 -1 O VAL C 522 N ALA C 515
SHEET 1 AC1 2 LEU C 503 GLU C 504 0
SHEET 2 AC1 2 ARG C 507 ILE C 508 -1 O ARG C 507 N GLU C 504
SHEET 1 AC2 3 LEU C 595 TYR C 596 0
SHEET 2 AC2 3 LEU C 654 ASP C 657 -1 O ALA C 656 N LEU C 595
SHEET 3 AC2 3 ARG C 640 PRO C 641 -1 N ARG C 640 O ASP C 657
SHEET 1 AC3 4 LEU C 620 PRO C 624 0
SHEET 2 AC3 4 ARG C 610 TYR C 615 -1 N ILE C 611 O TYR C 623
SHEET 3 AC3 4 GLY C 601 VAL C 606 -1 N GLU C 602 O ARG C 614
SHEET 4 AC3 4 ARG C 648 VAL C 649 -1 O VAL C 649 N GLY C 601
SHEET 1 AC4 2 TYR C 629 ARG C 630 0
SHEET 2 AC4 2 ALA C 636 LEU C 637 -1 O LEU C 637 N TYR C 629
SHEET 1 AC5 2 SER C 661 GLU C 662 0
SHEET 2 AC5 2 PHE C 665 LEU C 666 -1 O PHE C 665 N GLU C 662
SHEET 1 AC6 8 LYS C 971 VAL C 972 0
SHEET 2 AC6 8 ILE C 987 LYS C 996 -1 O ILE C 987 N VAL C 972
SHEET 3 AC6 8 LYS C 838 ASN C 841 -1 N ALA C 840 O MET C 995
SHEET 4 AC6 8 LYS C 846 LEU C 853 -1 O GLY C 847 N LEU C 839
SHEET 5 AC6 8 ILE C 688 SER C 691 1 N ILE C 688 O VAL C 848
SHEET 6 AC6 8 VAL C 869 LEU C 871 -1 O ILE C 870 N VAL C 689
SHEET 7 AC6 8 GLN C 670 ILE C 676 1 N ALA C 675 O VAL C 869
SHEET 8 AC6 8 ILE C 987 LYS C 996 -1 O GLY C 990 N VAL C 674
SHEET 1 AC7 4 SER C 702 ARG C 713 0
SHEET 2 AC7 4 VAL C 819 ARG C 831 -1 O ARG C 831 N SER C 702
SHEET 3 AC7 4 GLY C 798 ARG C 807 -1 N VAL C 804 O ARG C 824
SHEET 4 AC7 4 GLU C 748 VAL C 749 -1 N VAL C 749 O GLY C 798
SHEET 1 AC8 2 ILE C 754 VAL C 756 0
SHEET 2 AC8 2 LEU C 790 ARG C 791 -1 O LEU C 790 N LEU C 755
SHEET 1 AC9 2 THR C 759 PHE C 761 0
SHEET 2 AC9 2 VAL C 785 ASP C 787 -1 O LYS C 786 N SER C 760
SHEET 1 AD1 8 HIS C1006 ARG C1008 0
SHEET 2 AD1 8 SER D 626 VAL D 633 -1 O ARG D 628 N HIS C1006
SHEET 3 AD1 8 GLN D 744 HIS D 748 -1 O VAL D 747 N GLY D 627
SHEET 4 AD1 8 VAL D 700 ASN D 703 -1 N LEU D 701 O HIS D 748
SHEET 5 AD1 8 ILE D 713 VAL D 721 -1 O GLN D 714 N LEU D 702
SHEET 6 AD1 8 GLN D 641 PRO D 645 1 N CYS D 642 O VAL D 719
SHEET 7 AD1 8 ILE D 726 LEU D 728 -1 O GLN D 727 N GLY D 643
SHEET 8 AD1 8 SER D 626 VAL D 633 1 N VAL D 630 O ILE D 726
SHEET 1 AD2 2 ARG C1031 PHE C1032 0
SHEET 2 AD2 2 LYS D 621 ARG D 622 -1 O LYS D 621 N PHE C1032
SHEET 1 AD3 4 PRO C1108 VAL C1109 0
SHEET 2 AD3 4 LEU C1097 LEU C1102 -1 N THR C1101 O VAL C1109
SHEET 3 AD3 4 LYS D 7 LEU D 12 -1 O ARG D 9 N GLN C1100
SHEET 4 AD3 4 LYS D1456 ASP D1457 -1 O ASP D1457 N VAL D 8
SHEET 1 AD4 2 GLY D 91 ALA D 100 0
SHEET 2 AD4 2 ILE D 513 VAL D 519 -1 O VAL D 517 N ILE D 93
SHEET 1 AD5 3 LEU D 152 LEU D 153 0
SHEET 2 AD5 3 TYR D 132 ASP D 136 -1 N TYR D 132 O LEU D 153
SHEET 3 AD5 3 ASP D 453 ARG D 455 -1 O ASP D 453 N LEU D 135
SHEET 1 AD6 2 ILE D 141 LEU D 142 0
SHEET 2 AD6 2 VAL D 145 PRO D 146 -1 O VAL D 145 N LEU D 142
SHEET 1 AD7 5 GLN D 166 PRO D 170 0
SHEET 2 AD7 5 GLY D 383 VAL D 396 -1 O ILE D 393 N TYR D 169
SHEET 3 AD7 5 GLY D 201 PRO D 226 -1 N ARG D 209 O GLU D 389
SHEET 4 AD7 5 THR D 330 ARG D 346 -1 O LEU D 333 N LEU D 223
SHEET 5 AD7 5 VAL D 317 GLU D 327 -1 N GLU D 323 O THR D 334
SHEET 1 AD8 4 GLU D 184 VAL D 185 0
SHEET 2 AD8 4 GLY D 201 PRO D 226 -1 O GLY D 201 N VAL D 185
SHEET 3 AD8 4 GLY D 383 VAL D 396 -1 O GLU D 389 N ARG D 209
SHEET 4 AD8 4 ARG D 360 VAL D 361 -1 N VAL D 361 O GLY D 383
SHEET 1 AD9 2 GLU D 190 ALA D 192 0
SHEET 2 AD9 2 VAL D 195 VAL D 196 -1 O VAL D 195 N ALA D 192
SHEET 1 AE1 3 ILE D 241 GLU D 244 0
SHEET 2 AE1 3 PRO D 303 ARG D 312 -1 O LEU D 311 N ALA D 243
SHEET 3 AE1 3 TYR D 249 ARG D 252 -1 N TYR D 249 O ALA D 307
SHEET 1 AE2 3 ILE D 241 GLU D 244 0
SHEET 2 AE2 3 PRO D 303 ARG D 312 -1 O LEU D 311 N ALA D 243
SHEET 3 AE2 3 VAL D 286 PRO D 290 -1 N THR D 289 O GLU D 306
SHEET 1 AE3 4 PRO D 278 LEU D 284 0
SHEET 2 AE3 4 ALA D 268 ARG D 273 -1 N LEU D 270 O TYR D 282
SHEET 3 AE3 4 GLY D 257 GLU D 263 -1 N GLU D 260 O VAL D 271
SHEET 4 AE3 4 ILE D 297 VAL D 298 -1 O VAL D 298 N GLY D 257
SHEET 1 AE4 3 ASN D 352 VAL D 353 0
SHEET 2 AE4 3 LYS D 366 ALA D 369 -1 O ALA D 369 N ASN D 352
SHEET 3 AE4 3 VAL D 377 ILE D 378 -1 O VAL D 377 N ILE D 367
SHEET 1 AE5 4 ALA D 398 PRO D 402 0
SHEET 2 AE5 4 VAL D 443 GLU D 448 -1 O VAL D 446 N ARG D 399
SHEET 3 AE5 4 GLY D 433 ASP D 438 -1 N GLU D 436 O ARG D 445
SHEET 4 AE5 4 ARG D 414 VAL D 415 -1 N VAL D 415 O GLY D 433
SHEET 1 AE6 2 VAL D 420 ALA D 422 0
SHEET 2 AE6 2 VAL D 427 LYS D 428 -1 O VAL D 427 N LEU D 421
SHEET 1 AE7 3 MET D 527 GLN D 529 0
SHEET 2 AE7 3 PHE D 535 THR D 537 -1 O ALA D 536 N VAL D 528
SHEET 3 AE7 3 VAL F 315 SER F 316 1 O VAL F 315 N PHE D 535
SHEET 1 AE8 3 GLU D 805 PHE D 806 0
SHEET 2 AE8 3 ILE D 827 VAL D 829 1 O LYS D 828 N PHE D 806
SHEET 3 AE8 3 ARG D 832 THR D 834 -1 O THR D 834 N ILE D 827
SHEET 1 AE9 3 VAL D 842 PHE D 843 0
SHEET 2 AE9 3 VAL D 864 TYR D 868 1 O THR D 865 N PHE D 843
SHEET 3 AE9 3 LYS D 871 THR D 875 -1 O LEU D 873 N VAL D 866
SHEET 1 AF1 2 VAL D1107 GLU D1109 0
SHEET 2 AF1 2 VAL D1200 CYS D1201 1 O VAL D1200 N ARG D1108
SHEET 1 AF2 2 ILE D1118 PRO D1121 0
SHEET 2 AF2 2 GLU D1185 VAL D1188 -1 O VAL D1188 N ILE D1118
SHEET 1 AF3 2 PHE D1123 PRO D1125 0
SHEET 2 AF3 2 LEU D1132 LEU D1134 -1 O ARG D1133 N GLN D1124
SHEET 1 AF4 2 VAL D1153 VAL D1155 0
SHEET 2 AF4 2 VAL D1158 LEU D1160 -1 O LEU D1160 N VAL D1153
SHEET 1 AF5 2 TYR D1207 ASP D1208 0
SHEET 2 AF5 2 ARG D1213 PRO D1214 -1 O ARG D1213 N ASP D1208
SHEET 1 AF6 4 SER D1300 LYS D1304 0
SHEET 2 AF6 4 LEU D1290 GLU D1295 -1 N VAL D1292 O TYR D1303
SHEET 3 AF6 4 GLY D1279 GLU D1285 -1 N ARG D1282 O PHE D1293
SHEET 4 AF6 4 TYR D1318 VAL D1319 -1 O VAL D1319 N GLY D1279
SHEET 1 AF7 3 VAL D1394 GLU D1396 0
SHEET 2 AF7 3 TYR D1378 ASP D1383 -1 N VAL D1379 O LEU D1395
SHEET 3 AF7 3 ALA D1416 LEU D1420 -1 O LYS D1418 N GLU D1380
SHEET 1 AF8 2 GLN D1485 ASP D1488 0
SHEET 2 AF8 2 LEU E 73 GLY E 76 -1 O GLY E 76 N GLN D1485
SHEET 1 AF9 2 LYS E 47 GLN E 49 0
SHEET 2 AF9 2 LEU E 54 ASP E 56 -1 O PHE E 55 N MET E 48
SSBOND 1 CYS D 60 CYS D 76 1555 1555 2.57
SSBOND 2 CYS D 73 CYS D 76 1555 1555 2.80
SSBOND 3 CYS D 1194 CYS D 1201 1555 1555 2.97
LINK OD1 ASP B 183 MG MG B2001 1555 1555 2.80
LINK O ASP B 191 MG MG B2001 1555 1555 2.13
LINK O HOH B2105 MG MG D1601 1555 1555 2.08
LINK O HOH B2110 MG MG D1601 1555 1555 2.11
LINK SG CYS D 58 ZN ZN D1603 1555 1555 2.24
LINK SG CYS D 60 ZN ZN D1603 1555 1555 2.17
LINK SG CYS D 73 ZN ZN D1603 1555 1555 2.21
LINK SG CYS D 76 ZN ZN D1603 1555 1555 2.26
LINK OD1 ASP D 739 MG MG D1604 1555 1555 2.04
LINK OD1 ASP D 741 MG MG D1604 1555 1555 2.07
LINK OD2 ASP D 741 MG MG D1604 1555 1555 2.63
LINK OD1 ASP D 743 MG MG D1604 1555 1555 2.06
LINK OD2 ASP D 743 MG MG D1604 1555 1555 2.83
LINK O LYS D 840 MG MG D1601 1555 1555 2.53
LINK SG CYS D1112 ZN ZN D1602 1555 1555 2.13
LINK SG CYS D1194 ZN ZN D1602 1555 1555 2.16
LINK SG CYS D1201 ZN ZN D1602 1555 1555 2.08
LINK SG CYS D1204 ZN ZN D1602 1555 1555 2.21
LINK MG MG D1601 O HOH D2117 1555 1555 2.31
LINK MG MG D1604 O HOH D2104 1555 1555 2.06
LINK MG MG D1604 O HOH D2105 1555 1555 2.08
LINK MG MG D1604 O3' A I 7 1555 1555 2.39
LINK O ALA F 292 MG MG F2001 1555 1555 2.32
LINK O GLY F 296 MG MG F2001 1555 1555 2.44
CISPEP 1 GLU A 26 PRO A 27 0 -11.45
CISPEP 2 ALA B 8 PRO B 9 0 8.37
CISPEP 3 GLU B 26 PRO B 27 0 -9.93
CISPEP 4 PHE C 52 PRO C 53 0 2.85
CISPEP 5 VAL D 108 PRO D 109 0 -5.83
CISPEP 6 ALA D 705 PRO D 706 0 -0.50
SITE 1 AC1 3 ASP B 183 ASP B 191 ASP B 193
SITE 1 AC2 6 GLU B 154 ASP B 168 HOH B2105 HOH B2110
SITE 2 AC2 6 LYS D 840 HOH D2117
SITE 1 AC3 4 CYS D1112 CYS D1194 CYS D1201 CYS D1204
SITE 1 AC4 5 CYS D 58 CYS D 60 LYS D 62 CYS D 73
SITE 2 AC4 5 CYS D 76
SITE 1 AC5 6 ASP D 739 ASP D 741 ASP D 743 HOH D2104
SITE 2 AC5 6 HOH D2105 A I 7
SITE 1 AC6 4 ALA F 292 GLU F 293 GLY F 296 TRP F 299
CRYST1 183.007 103.566 294.935 90.00 99.20 90.00 C 1 2 1 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 0.005464 0.000000 0.000885 0.00000
SCALE2 0.000000 0.009656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003435 0.00000
(ATOM LINES ARE NOT SHOWN.)
END