HEADER TRANSFERASE/DNA 24-NOV-18 6N61
TITLE ESCHERICHIA COLI RNA POLYMERASE SIGMA70-HOLOENZYME BOUND TO UPSTREAM
TITLE 2 FORK PROMOTER DNA AND CAPISTRUIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (UNP RESIDUES 1-234);
COMPND 5 SYNONYM: RNAP SUBUNIT ALPHA,RNA POLYMERASE SUBUNIT ALPHA,
COMPND 6 TRANSCRIPTASE SUBUNIT ALPHA;
COMPND 7 EC: 2.7.7.6;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND 11 CHAIN: C;
COMPND 12 SYNONYM: RNAP SUBUNIT BETA,RNA POLYMERASE SUBUNIT BETA,TRANSCRIPTASE
COMPND 13 SUBUNIT BETA;
COMPND 14 EC: 2.7.7.6;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA';
COMPND 18 CHAIN: D;
COMPND 19 SYNONYM: RNAP SUBUNIT BETA',RNA POLYMERASE SUBUNIT BETA',
COMPND 20 TRANSCRIPTASE SUBUNIT BETA';
COMPND 21 EC: 2.7.7.6;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 4;
COMPND 24 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA;
COMPND 25 CHAIN: E;
COMPND 26 SYNONYM: RNAP OMEGA SUBUNIT,RNA POLYMERASE OMEGA SUBUNIT,
COMPND 27 TRANSCRIPTASE SUBUNIT OMEGA;
COMPND 28 EC: 2.7.7.6;
COMPND 29 ENGINEERED: YES;
COMPND 30 MOL_ID: 5;
COMPND 31 MOLECULE: RNA POLYMERASE SIGMA FACTOR RPOD;
COMPND 32 CHAIN: F;
COMPND 33 SYNONYM: SIGMA-70;
COMPND 34 ENGINEERED: YES;
COMPND 35 MOL_ID: 6;
COMPND 36 MOLECULE: NON-TEMPLATE STRAND DNA;
COMPND 37 CHAIN: N;
COMPND 38 ENGINEERED: YES;
COMPND 39 MOL_ID: 7;
COMPND 40 MOLECULE: TEMPLATE STRAND DNA;
COMPND 41 CHAIN: T;
COMPND 42 ENGINEERED: YES;
COMPND 43 MOL_ID: 8;
COMPND 44 MOLECULE: CAPISTRUIN;
COMPND 45 CHAIN: I;
COMPND 46 FRAGMENT: UNP RESIDUES 29-47;
COMPND 47 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: RPOA, PEZ, PHS, SEZ, B3295, JW3257;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 9 ORGANISM_TAXID: 562;
SOURCE 10 GENE: RPOB, GRON, NITB, RIF, RON, STL, STV, TABD, B3987, JW3950;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 15 ORGANISM_TAXID: 562;
SOURCE 16 GENE: RPOC, TABB, B3988, JW3951;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 21 ORGANISM_TAXID: 562;
SOURCE 22 GENE: RPOZ, B3649, JW3624;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 25 MOL_ID: 5;
SOURCE 26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 27 ORGANISM_TAXID: 562;
SOURCE 28 GENE: RPOD;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 31 MOL_ID: 6;
SOURCE 32 SYNTHETIC: YES;
SOURCE 33 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 34 ORGANISM_TAXID: 562;
SOURCE 35 MOL_ID: 7;
SOURCE 36 SYNTHETIC: YES;
SOURCE 37 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 38 ORGANISM_TAXID: 562;
SOURCE 39 MOL_ID: 8;
SOURCE 40 ORGANISM_SCIENTIFIC: BURKHOLDERIA THAILANDENSIS (STRAIN ATCC 700388
SOURCE 41 / DSM 13276 / CIP 106301 / E264);
SOURCE 42 ORGANISM_TAXID: 271848;
SOURCE 43 STRAIN: ATCC 700388 / DSM 13276 / CIP 106301 / E264;
SOURCE 44 GENE: DR63_3338;
SOURCE 45 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 46 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CAPISTRUIN, COMPLEX, INHIBITOR, LASSO PEPTIDE, RNA POLYMERASE,
KEYWDS 2 TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.BRAFFMAN,J.HAUVER,E.A.CAMPBELL,S.A.DARST
REVDAT 5 11-OCT-23 6N61 1 REMARK
REVDAT 4 01-JAN-20 6N61 1 REMARK
REVDAT 3 06-FEB-19 6N61 1 JRNL
REVDAT 2 23-JAN-19 6N61 1 JRNL
REVDAT 1 09-JAN-19 6N61 0
JRNL AUTH N.R.BRAFFMAN,F.J.PISCOTTA,J.HAUVER,E.A.CAMPBELL,A.J.LINK,
JRNL AUTH 2 S.A.DARST
JRNL TITL STRUCTURAL MECHANISM OF TRANSCRIPTION INHIBITION BY LASSO
JRNL TITL 2 PEPTIDES MICROCIN J25 AND CAPISTRUIN.
JRNL REF PROC. NATL. ACAD. SCI. V. 116 1273 2019
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 30626643
JRNL DOI 10.1073/PNAS.1817352116
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 91638
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.274
REMARK 3 R VALUE (WORKING SET) : 0.273
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1898
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 49.4503 - 7.8306 1.00 6881 146 0.2230 0.2502
REMARK 3 2 7.8306 - 6.2192 1.00 6570 139 0.2591 0.2996
REMARK 3 3 6.2192 - 5.4342 1.00 6499 138 0.2565 0.3276
REMARK 3 4 5.4342 - 4.9378 1.00 6457 135 0.2471 0.2936
REMARK 3 5 4.9378 - 4.5842 0.99 6392 135 0.2395 0.3117
REMARK 3 6 4.5842 - 4.3141 0.99 6376 133 0.2446 0.2883
REMARK 3 7 4.3141 - 4.0981 0.99 6336 133 0.2786 0.3024
REMARK 3 8 4.0981 - 3.9198 0.99 6363 136 0.3132 0.3953
REMARK 3 9 3.9198 - 3.7690 1.00 6334 134 0.3330 0.3855
REMARK 3 10 3.7690 - 3.6390 1.00 6381 135 0.3339 0.3868
REMARK 3 11 3.6390 - 3.5252 1.00 6335 134 0.3640 0.3887
REMARK 3 12 3.5252 - 3.4245 1.00 6356 134 0.3634 0.4153
REMARK 3 13 3.4245 - 3.3343 0.99 6287 133 0.3961 0.4208
REMARK 3 14 3.3343 - 3.2530 0.97 6173 133 0.4047 0.4525
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.720
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.002 29083
REMARK 3 ANGLE : 0.530 39469
REMARK 3 CHIRALITY : 0.039 4501
REMARK 3 PLANARITY : 0.003 4978
REMARK 3 DIHEDRAL : 17.511 17749
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 6N61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000238242.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97919
REMARK 200 MONOCHROMATOR : CRYOGENICALLY-COOLED SINGLE
REMARK 200 CRYSTAL SI(220) SIDE BOUNCE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92082
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 20.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.760
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 4LJZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 6.8, 0.2 M MAGNESIUM
REMARK 280 CHLORIDE, 7% W/V PEG3350, 4% V/V GLYCEROL, 4% V/V ETHYLENE
REMARK 280 GLYCOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 192.50750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 86.44400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 86.44400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 96.25375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 86.44400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 86.44400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 288.76125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 86.44400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 86.44400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 96.25375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 86.44400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 86.44400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 288.76125
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 192.50750
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: 44950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 158980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -213.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, N, T, 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 GLN A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 VAL A 5
REMARK 465 THR A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 236
REMARK 465 LEU A 237
REMARK 465 PHE A 238
REMARK 465 GLN A 239
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 VAL B 5
REMARK 465 ILE B 159
REMARK 465 HIS B 160
REMARK 465 SER B 161
REMARK 465 GLU B 162
REMARK 465 GLU B 163
REMARK 465 ASP B 164
REMARK 465 GLU B 165
REMARK 465 ARG B 166
REMARK 465 PRO B 167
REMARK 465 ILE B 168
REMARK 465 GLY B 169
REMARK 465 ARG B 170
REMARK 465 GLU B 235
REMARK 465 VAL B 236
REMARK 465 LEU B 237
REMARK 465 PHE B 238
REMARK 465 GLN B 239
REMARK 465 MET C 1
REMARK 465 GLU C 108
REMARK 465 ALA C 109
REMARK 465 PRO C 110
REMARK 465 GLU C 256
REMARK 465 ALA C 257
REMARK 465 ASN C 258
REMARK 465 GLY C 259
REMARK 465 LYS C 260
REMARK 465 VAL C 261
REMARK 465 VAL D 1
REMARK 465 LYS D 2
REMARK 465 ASP D 3
REMARK 465 LEU D 4
REMARK 465 LEU D 5
REMARK 465 LYS D 6
REMARK 465 PHE D 7
REMARK 465 LEU D 8
REMARK 465 LYS D 9
REMARK 465 ALA D 10
REMARK 465 GLN D 11
REMARK 465 THR D 12
REMARK 465 LYS D 13
REMARK 465 THR D 14
REMARK 465 GLU D 15
REMARK 465 GLU D 16
REMARK 465 GLY D 939
REMARK 465 ALA D 940
REMARK 465 ALA D 941
REMARK 465 SER D 942
REMARK 465 ARG D 943
REMARK 465 ALA D 944
REMARK 465 ALA D 945
REMARK 465 ALA D 946
REMARK 465 GLU D 947
REMARK 465 PRO D 1026
REMARK 465 VAL D 1027
REMARK 465 ILE D 1028
REMARK 465 THR D 1029
REMARK 465 GLU D 1030
REMARK 465 VAL D 1031
REMARK 465 SER D 1032
REMARK 465 GLY D 1033
REMARK 465 PHE D 1034
REMARK 465 VAL D 1035
REMARK 465 ARG D 1036
REMARK 465 PHE D 1037
REMARK 465 THR D 1038
REMARK 465 ASP D 1039
REMARK 465 MET D 1040
REMARK 465 ILE D 1041
REMARK 465 ASP D 1042
REMARK 465 GLY D 1043
REMARK 465 GLN D 1044
REMARK 465 THR D 1045
REMARK 465 ILE D 1046
REMARK 465 THR D 1047
REMARK 465 ARG D 1048
REMARK 465 GLN D 1049
REMARK 465 THR D 1050
REMARK 465 ASP D 1051
REMARK 465 GLU D 1052
REMARK 465 LEU D 1053
REMARK 465 THR D 1054
REMARK 465 GLY D 1055
REMARK 465 LEU D 1056
REMARK 465 SER D 1057
REMARK 465 SER D 1058
REMARK 465 LEU D 1059
REMARK 465 VAL D 1060
REMARK 465 VAL D 1061
REMARK 465 LEU D 1062
REMARK 465 ASP D 1063
REMARK 465 SER D 1064
REMARK 465 ALA D 1065
REMARK 465 GLU D 1066
REMARK 465 ARG D 1067
REMARK 465 THR D 1068
REMARK 465 ALA D 1069
REMARK 465 GLY D 1070
REMARK 465 GLY D 1071
REMARK 465 LYS D 1072
REMARK 465 ASP D 1073
REMARK 465 LEU D 1074
REMARK 465 ARG D 1075
REMARK 465 PRO D 1076
REMARK 465 ALA D 1077
REMARK 465 LEU D 1078
REMARK 465 LYS D 1079
REMARK 465 ILE D 1080
REMARK 465 VAL D 1081
REMARK 465 ASP D 1082
REMARK 465 ALA D 1083
REMARK 465 GLN D 1084
REMARK 465 GLY D 1085
REMARK 465 ASN D 1086
REMARK 465 ASP D 1087
REMARK 465 VAL D 1088
REMARK 465 LEU D 1089
REMARK 465 ILE D 1090
REMARK 465 PRO D 1091
REMARK 465 GLY D 1092
REMARK 465 THR D 1093
REMARK 465 ASP D 1094
REMARK 465 MET D 1095
REMARK 465 PRO D 1096
REMARK 465 ALA D 1097
REMARK 465 GLN D 1098
REMARK 465 TYR D 1099
REMARK 465 PHE D 1100
REMARK 465 LEU D 1101
REMARK 465 PRO D 1102
REMARK 465 GLY D 1103
REMARK 465 LYS D 1104
REMARK 465 ALA D 1105
REMARK 465 ILE D 1106
REMARK 465 VAL D 1107
REMARK 465 GLN D 1108
REMARK 465 LEU D 1109
REMARK 465 GLU D 1110
REMARK 465 ASP D 1111
REMARK 465 GLY D 1112
REMARK 465 VAL D 1113
REMARK 465 GLN D 1114
REMARK 465 ILE D 1115
REMARK 465 SER D 1116
REMARK 465 SER D 1117
REMARK 465 GLY D 1118
REMARK 465 ASP D 1119
REMARK 465 THR D 1120
REMARK 465 LEU D 1121
REMARK 465 ALA D 1122
REMARK 465 ARG D 1123
REMARK 465 ILE D 1124
REMARK 465 PRO D 1125
REMARK 465 GLN D 1126
REMARK 465 GLU D 1127
REMARK 465 SER D 1128
REMARK 465 GLY D 1129
REMARK 465 GLY D 1130
REMARK 465 THR D 1131
REMARK 465 LYS D 1132
REMARK 465 ASP D 1133
REMARK 465 PHE D 1274
REMARK 465 LEU D 1275
REMARK 465 GLU D 1276
REMARK 465 GLY D 1376
REMARK 465 GLU D 1377
REMARK 465 ALA D 1378
REMARK 465 PRO D 1379
REMARK 465 ALA D 1380
REMARK 465 ALA D 1381
REMARK 465 PRO D 1382
REMARK 465 GLN D 1383
REMARK 465 VAL D 1384
REMARK 465 THR D 1385
REMARK 465 ALA D 1386
REMARK 465 GLU D 1387
REMARK 465 ASP D 1388
REMARK 465 ALA D 1389
REMARK 465 SER D 1390
REMARK 465 ALA D 1391
REMARK 465 SER D 1392
REMARK 465 LEU D 1393
REMARK 465 ALA D 1394
REMARK 465 GLU D 1395
REMARK 465 LEU D 1396
REMARK 465 LEU D 1397
REMARK 465 ASN D 1398
REMARK 465 ALA D 1399
REMARK 465 GLY D 1400
REMARK 465 LEU D 1401
REMARK 465 GLY D 1402
REMARK 465 GLY D 1403
REMARK 465 SER D 1404
REMARK 465 ASP D 1405
REMARK 465 ASN D 1406
REMARK 465 GLU D 1407
REMARK 465 LEU D 1408
REMARK 465 GLU D 1409
REMARK 465 MET E 1
REMARK 465 GLN E 81
REMARK 465 ALA E 82
REMARK 465 VAL E 83
REMARK 465 THR E 84
REMARK 465 ALA E 85
REMARK 465 ILE E 86
REMARK 465 ALA E 87
REMARK 465 GLU E 88
REMARK 465 GLY E 89
REMARK 465 ARG E 90
REMARK 465 MET F 1
REMARK 465 GLU F 2
REMARK 465 GLN F 3
REMARK 465 ASN F 4
REMARK 465 PRO F 5
REMARK 465 GLN F 6
REMARK 465 SER F 7
REMARK 465 GLN F 8
REMARK 465 LEU F 9
REMARK 465 LYS F 10
REMARK 465 LEU F 11
REMARK 465 LEU F 12
REMARK 465 VAL F 13
REMARK 465 THR F 14
REMARK 465 ARG F 15
REMARK 465 GLY F 16
REMARK 465 LYS F 17
REMARK 465 GLU F 18
REMARK 465 GLN F 19
REMARK 465 GLY F 20
REMARK 465 TYR F 21
REMARK 465 LEU F 22
REMARK 465 THR F 23
REMARK 465 TYR F 24
REMARK 465 ALA F 25
REMARK 465 GLU F 26
REMARK 465 VAL F 27
REMARK 465 ASN F 28
REMARK 465 ASP F 29
REMARK 465 HIS F 30
REMARK 465 LEU F 31
REMARK 465 PRO F 32
REMARK 465 GLU F 33
REMARK 465 ASP F 34
REMARK 465 ILE F 35
REMARK 465 VAL F 36
REMARK 465 ASP F 37
REMARK 465 SER F 38
REMARK 465 ASP F 39
REMARK 465 GLN F 40
REMARK 465 ILE F 41
REMARK 465 GLU F 42
REMARK 465 ASP F 43
REMARK 465 ILE F 44
REMARK 465 ILE F 45
REMARK 465 GLN F 46
REMARK 465 MET F 47
REMARK 465 ILE F 48
REMARK 465 ASN F 49
REMARK 465 ASP F 50
REMARK 465 MET F 51
REMARK 465 GLY F 52
REMARK 465 ILE F 53
REMARK 465 GLN F 54
REMARK 465 VAL F 55
REMARK 465 MET F 56
REMARK 465 GLU F 57
REMARK 465 GLU F 58
REMARK 465 ALA F 59
REMARK 465 PRO F 60
REMARK 465 ASP F 61
REMARK 465 ALA F 62
REMARK 465 ASP F 63
REMARK 465 ASP F 64
REMARK 465 LEU F 65
REMARK 465 MET F 66
REMARK 465 LEU F 67
REMARK 465 ALA F 68
REMARK 465 GLU F 69
REMARK 465 ASN F 70
REMARK 465 THR F 71
REMARK 465 ALA F 72
REMARK 465 ASP F 73
REMARK 465 GLU F 74
REMARK 465 ASP F 75
REMARK 465 ALA F 76
REMARK 465 ALA F 77
REMARK 465 GLU F 78
REMARK 465 ALA F 79
REMARK 465 ALA F 80
REMARK 465 ALA F 81
REMARK 465 GLN F 82
REMARK 465 VAL F 83
REMARK 465 LEU F 84
REMARK 465 SER F 85
REMARK 465 SER F 86
REMARK 465 VAL F 87
REMARK 465 GLU F 88
REMARK 465 SER F 89
REMARK 465 GLU F 90
REMARK 465 ILE F 91
REMARK 465 GLY F 92
REMARK 465 ARG F 93
REMARK 465 TYR F 137
REMARK 465 PRO F 138
REMARK 465 GLU F 139
REMARK 465 ALA F 140
REMARK 465 ILE F 141
REMARK 465 THR F 142
REMARK 465 TYR F 143
REMARK 465 LEU F 144
REMARK 465 LEU F 145
REMARK 465 GLU F 146
REMARK 465 GLN F 147
REMARK 465 TYR F 148
REMARK 465 ASN F 149
REMARK 465 ARG F 150
REMARK 465 VAL F 151
REMARK 465 GLU F 152
REMARK 465 ALA F 153
REMARK 465 GLU F 154
REMARK 465 GLU F 155
REMARK 465 ALA F 156
REMARK 465 ARG F 157
REMARK 465 LEU F 158
REMARK 465 SER F 159
REMARK 465 ASP F 160
REMARK 465 LEU F 161
REMARK 465 ILE F 162
REMARK 465 THR F 163
REMARK 465 GLY F 164
REMARK 465 PHE F 165
REMARK 465 VAL F 166
REMARK 465 ASP F 167
REMARK 465 PRO F 168
REMARK 465 ASN F 169
REMARK 465 ALA F 170
REMARK 465 GLU F 171
REMARK 465 GLU F 172
REMARK 465 ASP F 173
REMARK 465 LEU F 174
REMARK 465 ALA F 175
REMARK 465 PRO F 176
REMARK 465 THR F 177
REMARK 465 ALA F 178
REMARK 465 THR F 179
REMARK 465 HIS F 180
REMARK 465 VAL F 181
REMARK 465 GLY F 182
REMARK 465 SER F 183
REMARK 465 GLU F 184
REMARK 465 LEU F 185
REMARK 465 SER F 186
REMARK 465 GLN F 187
REMARK 465 GLU F 188
REMARK 465 ASP F 189
REMARK 465 LEU F 190
REMARK 465 ASP F 191
REMARK 465 ASP F 192
REMARK 465 ASP F 193
REMARK 465 GLU F 194
REMARK 465 ASP F 195
REMARK 465 GLU F 196
REMARK 465 ASP F 197
REMARK 465 GLU F 198
REMARK 465 GLU F 199
REMARK 465 ASP F 200
REMARK 465 GLY F 201
REMARK 465 ASP F 202
REMARK 465 ASP F 203
REMARK 465 ASP F 204
REMARK 465 SER F 205
REMARK 465 ALA F 206
REMARK 465 ASP F 207
REMARK 465 ASP F 208
REMARK 465 ASP F 209
REMARK 465 ASN F 210
REMARK 465 SER F 211
REMARK 465 ILE F 212
REMARK 465 ASP F 213
REMARK 465 PRO F 214
REMARK 465 GLU F 215
REMARK 465 LEU F 216
REMARK 465 ALA F 217
REMARK 465 ARG F 218
REMARK 465 GLU F 219
REMARK 465 LYS F 220
REMARK 465 PHE F 221
REMARK 465 ALA F 222
REMARK 465 GLU F 223
REMARK 465 LEU F 224
REMARK 465 ARG F 225
REMARK 465 ALA F 226
REMARK 465 GLN F 227
REMARK 465 TYR F 228
REMARK 465 VAL F 229
REMARK 465 VAL F 230
REMARK 465 THR F 231
REMARK 465 ARG F 232
REMARK 465 ASP F 233
REMARK 465 THR F 234
REMARK 465 ILE F 235
REMARK 465 LYS F 236
REMARK 465 ALA F 237
REMARK 465 LYS F 238
REMARK 465 GLY F 239
REMARK 465 ARG F 240
REMARK 465 SER F 241
REMARK 465 HIS F 242
REMARK 465 ALA F 243
REMARK 465 THR F 244
REMARK 465 ALA F 245
REMARK 465 GLN F 246
REMARK 465 GLU F 247
REMARK 465 GLU F 248
REMARK 465 ILE F 249
REMARK 465 LEU F 250
REMARK 465 LYS F 251
REMARK 465 LEU F 252
REMARK 465 SER F 253
REMARK 465 GLU F 254
REMARK 465 VAL F 255
REMARK 465 PHE F 256
REMARK 465 LYS F 257
REMARK 465 GLN F 258
REMARK 465 PHE F 259
REMARK 465 ARG F 260
REMARK 465 LEU F 261
REMARK 465 PHE I 18
REMARK 465 ASN I 19
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 PHE A 8 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS A 160 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 161 OG
REMARK 470 GLU A 162 CG CD OE1 OE2
REMARK 470 ASP A 164 CG OD1 OD2
REMARK 470 ARG A 166 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 191 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 192 CG1 CG2
REMARK 470 GLU A 193 CG CD OE1 OE2
REMARK 470 GLN A 194 CG CD OE1 NE2
REMARK 470 ARG A 195 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 232 CG1 CG2
REMARK 470 ASP A 233 CG OD1 OD2
REMARK 470 LEU A 234 CG CD1 CD2
REMARK 470 GLU A 235 CG CD OE1 OE2
REMARK 470 ARG B 158 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 171 CG CD1 CD2
REMARK 470 VAL B 232 CG1 CG2
REMARK 470 ASP B 233 CG OD1 OD2
REMARK 470 LEU B 234 CG CD1 CD2
REMARK 470 GLU C 111 CG CD OE1 OE2
REMARK 470 LYS C 236 CG CD CE NZ
REMARK 470 ASP C 624 CG OD1 OD2
REMARK 470 GLU C 631 CG CD OE1 OE2
REMARK 470 LYS C 890 CG CD CE NZ
REMARK 470 PHE C1164 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE D1134 CG1 CG2 CD1
REMARK 470 THR D1135 OG1 CG2
REMARK 470 TRP D1193 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D1193 CZ3 CH2
REMARK 470 LEU F 269 CG CD1 CD2
REMARK 470 LYS F 371 CG CD CE NZ
REMARK 470 GLU F 481 CG CD OE1 OE2
REMARK 470 ASP I 9 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N GLY I 1 CG ASP I 9 1.33
REMARK 500 N GLU C 111 O HOH C 1501 2.08
REMARK 500 NE ARG C 368 O HOH C 1502 2.08
REMARK 500 OG SER D 957 O GLU D 1009 2.11
REMARK 500 O ASP C 199 N ARG C 201 2.11
REMARK 500 NZ LYS C 118 O LEU C 487 2.12
REMARK 500 OE2 GLU F 284 NZ LYS F 359 2.13
REMARK 500 O LYS A 95 NH2 ARG A 148 2.14
REMARK 500 O THR I 7 N SER I 14 2.15
REMARK 500 OG1 THR D 514 O ALA D 595 2.15
REMARK 500 OE1 GLU C 231 NH2 ARG C 332 2.16
REMARK 500 OG SER D 230 ND2 ASN D 232 2.17
REMARK 500 O LEU D 1344 N GLY D 1346 2.18
REMARK 500 O PHE A 231 O HOH A 301 2.18
REMARK 500 OG1 THR A 22 O THR A 207 2.19
REMARK 500 OE1 GLU A 215 NH1 ARG A 219 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 A 14 -61.08 -123.82
REMARK 500 PRO A 30 79.92 -68.61
REMARK 500 LYS A 125 80.52 -157.72
REMARK 500 HIS A 160 -39.63 -133.53
REMARK 500 GLU A 162 -15.63 76.09
REMARK 500 GLU A 163 28.55 32.57
REMARK 500 SER A 178 84.68 -155.34
REMARK 500 LEU A 234 146.06 178.47
REMARK 500 THR B 57 -60.61 -101.20
REMARK 500 HIS B 66 144.55 -171.46
REMARK 500 LYS B 125 78.67 -113.49
REMARK 500 ASP B 135 -151.47 -73.30
REMARK 500 ASN B 137 -57.47 -125.44
REMARK 500 PHE B 231 -145.69 -150.53
REMARK 500 ASP B 233 -173.22 -172.96
REMARK 500 ARG C 10 118.29 -160.63
REMARK 500 SER C 63 -1.99 66.58
REMARK 500 VAL C 71 -61.67 -94.86
REMARK 500 PRO C 153 -179.92 -67.35
REMARK 500 HIS C 165 -2.31 81.00
REMARK 500 ASP C 199 -178.29 -36.52
REMARK 500 ARG C 200 13.62 -54.13
REMARK 500 ARG C 201 -162.66 -74.61
REMARK 500 LEU C 204 86.23 56.32
REMARK 500 PRO C 205 148.08 -36.92
REMARK 500 ASP C 234 -29.68 73.67
REMARK 500 ASN C 235 -178.50 160.09
REMARK 500 LYS C 236 71.98 58.78
REMARK 500 PHE C 390 30.16 -140.28
REMARK 500 SER C 398 178.65 -56.05
REMARK 500 LEU C 484 -157.93 -80.53
REMARK 500 ASP C 485 -13.01 -46.68
REMARK 500 PRO C 489 47.61 -73.60
REMARK 500 GLN C 490 -35.83 -130.84
REMARK 500 ASN C 518 1.31 82.31
REMARK 500 ASN C 573 154.82 -46.90
REMARK 500 TYR C 584 -74.90 -84.97
REMARK 500 THR C 595 -65.53 -94.29
REMARK 500 SER C 621 -179.67 -170.60
REMARK 500 GLU C 625 -168.40 -127.16
REMARK 500 GLU C 626 15.49 54.84
REMARK 500 MET C 805 142.38 -170.56
REMARK 500 ALA C 986 -70.14 -40.33
REMARK 500 GLU C1006 -11.06 77.76
REMARK 500 ARG C1059 -169.93 -79.42
REMARK 500 GLU C1137 175.59 176.09
REMARK 500 ARG C1223 80.57 60.74
REMARK 500 PRO C1224 143.08 -37.18
REMARK 500 ASP C1297 64.27 67.46
REMARK 500 GLU C1340 -167.21 -103.06
REMARK 500
REMARK 500 THIS ENTRY HAS 97 RAMACHANDRAN OUTLIERS.
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 ASP B 135 GLU B 136 -127.92
REMARK 500 PHE B 231 VAL B 232 -125.00
REMARK 500 ILE C 198 ASP C 199 -139.57
REMARK 500 ASP C 234 ASN C 235 149.49
REMARK 500 GLU C 985 ALA C 986 -149.80
REMARK 500 GLU C 1340 ASP C 1341 -146.29
REMARK 500 VAL D 357 GLY D 358 149.34
REMARK 500 HIS D 1023 THR D 1024 -116.99
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 ZN D1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 70 SG
REMARK 620 2 CYS D 72 SG 89.3
REMARK 620 3 CYS D 85 SG 116.7 99.5
REMARK 620 4 CYS D 88 SG 83.7 97.4 153.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 460 OD1
REMARK 620 2 ASP D 462 OD2 92.7
REMARK 620 3 ASP D 464 OD1 117.9 74.2
REMARK 620 4 ASP D 464 OD2 82.3 104.4 46.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 814 SG
REMARK 620 2 CYS D 888 SG 102.1
REMARK 620 3 CYS D 895 SG 95.7 113.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE D 1504
DBREF 6N61 A 1 234 UNP P0A7Z4 RPOA_ECOLI 1 234
DBREF 6N61 B 1 234 UNP P0A7Z4 RPOA_ECOLI 1 234
DBREF 6N61 C 1 1342 UNP P0A8V2 RPOB_ECOLI 1 1342
DBREF 6N61 D 2 1407 UNP P0A8T7 RPOC_ECOLI 2 1407
DBREF 6N61 E 1 90 UNP P0A800 RPOZ_ECOLI 1 90
DBREF 6N61 F 1 613 UNP Q0P6L9 Q0P6L9_ECOLX 1 613
DBREF 6N61 N 1 29 PDB 6N61 6N61 1 29
DBREF 6N61 T 1 24 PDB 6N61 6N61 1 24
DBREF1 6N61 I 1 19 UNP A0A096YQF1_BURTA
DBREF2 6N61 I A0A096YQF1 29 47
SEQADV 6N61 GLU A 235 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 VAL A 236 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 LEU A 237 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 PHE A 238 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 GLN A 239 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 GLU B 235 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 VAL B 236 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 LEU B 237 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 PHE B 238 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 GLN B 239 UNP P0A7Z4 EXPRESSION TAG
SEQADV 6N61 VAL D 1 UNP P0A8T7 EXPRESSION TAG
SEQADV 6N61 LEU D 1408 UNP P0A8T7 EXPRESSION TAG
SEQADV 6N61 GLU D 1409 UNP P0A8T7 EXPRESSION TAG
SEQADV 6N61 ASN F 149 UNP Q0P6L9 ASP 149 CONFLICT
SEQRES 1 A 239 MET GLN GLY SER VAL THR GLU PHE LEU LYS PRO ARG LEU
SEQRES 2 A 239 VAL ASP ILE GLU GLN VAL SER SER THR HIS ALA LYS VAL
SEQRES 3 A 239 THR LEU GLU PRO LEU GLU ARG GLY PHE GLY HIS THR LEU
SEQRES 4 A 239 GLY ASN ALA LEU ARG ARG ILE LEU LEU SER SER MET PRO
SEQRES 5 A 239 GLY CYS ALA VAL THR GLU VAL GLU ILE ASP GLY VAL LEU
SEQRES 6 A 239 HIS GLU TYR SER THR LYS GLU GLY VAL GLN GLU ASP ILE
SEQRES 7 A 239 LEU GLU ILE LEU LEU ASN LEU LYS GLY LEU ALA VAL ARG
SEQRES 8 A 239 VAL GLN GLY LYS ASP GLU VAL ILE LEU THR LEU ASN LYS
SEQRES 9 A 239 SER GLY ILE GLY PRO VAL THR ALA ALA ASP ILE THR HIS
SEQRES 10 A 239 ASP GLY ASP VAL GLU ILE VAL LYS PRO GLN HIS VAL ILE
SEQRES 11 A 239 CYS HIS LEU THR ASP GLU ASN ALA SER ILE SER MET ARG
SEQRES 12 A 239 ILE LYS VAL GLN ARG GLY ARG GLY TYR VAL PRO ALA SER
SEQRES 13 A 239 THR ARG ILE HIS SER GLU GLU ASP GLU ARG PRO ILE GLY
SEQRES 14 A 239 ARG LEU LEU VAL ASP ALA CYS TYR SER PRO VAL GLU ARG
SEQRES 15 A 239 ILE ALA TYR ASN VAL GLU ALA ALA ARG VAL GLU GLN ARG
SEQRES 16 A 239 THR ASP LEU ASP LYS LEU VAL ILE GLU MET GLU THR ASN
SEQRES 17 A 239 GLY THR ILE ASP PRO GLU GLU ALA ILE ARG ARG ALA ALA
SEQRES 18 A 239 THR ILE LEU ALA GLU GLN LEU GLU ALA PHE VAL ASP LEU
SEQRES 19 A 239 GLU VAL LEU PHE GLN
SEQRES 1 B 239 MET GLN GLY SER VAL THR GLU PHE LEU LYS PRO ARG LEU
SEQRES 2 B 239 VAL ASP ILE GLU GLN VAL SER SER THR HIS ALA LYS VAL
SEQRES 3 B 239 THR LEU GLU PRO LEU GLU ARG GLY PHE GLY HIS THR LEU
SEQRES 4 B 239 GLY ASN ALA LEU ARG ARG ILE LEU LEU SER SER MET PRO
SEQRES 5 B 239 GLY CYS ALA VAL THR GLU VAL GLU ILE ASP GLY VAL LEU
SEQRES 6 B 239 HIS GLU TYR SER THR LYS GLU GLY VAL GLN GLU ASP ILE
SEQRES 7 B 239 LEU GLU ILE LEU LEU ASN LEU LYS GLY LEU ALA VAL ARG
SEQRES 8 B 239 VAL GLN GLY LYS ASP GLU VAL ILE LEU THR LEU ASN LYS
SEQRES 9 B 239 SER GLY ILE GLY PRO VAL THR ALA ALA ASP ILE THR HIS
SEQRES 10 B 239 ASP GLY ASP VAL GLU ILE VAL LYS PRO GLN HIS VAL ILE
SEQRES 11 B 239 CYS HIS LEU THR ASP GLU ASN ALA SER ILE SER MET ARG
SEQRES 12 B 239 ILE LYS VAL GLN ARG GLY ARG GLY TYR VAL PRO ALA SER
SEQRES 13 B 239 THR ARG ILE HIS SER GLU GLU ASP GLU ARG PRO ILE GLY
SEQRES 14 B 239 ARG LEU LEU VAL ASP ALA CYS TYR SER PRO VAL GLU ARG
SEQRES 15 B 239 ILE ALA TYR ASN VAL GLU ALA ALA ARG VAL GLU GLN ARG
SEQRES 16 B 239 THR ASP LEU ASP LYS LEU VAL ILE GLU MET GLU THR ASN
SEQRES 17 B 239 GLY THR ILE ASP PRO GLU GLU ALA ILE ARG ARG ALA ALA
SEQRES 18 B 239 THR ILE LEU ALA GLU GLN LEU GLU ALA PHE VAL ASP LEU
SEQRES 19 B 239 GLU VAL LEU PHE GLN
SEQRES 1 C 1342 MET VAL TYR SER TYR THR GLU LYS LYS ARG ILE ARG LYS
SEQRES 2 C 1342 ASP PHE GLY LYS ARG PRO GLN VAL LEU ASP VAL PRO TYR
SEQRES 3 C 1342 LEU LEU SER ILE GLN LEU ASP SER PHE GLN LYS PHE ILE
SEQRES 4 C 1342 GLU GLN ASP PRO GLU GLY GLN TYR GLY LEU GLU ALA ALA
SEQRES 5 C 1342 PHE ARG SER VAL PHE PRO ILE GLN SER TYR SER GLY ASN
SEQRES 6 C 1342 SER GLU LEU GLN TYR VAL SER TYR ARG LEU GLY GLU PRO
SEQRES 7 C 1342 VAL PHE ASP VAL GLN GLU CYS GLN ILE ARG GLY VAL THR
SEQRES 8 C 1342 TYR SER ALA PRO LEU ARG VAL LYS LEU ARG LEU VAL ILE
SEQRES 9 C 1342 TYR GLU ARG GLU ALA PRO GLU GLY THR VAL LYS ASP ILE
SEQRES 10 C 1342 LYS GLU GLN GLU VAL TYR MET GLY GLU ILE PRO LEU MET
SEQRES 11 C 1342 THR ASP ASN GLY THR PHE VAL ILE ASN GLY THR GLU ARG
SEQRES 12 C 1342 VAL ILE VAL SER GLN LEU HIS ARG SER PRO GLY VAL PHE
SEQRES 13 C 1342 PHE ASP SER ASP LYS GLY LYS THR HIS SER SER GLY LYS
SEQRES 14 C 1342 VAL LEU TYR ASN ALA ARG ILE ILE PRO TYR ARG GLY SER
SEQRES 15 C 1342 TRP LEU ASP PHE GLU PHE ASP PRO LYS ASP ASN LEU PHE
SEQRES 16 C 1342 VAL ARG ILE ASP ARG ARG ARG LYS LEU PRO ALA THR ILE
SEQRES 17 C 1342 ILE LEU ARG ALA LEU ASN TYR THR THR GLU GLN ILE LEU
SEQRES 18 C 1342 ASP LEU PHE PHE GLU LYS VAL ILE PHE GLU ILE ARG ASP
SEQRES 19 C 1342 ASN LYS LEU GLN MET GLU LEU VAL PRO GLU ARG LEU ARG
SEQRES 20 C 1342 GLY GLU THR ALA SER PHE ASP ILE GLU ALA ASN GLY LYS
SEQRES 21 C 1342 VAL TYR VAL GLU LYS GLY ARG ARG ILE THR ALA ARG HIS
SEQRES 22 C 1342 ILE ARG GLN LEU GLU LYS ASP ASP VAL LYS LEU ILE GLU
SEQRES 23 C 1342 VAL PRO VAL GLU TYR ILE ALA GLY LYS VAL VAL ALA LYS
SEQRES 24 C 1342 ASP TYR ILE ASP GLU SER THR GLY GLU LEU ILE CYS ALA
SEQRES 25 C 1342 ALA ASN MET GLU LEU SER LEU ASP LEU LEU ALA LYS LEU
SEQRES 26 C 1342 SER GLN SER GLY HIS LYS ARG ILE GLU THR LEU PHE THR
SEQRES 27 C 1342 ASN ASP LEU ASP HIS GLY PRO TYR ILE SER GLU THR LEU
SEQRES 28 C 1342 ARG VAL ASP PRO THR ASN ASP ARG LEU SER ALA LEU VAL
SEQRES 29 C 1342 GLU ILE TYR ARG MET MET ARG PRO GLY GLU PRO PRO THR
SEQRES 30 C 1342 ARG GLU ALA ALA GLU SER LEU PHE GLU ASN LEU PHE PHE
SEQRES 31 C 1342 SER GLU ASP ARG TYR ASP LEU SER ALA VAL GLY ARG MET
SEQRES 32 C 1342 LYS PHE ASN ARG SER LEU LEU ARG GLU GLU ILE GLU GLY
SEQRES 33 C 1342 SER GLY ILE LEU SER LYS ASP ASP ILE ILE ASP VAL MET
SEQRES 34 C 1342 LYS LYS LEU ILE ASP ILE ARG ASN GLY LYS GLY GLU VAL
SEQRES 35 C 1342 ASP ASP ILE ASP HIS LEU GLY ASN ARG ARG ILE ARG SER
SEQRES 36 C 1342 VAL GLY GLU MET ALA GLU ASN GLN PHE ARG VAL GLY LEU
SEQRES 37 C 1342 VAL ARG VAL GLU ARG ALA VAL LYS GLU ARG LEU SER LEU
SEQRES 38 C 1342 GLY ASP LEU ASP THR LEU MET PRO GLN ASP MET ILE ASN
SEQRES 39 C 1342 ALA LYS PRO ILE SER ALA ALA VAL LYS GLU PHE PHE GLY
SEQRES 40 C 1342 SER SER GLN LEU SER GLN PHE MET ASP GLN ASN ASN PRO
SEQRES 41 C 1342 LEU SER GLU ILE THR HIS LYS ARG ARG ILE SER ALA LEU
SEQRES 42 C 1342 GLY PRO GLY GLY LEU THR ARG GLU ARG ALA GLY PHE GLU
SEQRES 43 C 1342 VAL ARG ASP VAL HIS PRO THR HIS TYR GLY ARG VAL CYS
SEQRES 44 C 1342 PRO ILE GLU THR PRO GLU GLY PRO ASN ILE GLY LEU ILE
SEQRES 45 C 1342 ASN SER LEU SER VAL TYR ALA GLN THR ASN GLU TYR GLY
SEQRES 46 C 1342 PHE LEU GLU THR PRO TYR ARG LYS VAL THR ASP GLY VAL
SEQRES 47 C 1342 VAL THR ASP GLU ILE HIS TYR LEU SER ALA ILE GLU GLU
SEQRES 48 C 1342 GLY ASN TYR VAL ILE ALA GLN ALA ASN SER ASN LEU ASP
SEQRES 49 C 1342 GLU GLU GLY HIS PHE VAL GLU ASP LEU VAL THR CYS ARG
SEQRES 50 C 1342 SER LYS GLY GLU SER SER LEU PHE SER ARG ASP GLN VAL
SEQRES 51 C 1342 ASP TYR MET ASP VAL SER THR GLN GLN VAL VAL SER VAL
SEQRES 52 C 1342 GLY ALA SER LEU ILE PRO PHE LEU GLU HIS ASP ASP ALA
SEQRES 53 C 1342 ASN ARG ALA LEU MET GLY ALA ASN MET GLN ARG GLN ALA
SEQRES 54 C 1342 VAL PRO THR LEU ARG ALA ASP LYS PRO LEU VAL GLY THR
SEQRES 55 C 1342 GLY MET GLU ARG ALA VAL ALA VAL ASP SER GLY VAL THR
SEQRES 56 C 1342 ALA VAL ALA LYS ARG GLY GLY VAL VAL GLN TYR VAL ASP
SEQRES 57 C 1342 ALA SER ARG ILE VAL ILE LYS VAL ASN GLU ASP GLU MET
SEQRES 58 C 1342 TYR PRO GLY GLU ALA GLY ILE ASP ILE TYR ASN LEU THR
SEQRES 59 C 1342 LYS TYR THR ARG SER ASN GLN ASN THR CYS ILE ASN GLN
SEQRES 60 C 1342 MET PRO CYS VAL SER LEU GLY GLU PRO VAL GLU ARG GLY
SEQRES 61 C 1342 ASP VAL LEU ALA ASP GLY PRO SER THR ASP LEU GLY GLU
SEQRES 62 C 1342 LEU ALA LEU GLY GLN ASN MET ARG VAL ALA PHE MET PRO
SEQRES 63 C 1342 TRP ASN GLY TYR ASN PHE GLU ASP SER ILE LEU VAL SER
SEQRES 64 C 1342 GLU ARG VAL VAL GLN GLU ASP ARG PHE THR THR ILE HIS
SEQRES 65 C 1342 ILE GLN GLU LEU ALA CYS VAL SER ARG ASP THR LYS LEU
SEQRES 66 C 1342 GLY PRO GLU GLU ILE THR ALA ASP ILE PRO ASN VAL GLY
SEQRES 67 C 1342 GLU ALA ALA LEU SER LYS LEU ASP GLU SER GLY ILE VAL
SEQRES 68 C 1342 TYR ILE GLY ALA GLU VAL THR GLY GLY ASP ILE LEU VAL
SEQRES 69 C 1342 GLY LYS VAL THR PRO LYS GLY GLU THR GLN LEU THR PRO
SEQRES 70 C 1342 GLU GLU LYS LEU LEU ARG ALA ILE PHE GLY GLU LYS ALA
SEQRES 71 C 1342 SER ASP VAL LYS ASP SER SER LEU ARG VAL PRO ASN GLY
SEQRES 72 C 1342 VAL SER GLY THR VAL ILE ASP VAL GLN VAL PHE THR ARG
SEQRES 73 C 1342 ASP GLY VAL GLU LYS ASP LYS ARG ALA LEU GLU ILE GLU
SEQRES 74 C 1342 GLU MET GLN LEU LYS GLN ALA LYS LYS ASP LEU SER GLU
SEQRES 75 C 1342 GLU LEU GLN ILE LEU GLU ALA GLY LEU PHE SER ARG ILE
SEQRES 76 C 1342 ARG ALA VAL LEU VAL ALA GLY GLY VAL GLU ALA GLU LYS
SEQRES 77 C 1342 LEU ASP LYS LEU PRO ARG ASP ARG TRP LEU GLU LEU GLY
SEQRES 78 C 1342 LEU THR ASP GLU GLU LYS GLN ASN GLN LEU GLU GLN LEU
SEQRES 79 C 1342 ALA GLU GLN TYR ASP GLU LEU LYS HIS GLU PHE GLU LYS
SEQRES 80 C 1342 LYS LEU GLU ALA LYS ARG ARG LYS ILE THR GLN GLY ASP
SEQRES 81 C 1342 ASP LEU ALA PRO GLY VAL LEU LYS ILE VAL LYS VAL TYR
SEQRES 82 C 1342 LEU ALA VAL LYS ARG ARG ILE GLN PRO GLY ASP LYS MET
SEQRES 83 C 1342 ALA GLY ARG HIS GLY ASN LYS GLY VAL ILE SER LYS ILE
SEQRES 84 C 1342 ASN PRO ILE GLU ASP MET PRO TYR ASP GLU ASN GLY THR
SEQRES 85 C 1342 PRO VAL ASP ILE VAL LEU ASN PRO LEU GLY VAL PRO SER
SEQRES 86 C 1342 ARG MET ASN ILE GLY GLN ILE LEU GLU THR HIS LEU GLY
SEQRES 87 C 1342 MET ALA ALA LYS GLY ILE GLY ASP LYS ILE ASN ALA MET
SEQRES 88 C 1342 LEU LYS GLN GLN GLN GLU VAL ALA LYS LEU ARG GLU PHE
SEQRES 89 C 1342 ILE GLN ARG ALA TYR ASP LEU GLY ALA ASP VAL ARG GLN
SEQRES 90 C 1342 LYS VAL ASP LEU SER THR PHE SER ASP GLU GLU VAL MET
SEQRES 91 C 1342 ARG LEU ALA GLU ASN LEU ARG LYS GLY MET PRO ILE ALA
SEQRES 92 C 1342 THR PRO VAL PHE ASP GLY ALA LYS GLU ALA GLU ILE LYS
SEQRES 93 C 1342 GLU LEU LEU LYS LEU GLY ASP LEU PRO THR SER GLY GLN
SEQRES 94 C 1342 ILE ARG LEU TYR ASP GLY ARG THR GLY GLU GLN PHE GLU
SEQRES 95 C 1342 ARG PRO VAL THR VAL GLY TYR MET TYR MET LEU LYS LEU
SEQRES 96 C 1342 ASN HIS LEU VAL ASP ASP LYS MET HIS ALA ARG SER THR
SEQRES 97 C 1342 GLY SER TYR SER LEU VAL THR GLN GLN PRO LEU GLY GLY
SEQRES 98 C 1342 LYS ALA GLN PHE GLY GLY GLN ARG PHE GLY GLU MET GLU
SEQRES 99 C 1342 VAL TRP ALA LEU GLU ALA TYR GLY ALA ALA TYR THR LEU
SEQRES 100 C 1342 GLN GLU MET LEU THR VAL LYS SER ASP ASP VAL ASN GLY
SEQRES 101 C 1342 ARG THR LYS MET TYR LYS ASN ILE VAL ASP GLY ASN HIS
SEQRES 102 C 1342 GLN MET GLU PRO GLY MET PRO GLU SER PHE ASN VAL LEU
SEQRES 103 C 1342 LEU LYS GLU ILE ARG SER LEU GLY ILE ASN ILE GLU LEU
SEQRES 104 C 1342 GLU ASP GLU
SEQRES 1 D 1409 VAL LYS ASP LEU LEU LYS PHE LEU LYS ALA GLN THR LYS
SEQRES 2 D 1409 THR GLU GLU PHE ASP ALA ILE LYS ILE ALA LEU ALA SER
SEQRES 3 D 1409 PRO ASP MET ILE ARG SER TRP SER PHE GLY GLU VAL LYS
SEQRES 4 D 1409 LYS PRO GLU THR ILE ASN TYR ARG THR PHE LYS PRO GLU
SEQRES 5 D 1409 ARG ASP GLY LEU PHE CYS ALA ARG ILE PHE GLY PRO VAL
SEQRES 6 D 1409 LYS ASP TYR GLU CYS LEU CYS GLY LYS TYR LYS ARG LEU
SEQRES 7 D 1409 LYS HIS ARG GLY VAL ILE CYS GLU LYS CYS GLY VAL GLU
SEQRES 8 D 1409 VAL THR GLN THR LYS VAL ARG ARG GLU ARG MET GLY HIS
SEQRES 9 D 1409 ILE GLU LEU ALA SER PRO THR ALA HIS ILE TRP PHE LEU
SEQRES 10 D 1409 LYS SER LEU PRO SER ARG ILE GLY LEU LEU LEU ASP MET
SEQRES 11 D 1409 PRO LEU ARG ASP ILE GLU ARG VAL LEU TYR PHE GLU SER
SEQRES 12 D 1409 TYR VAL VAL ILE GLU GLY GLY MET THR ASN LEU GLU ARG
SEQRES 13 D 1409 GLN GLN ILE LEU THR GLU GLU GLN TYR LEU ASP ALA LEU
SEQRES 14 D 1409 GLU GLU PHE GLY ASP GLU PHE ASP ALA LYS MET GLY ALA
SEQRES 15 D 1409 GLU ALA ILE GLN ALA LEU LEU LYS SER MET ASP LEU GLU
SEQRES 16 D 1409 GLN GLU CYS GLU GLN LEU ARG GLU GLU LEU ASN GLU THR
SEQRES 17 D 1409 ASN SER GLU THR LYS ARG LYS LYS LEU THR LYS ARG ILE
SEQRES 18 D 1409 LYS LEU LEU GLU ALA PHE VAL GLN SER GLY ASN LYS PRO
SEQRES 19 D 1409 GLU TRP MET ILE LEU THR VAL LEU PRO VAL LEU PRO PRO
SEQRES 20 D 1409 ASP LEU ARG PRO LEU VAL PRO LEU ASP GLY GLY ARG PHE
SEQRES 21 D 1409 ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG VAL ILE
SEQRES 22 D 1409 ASN ARG ASN ASN ARG LEU LYS ARG LEU LEU ASP LEU ALA
SEQRES 23 D 1409 ALA PRO ASP ILE ILE VAL ARG ASN GLU LYS ARG MET LEU
SEQRES 24 D 1409 GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY ARG ARG
SEQRES 25 D 1409 GLY ARG ALA ILE THR GLY SER ASN LYS ARG PRO LEU LYS
SEQRES 26 D 1409 SER LEU ALA ASP MET ILE LYS GLY LYS GLN GLY ARG PHE
SEQRES 27 D 1409 ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP TYR SER GLY
SEQRES 28 D 1409 ARG SER VAL ILE THR VAL GLY PRO TYR LEU ARG LEU HIS
SEQRES 29 D 1409 GLN CYS GLY LEU PRO LYS LYS MET ALA LEU GLU LEU PHE
SEQRES 30 D 1409 LYS PRO PHE ILE TYR GLY LYS LEU GLU LEU ARG GLY LEU
SEQRES 31 D 1409 ALA THR THR ILE LYS ALA ALA LYS LYS MET VAL GLU ARG
SEQRES 32 D 1409 GLU GLU ALA VAL VAL TRP ASP ILE LEU ASP GLU VAL ILE
SEQRES 33 D 1409 ARG GLU HIS PRO VAL LEU LEU ASN ARG ALA PRO THR LEU
SEQRES 34 D 1409 HIS ARG LEU GLY ILE GLN ALA PHE GLU PRO VAL LEU ILE
SEQRES 35 D 1409 GLU GLY LYS ALA ILE GLN LEU HIS PRO LEU VAL CYS ALA
SEQRES 36 D 1409 ALA TYR ASN ALA ASP PHE ASP GLY ASP GLN MET ALA VAL
SEQRES 37 D 1409 HIS VAL PRO LEU THR LEU GLU ALA GLN LEU GLU ALA ARG
SEQRES 38 D 1409 ALA LEU MET MET SER THR ASN ASN ILE LEU SER PRO ALA
SEQRES 39 D 1409 ASN GLY GLU PRO ILE ILE VAL PRO SER GLN ASP VAL VAL
SEQRES 40 D 1409 LEU GLY LEU TYR TYR MET THR ARG ASP CYS VAL ASN ALA
SEQRES 41 D 1409 LYS GLY GLU GLY MET VAL LEU THR GLY PRO LYS GLU ALA
SEQRES 42 D 1409 GLU ARG LEU TYR ARG SER GLY LEU ALA SER LEU HIS ALA
SEQRES 43 D 1409 ARG VAL LYS VAL ARG ILE THR GLU TYR GLU LYS ASP ALA
SEQRES 44 D 1409 ASN GLY GLU LEU VAL ALA LYS THR SER LEU LYS ASP THR
SEQRES 45 D 1409 THR VAL GLY ARG ALA ILE LEU TRP MET ILE VAL PRO LYS
SEQRES 46 D 1409 GLY LEU PRO TYR SER ILE VAL ASN GLN ALA LEU GLY LYS
SEQRES 47 D 1409 LYS ALA ILE SER LYS MET LEU ASN THR CYS TYR ARG ILE
SEQRES 48 D 1409 LEU GLY LEU LYS PRO THR VAL ILE PHE ALA ASP GLN ILE
SEQRES 49 D 1409 MET TYR THR GLY PHE ALA TYR ALA ALA ARG SER GLY ALA
SEQRES 50 D 1409 SER VAL GLY ILE ASP ASP MET VAL ILE PRO GLU LYS LYS
SEQRES 51 D 1409 HIS GLU ILE ILE SER GLU ALA GLU ALA GLU VAL ALA GLU
SEQRES 52 D 1409 ILE GLN GLU GLN PHE GLN SER GLY LEU VAL THR ALA GLY
SEQRES 53 D 1409 GLU ARG TYR ASN LYS VAL ILE ASP ILE TRP ALA ALA ALA
SEQRES 54 D 1409 ASN ASP ARG VAL SER LYS ALA MET MET ASP ASN LEU GLN
SEQRES 55 D 1409 THR GLU THR VAL ILE ASN ARG ASP GLY GLN GLU GLU LYS
SEQRES 56 D 1409 GLN VAL SER PHE ASN SER ILE TYR MET MET ALA ASP SER
SEQRES 57 D 1409 GLY ALA ARG GLY SER ALA ALA GLN ILE ARG GLN LEU ALA
SEQRES 58 D 1409 GLY MET ARG GLY LEU MET ALA LYS PRO ASP GLY SER ILE
SEQRES 59 D 1409 ILE GLU THR PRO ILE THR ALA ASN PHE ARG GLU GLY LEU
SEQRES 60 D 1409 ASN VAL LEU GLN TYR PHE ILE SER THR HIS GLY ALA ARG
SEQRES 61 D 1409 LYS GLY LEU ALA ASP THR ALA LEU LYS THR ALA ASN SER
SEQRES 62 D 1409 GLY TYR LEU THR ARG ARG LEU VAL ASP VAL ALA GLN ASP
SEQRES 63 D 1409 LEU VAL VAL THR GLU ASP ASP CYS GLY THR HIS GLU GLY
SEQRES 64 D 1409 ILE MET MET THR PRO VAL ILE GLU GLY GLY ASP VAL LYS
SEQRES 65 D 1409 GLU PRO LEU ARG ASP ARG VAL LEU GLY ARG VAL THR ALA
SEQRES 66 D 1409 GLU ASP VAL LEU LYS PRO GLY THR ALA ASP ILE LEU VAL
SEQRES 67 D 1409 PRO ARG ASN THR LEU LEU HIS GLU GLN TRP CYS ASP LEU
SEQRES 68 D 1409 LEU GLU GLU ASN SER VAL ASP ALA VAL LYS VAL ARG SER
SEQRES 69 D 1409 VAL VAL SER CYS ASP THR ASP PHE GLY VAL CYS ALA HIS
SEQRES 70 D 1409 CYS TYR GLY ARG ASP LEU ALA ARG GLY HIS ILE ILE ASN
SEQRES 71 D 1409 LYS GLY GLU ALA ILE GLY VAL ILE ALA ALA GLN SER ILE
SEQRES 72 D 1409 GLY GLU PRO GLY THR GLN LEU THR MET ARG THR PHE HIS
SEQRES 73 D 1409 ILE GLY GLY ALA ALA SER ARG ALA ALA ALA GLU SER SER
SEQRES 74 D 1409 ILE GLN VAL LYS ASN LYS GLY SER ILE LYS LEU SER ASN
SEQRES 75 D 1409 VAL LYS SER VAL VAL ASN SER SER GLY LYS LEU VAL ILE
SEQRES 76 D 1409 THR SER ARG ASN THR GLU LEU LYS LEU ILE ASP GLU PHE
SEQRES 77 D 1409 GLY ARG THR LYS GLU SER TYR LYS VAL PRO TYR GLY ALA
SEQRES 78 D 1409 VAL LEU ALA LYS GLY ASP GLY GLU GLN VAL ALA GLY GLY
SEQRES 79 D 1409 GLU THR VAL ALA ASN TRP ASP PRO HIS THR MET PRO VAL
SEQRES 80 D 1409 ILE THR GLU VAL SER GLY PHE VAL ARG PHE THR ASP MET
SEQRES 81 D 1409 ILE ASP GLY GLN THR ILE THR ARG GLN THR ASP GLU LEU
SEQRES 82 D 1409 THR GLY LEU SER SER LEU VAL VAL LEU ASP SER ALA GLU
SEQRES 83 D 1409 ARG THR ALA GLY GLY LYS ASP LEU ARG PRO ALA LEU LYS
SEQRES 84 D 1409 ILE VAL ASP ALA GLN GLY ASN ASP VAL LEU ILE PRO GLY
SEQRES 85 D 1409 THR ASP MET PRO ALA GLN TYR PHE LEU PRO GLY LYS ALA
SEQRES 86 D 1409 ILE VAL GLN LEU GLU ASP GLY VAL GLN ILE SER SER GLY
SEQRES 87 D 1409 ASP THR LEU ALA ARG ILE PRO GLN GLU SER GLY GLY THR
SEQRES 88 D 1409 LYS ASP ILE THR GLY GLY LEU PRO ARG VAL ALA ASP LEU
SEQRES 89 D 1409 PHE GLU ALA ARG ARG PRO LYS GLU PRO ALA ILE LEU ALA
SEQRES 90 D 1409 GLU ILE SER GLY ILE VAL SER PHE GLY LYS GLU THR LYS
SEQRES 91 D 1409 GLY LYS ARG ARG LEU VAL ILE THR PRO VAL ASP GLY SER
SEQRES 92 D 1409 ASP PRO TYR GLU GLU MET ILE PRO LYS TRP ARG GLN LEU
SEQRES 93 D 1409 ASN VAL PHE GLU GLY GLU ARG VAL GLU ARG GLY ASP VAL
SEQRES 94 D 1409 ILE SER ASP GLY PRO GLU ALA PRO HIS ASP ILE LEU ARG
SEQRES 95 D 1409 LEU ARG GLY VAL HIS ALA VAL THR ARG TYR ILE VAL ASN
SEQRES 96 D 1409 GLU VAL GLN ASP VAL TYR ARG LEU GLN GLY VAL LYS ILE
SEQRES 97 D 1409 ASN ASP LYS HIS ILE GLU VAL ILE VAL ARG GLN MET LEU
SEQRES 98 D 1409 ARG LYS ALA THR ILE VAL ASN ALA GLY SER SER ASP PHE
SEQRES 99 D 1409 LEU GLU GLY GLU GLN VAL GLU TYR SER ARG VAL LYS ILE
SEQRES 100 D 1409 ALA ASN ARG GLU LEU GLU ALA ASN GLY LYS VAL GLY ALA
SEQRES 101 D 1409 THR TYR SER ARG ASP LEU LEU GLY ILE THR LYS ALA SER
SEQRES 102 D 1409 LEU ALA THR GLU SER PHE ILE SER ALA ALA SER PHE GLN
SEQRES 103 D 1409 GLU THR THR ARG VAL LEU THR GLU ALA ALA VAL ALA GLY
SEQRES 104 D 1409 LYS ARG ASP GLU LEU ARG GLY LEU LYS GLU ASN VAL ILE
SEQRES 105 D 1409 VAL GLY ARG LEU ILE PRO ALA GLY THR GLY TYR ALA TYR
SEQRES 106 D 1409 HIS GLN ASP ARG MET ARG ARG ARG ALA ALA GLY GLU ALA
SEQRES 107 D 1409 PRO ALA ALA PRO GLN VAL THR ALA GLU ASP ALA SER ALA
SEQRES 108 D 1409 SER LEU ALA GLU LEU LEU ASN ALA GLY LEU GLY GLY SER
SEQRES 109 D 1409 ASP ASN GLU LEU GLU
SEQRES 1 E 90 MET ALA ARG VAL THR VAL GLN ASP ALA VAL GLU LYS ILE
SEQRES 2 E 90 GLY ASN ARG PHE ASP LEU VAL LEU VAL ALA ALA ARG ARG
SEQRES 3 E 90 ALA ARG GLN MET GLN VAL GLY GLY LYS ASP PRO LEU VAL
SEQRES 4 E 90 PRO GLU GLU ASN ASP LYS THR THR VAL ILE ALA LEU ARG
SEQRES 5 E 90 GLU ILE GLU GLU GLY LEU ILE ASN ASN GLN ILE LEU ASP
SEQRES 6 E 90 VAL ARG GLU ARG GLN GLU GLN GLN GLU GLN GLU ALA ALA
SEQRES 7 E 90 GLU LEU GLN ALA VAL THR ALA ILE ALA GLU GLY ARG
SEQRES 1 F 613 MET GLU GLN ASN PRO GLN SER GLN LEU LYS LEU LEU VAL
SEQRES 2 F 613 THR ARG GLY LYS GLU GLN GLY TYR LEU THR TYR ALA GLU
SEQRES 3 F 613 VAL ASN ASP HIS LEU PRO GLU ASP ILE VAL ASP SER ASP
SEQRES 4 F 613 GLN ILE GLU ASP ILE ILE GLN MET ILE ASN ASP MET GLY
SEQRES 5 F 613 ILE GLN VAL MET GLU GLU ALA PRO ASP ALA ASP ASP LEU
SEQRES 6 F 613 MET LEU ALA GLU ASN THR ALA ASP GLU ASP ALA ALA GLU
SEQRES 7 F 613 ALA ALA ALA GLN VAL LEU SER SER VAL GLU SER GLU ILE
SEQRES 8 F 613 GLY ARG THR THR ASP PRO VAL ARG MET TYR MET ARG GLU
SEQRES 9 F 613 MET GLY THR VAL GLU LEU LEU THR ARG GLU GLY GLU ILE
SEQRES 10 F 613 ASP ILE ALA LYS ARG ILE GLU ASP GLY ILE ASN GLN VAL
SEQRES 11 F 613 GLN CYS SER VAL ALA GLU TYR PRO GLU ALA ILE THR TYR
SEQRES 12 F 613 LEU LEU GLU GLN TYR ASN ARG VAL GLU ALA GLU GLU ALA
SEQRES 13 F 613 ARG LEU SER ASP LEU ILE THR GLY PHE VAL ASP PRO ASN
SEQRES 14 F 613 ALA GLU GLU ASP LEU ALA PRO THR ALA THR HIS VAL GLY
SEQRES 15 F 613 SER GLU LEU SER GLN GLU ASP LEU ASP ASP ASP GLU ASP
SEQRES 16 F 613 GLU ASP GLU GLU ASP GLY ASP ASP ASP SER ALA ASP ASP
SEQRES 17 F 613 ASP ASN SER ILE ASP PRO GLU LEU ALA ARG GLU LYS PHE
SEQRES 18 F 613 ALA GLU LEU ARG ALA GLN TYR VAL VAL THR ARG ASP THR
SEQRES 19 F 613 ILE LYS ALA LYS GLY ARG SER HIS ALA THR ALA GLN GLU
SEQRES 20 F 613 GLU ILE LEU LYS LEU SER GLU VAL PHE LYS GLN PHE ARG
SEQRES 21 F 613 LEU VAL PRO LYS GLN PHE ASP TYR LEU VAL ASN SER MET
SEQRES 22 F 613 ARG VAL MET MET ASP ARG VAL ARG THR GLN GLU ARG LEU
SEQRES 23 F 613 ILE MET LYS LEU CYS VAL GLU GLN CYS LYS MET PRO LYS
SEQRES 24 F 613 LYS ASN PHE ILE THR LEU PHE THR GLY ASN GLU THR SER
SEQRES 25 F 613 ASP THR TRP PHE ASN ALA ALA ILE ALA MET ASN LYS PRO
SEQRES 26 F 613 TRP SER GLU LYS LEU HIS ASP VAL SER GLU GLU VAL HIS
SEQRES 27 F 613 ARG ALA LEU GLN LYS LEU GLN GLN ILE GLU GLU GLU THR
SEQRES 28 F 613 GLY LEU THR ILE GLU GLN VAL LYS ASP ILE ASN ARG ARG
SEQRES 29 F 613 MET SER ILE GLY GLU ALA LYS ALA ARG ARG ALA LYS LYS
SEQRES 30 F 613 GLU MET VAL GLU ALA ASN LEU ARG LEU VAL ILE SER ILE
SEQRES 31 F 613 ALA LYS LYS TYR THR ASN ARG GLY LEU GLN PHE LEU ASP
SEQRES 32 F 613 LEU ILE GLN GLU GLY ASN ILE GLY LEU MET LYS ALA VAL
SEQRES 33 F 613 ASP LYS PHE GLU TYR ARG ARG GLY TYR LYS PHE SER THR
SEQRES 34 F 613 TYR ALA THR TRP TRP ILE ARG GLN ALA ILE THR ARG SER
SEQRES 35 F 613 ILE ALA ASP GLN ALA ARG THR ILE ARG ILE PRO VAL HIS
SEQRES 36 F 613 MET ILE GLU THR ILE ASN LYS LEU ASN ARG ILE SER ARG
SEQRES 37 F 613 GLN MET LEU GLN GLU MET GLY ARG GLU PRO THR PRO GLU
SEQRES 38 F 613 GLU LEU ALA GLU ARG MET LEU MET PRO GLU ASP LYS ILE
SEQRES 39 F 613 ARG LYS VAL LEU LYS ILE ALA LYS GLU PRO ILE SER MET
SEQRES 40 F 613 GLU THR PRO ILE GLY ASP ASP GLU ASP SER HIS LEU GLY
SEQRES 41 F 613 ASP PHE ILE GLU ASP THR THR LEU GLU LEU PRO LEU ASP
SEQRES 42 F 613 SER ALA THR THR GLU SER LEU ARG ALA ALA THR HIS ASP
SEQRES 43 F 613 VAL LEU ALA GLY LEU THR ALA ARG GLU ALA LYS VAL LEU
SEQRES 44 F 613 ARG MET ARG PHE GLY ILE ASP MET ASN THR ASP TYR THR
SEQRES 45 F 613 LEU GLU GLU VAL GLY LYS GLN PHE ASP VAL THR ARG GLU
SEQRES 46 F 613 ARG ILE ARG GLN ILE GLU ALA LYS ALA LEU ARG LYS LEU
SEQRES 47 F 613 ARG HIS PRO SER ARG SER GLU VAL LEU ARG SER PHE LEU
SEQRES 48 F 613 ASP ASP
SEQRES 1 N 29 DG DA DC DC DT DT DC DC DC DC DT DG DA
SEQRES 2 N 29 DT DG DG DG DA DA DG DG DT DT DT DA DT
SEQRES 3 N 29 DA DA DT
SEQRES 1 T 24 DA DA DA DC DC DT DT DC DC DC DA DT DC
SEQRES 2 T 24 DA DG DG DG DG DA DA DG DG DT DC
SEQRES 1 I 19 GLY THR PRO GLY PHE GLN THR PRO ASP ALA ARG VAL ILE
SEQRES 2 I 19 SER ARG PHE GLY PHE ASN
HET EDO C1401 10
HET MG D1501 1
HET ZN D1502 1
HET ZN D1503 1
HET EPE D1504 32
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN EPE HEPES
FORMUL 10 EDO C2 H6 O2
FORMUL 11 MG MG 2+
FORMUL 12 ZN 2(ZN 2+)
FORMUL 14 EPE C8 H18 N2 O4 S
FORMUL 15 HOH *26(H2 O)
HELIX 1 AA1 GLY A 34 LEU A 48 1 15
HELIX 2 AA2 ASP A 77 GLY A 87 1 11
HELIX 3 AA3 PRO A 154 ILE A 159 1 6
HELIX 4 AA4 ASP A 212 LEU A 228 1 17
HELIX 5 AA5 GLU A 229 VAL A 232 5 4
HELIX 6 AA6 GLY B 34 SER B 50 1 17
HELIX 7 AA7 ASP B 77 LEU B 88 1 12
HELIX 8 AA8 ASP B 212 GLU B 229 1 18
HELIX 9 AA9 SER C 4 ARG C 10 1 7
HELIX 10 AB1 LEU C 28 GLU C 40 1 13
HELIX 11 AB2 GLY C 48 PHE C 57 1 10
HELIX 12 AB3 ASP C 81 GLY C 89 1 9
HELIX 13 AB4 GLU C 106 ARG C 107 1 2
HELIX 14 AB5 GLY C 112 VAL C 114 1 3
HELIX 15 AB6 ALA C 206 LEU C 213 1 8
HELIX 16 AB7 THR C 216 PHE C 225 1 10
HELIX 17 AB8 GLU C 244 GLY C 248 5 5
HELIX 18 AB9 THR C 270 ASP C 280 1 11
HELIX 19 AC1 PRO C 288 ALA C 293 1 6
HELIX 20 AC2 SER C 318 SER C 328 1 11
HELIX 21 AC3 PRO C 345 ARG C 352 1 8
HELIX 22 AC4 ASP C 358 ARG C 371 1 14
HELIX 23 AC5 THR C 377 SER C 391 1 15
HELIX 24 AC6 SER C 398 LEU C 409 1 12
HELIX 25 AC7 SER C 421 GLY C 438 1 18
HELIX 26 AC8 HIS C 447 GLY C 449 5 3
HELIX 27 AC9 SER C 455 VAL C 471 1 17
HELIX 28 AD1 VAL C 471 LEU C 481 1 11
HELIX 29 AD2 ASN C 494 SER C 508 1 15
HELIX 30 AD3 ASN C 519 ARG C 528 1 10
HELIX 31 AD4 HIS C 551 TYR C 555 5 5
HELIX 32 AD5 ALA C 608 TYR C 614 1 7
HELIX 33 AD6 SER C 662 LEU C 667 1 6
HELIX 34 AD7 PHE C 670 ASP C 674 5 5
HELIX 35 AD8 ASP C 675 GLN C 688 1 14
HELIX 36 AD9 MET C 704 VAL C 710 1 7
HELIX 37 AE1 GLU C 820 GLU C 825 1 6
HELIX 38 AE2 GLY C 858 SER C 863 1 6
HELIX 39 AE3 THR C 896 PHE C 906 1 11
HELIX 40 AE4 ASP C 942 VAL C 980 1 39
HELIX 41 AE5 GLU C 985 ASP C 990 1 6
HELIX 42 AE6 PRO C 993 LEU C 1000 1 8
HELIX 43 AE7 LYS C 1007 GLN C 1038 1 32
HELIX 44 AE8 LEU C 1101 ARG C 1106 1 6
HELIX 45 AE9 ILE C 1109 GLN C 1134 1 26
HELIX 46 AF1 GLU C 1137 ASP C 1150 1 14
HELIX 47 AF2 GLU C 1167 ASN C 1175 1 9
HELIX 48 AF3 LYS C 1191 GLY C 1202 1 12
HELIX 49 AF4 GLY C 1271 TYR C 1281 1 11
HELIX 50 AF5 ALA C 1283 THR C 1292 1 10
HELIX 51 AF6 ASP C 1297 ASP C 1310 1 14
HELIX 52 AF7 PRO C 1320 SER C 1332 1 13
HELIX 53 AF8 SER D 26 TRP D 33 1 8
HELIX 54 AF9 GLN D 94 GLU D 100 5 7
HELIX 55 AG1 ILE D 114 SER D 119 1 6
HELIX 56 AG2 SER D 122 LEU D 128 1 7
HELIX 57 AG3 PRO D 131 TYR D 140 1 10
HELIX 58 AG4 THR D 161 ASP D 167 1 7
HELIX 59 AG5 GLY D 181 SER D 191 1 11
HELIX 60 AG6 ASP D 193 GLU D 207 1 15
HELIX 61 AG7 GLU D 211 LYS D 216 1 6
HELIX 62 AG8 LYS D 216 GLY D 231 1 16
HELIX 63 AG9 LYS D 233 TRP D 236 5 4
HELIX 64 AH1 PRO D 246 ARG D 250 5 5
HELIX 65 AH2 SER D 263 ALA D 286 1 24
HELIX 66 AH3 PRO D 288 ASP D 308 1 21
HELIX 67 AH4 LEU D 327 ILE D 331 5 5
HELIX 68 AH5 LYS D 370 PHE D 377 1 8
HELIX 69 AH6 PHE D 377 ARG D 388 1 12
HELIX 70 AH7 THR D 393 GLU D 404 1 12
HELIX 71 AH8 GLU D 405 ARG D 417 1 13
HELIX 72 AH9 HIS D 430 LEU D 432 5 3
HELIX 73 AI1 HIS D 450 ASN D 458 1 9
HELIX 74 AI2 THR D 473 LEU D 483 1 11
HELIX 75 AI3 GLN D 504 ARG D 515 1 12
HELIX 76 AI4 GLY D 529 SER D 539 1 11
HELIX 77 AI5 THR D 573 TRP D 580 1 8
HELIX 78 AI6 GLY D 597 GLY D 613 1 17
HELIX 79 AI7 GLY D 613 GLY D 636 1 24
HELIX 80 AI8 LYS D 649 GLY D 671 1 23
HELIX 81 AI9 THR D 674 THR D 703 1 30
HELIX 82 AJ1 ASN D 720 GLY D 729 1 10
HELIX 83 AJ2 SER D 733 GLY D 742 1 10
HELIX 84 AJ3 ASN D 768 GLN D 805 1 38
HELIX 85 AJ4 PRO D 834 LEU D 840 1 7
HELIX 86 AJ5 HIS D 865 ASN D 875 1 11
HELIX 87 AJ6 ALA D 896 GLY D 900 1 5
HELIX 88 AJ7 ALA D 914 GLU D 925 1 12
HELIX 89 AJ8 PRO D 926 LEU D 930 5 5
HELIX 90 AJ9 GLY D 1137 GLU D 1146 1 10
HELIX 91 AK1 ALA D 1216 GLY D 1225 1 10
HELIX 92 AK2 GLY D 1225 GLN D 1244 1 20
HELIX 93 AK3 ASN D 1249 LEU D 1261 1 13
HELIX 94 AK4 TYR D 1282 ASN D 1295 1 14
HELIX 95 AK5 GLY D 1308 ALA D 1315 1 8
HELIX 96 AK6 SER D 1318 GLN D 1326 1 9
HELIX 97 AK7 GLU D 1327 ALA D 1338 1 12
HELIX 98 AK8 LEU D 1347 VAL D 1353 1 7
HELIX 99 AK9 GLY D 1360 ARG D 1372 1 13
HELIX 100 AL1 VAL E 6 ILE E 13 1 8
HELIX 101 AL2 ASN E 15 VAL E 32 1 18
HELIX 102 AL3 LYS E 45 GLY E 57 1 13
HELIX 103 AL4 ASN E 60 GLN E 75 1 16
HELIX 104 AL5 ASP F 96 ARG F 103 1 8
HELIX 105 AL6 GLU F 104 VAL F 108 5 5
HELIX 106 AL7 ARG F 113 GLU F 136 1 24
HELIX 107 AL8 PRO F 263 VAL F 292 1 30
HELIX 108 AL9 PRO F 298 THR F 307 1 10
HELIX 109 AM1 ASP F 313 MET F 322 1 10
HELIX 110 AM2 TRP F 326 GLY F 352 1 27
HELIX 111 AM3 THR F 354 LYS F 392 1 39
HELIX 112 AM4 GLN F 400 LYS F 418 1 19
HELIX 113 AM5 PHE F 419 GLY F 424 5 6
HELIX 114 AM6 LYS F 426 ALA F 447 1 22
HELIX 115 AM7 PRO F 453 MET F 470 1 18
HELIX 116 AM8 MET F 470 GLY F 475 1 6
HELIX 117 AM9 THR F 479 MET F 487 1 9
HELIX 118 AN1 GLU F 491 ALA F 501 1 11
HELIX 119 AN2 GLY F 512 ASP F 514 5 3
HELIX 120 AN3 LEU F 530 ALA F 549 1 20
HELIX 121 AN4 THR F 552 PHE F 563 1 12
HELIX 122 AN5 THR F 572 GLN F 579 1 8
HELIX 123 AN6 THR F 583 HIS F 600 1 18
HELIX 124 AN7 SER F 604 SER F 609 1 6
SHEET 1 AA1 4 LEU A 13 GLU A 17 0
SHEET 2 AA1 4 HIS A 23 LEU A 28 -1 O THR A 27 N VAL A 14
SHEET 3 AA1 4 ASP A 199 THR A 207 -1 O LEU A 201 N LEU A 28
SHEET 4 AA1 4 VAL A 180 ALA A 189 -1 N GLU A 188 O LYS A 200
SHEET 1 AA2 5 ILE A 115 THR A 116 0
SHEET 2 AA2 5 VAL A 98 SER A 105 -1 N THR A 101 O THR A 116
SHEET 3 AA2 5 SER A 139 ARG A 148 -1 O ILE A 144 N LEU A 100
SHEET 4 AA2 5 CYS A 54 ILE A 61 -1 N GLU A 58 O LYS A 145
SHEET 5 AA2 5 LEU A 171 LEU A 172 -1 O LEU A 171 N VAL A 59
SHEET 1 AA3 2 VAL A 90 ARG A 91 0
SHEET 2 AA3 2 GLU A 122 ILE A 123 -1 O GLU A 122 N ARG A 91
SHEET 1 AA4 2 GLY A 108 THR A 111 0
SHEET 2 AA4 2 VAL A 129 LEU A 133 -1 O CYS A 131 N VAL A 110
SHEET 1 AA5 2 GLY A 151 VAL A 153 0
SHEET 2 AA5 2 ALA A 175 TYR A 177 -1 O ALA A 175 N VAL A 153
SHEET 1 AA6 4 LEU B 13 GLU B 17 0
SHEET 2 AA6 4 HIS B 23 LEU B 28 -1 O LYS B 25 N GLU B 17
SHEET 3 AA6 4 LEU B 198 THR B 207 -1 O ILE B 203 N VAL B 26
SHEET 4 AA6 4 VAL B 180 ALA B 190 -1 N ALA B 184 O GLU B 204
SHEET 1 AA7 3 PRO B 52 GLU B 60 0
SHEET 2 AA7 3 ARG B 143 ARG B 150 -1 O ARG B 143 N GLU B 60
SHEET 3 AA7 3 VAL B 98 THR B 101 -1 N VAL B 98 O VAL B 146
SHEET 1 AA8 2 GLY B 108 VAL B 110 0
SHEET 2 AA8 2 CYS B 131 LEU B 133 -1 O CYS B 131 N VAL B 110
SHEET 1 AA9 2 TYR B 152 VAL B 153 0
SHEET 2 AA9 2 ALA B 175 CYS B 176 -1 O ALA B 175 N VAL B 153
SHEET 1 AB1 3 LYS C 13 ASP C 14 0
SHEET 2 AB1 3 ILE C1182 ALA C1183 1 O ALA C1183 N LYS C 13
SHEET 3 AB1 3 VAL C 700 GLY C 701 1 N GLY C 701 O ILE C1182
SHEET 1 AB2 4 ILE C 59 GLN C 60 0
SHEET 2 AB2 4 GLU C 67 LEU C 75 -1 O LEU C 68 N ILE C 59
SHEET 3 AB2 4 SER C 93 TYR C 105 -1 O ARG C 97 N ARG C 74
SHEET 4 AB2 4 LYS C 115 PRO C 128 -1 O ASP C 116 N ILE C 104
SHEET 1 AB3 3 PHE C 136 VAL C 137 0
SHEET 2 AB3 3 GLU C 142 ILE C 145 -1 O ARG C 143 N PHE C 136
SHEET 3 AB3 3 SER C 512 PHE C 514 -1 O GLN C 513 N VAL C 144
SHEET 1 AB4 3 ARG C 451 ARG C 454 0
SHEET 2 AB4 3 SER C 147 ARG C 151 -1 N GLN C 148 O ARG C 454
SHEET 3 AB4 3 ILE C 530 SER C 531 1 O SER C 531 N SER C 147
SHEET 1 AB5 4 GLY C 154 ASP C 158 0
SHEET 2 AB5 4 ASN C 173 ILE C 177 -1 O ILE C 177 N GLY C 154
SHEET 3 AB5 4 LEU C 184 PHE C 188 -1 O LEU C 184 N ILE C 176
SHEET 4 AB5 4 LEU C 194 ILE C 198 -1 O ARG C 197 N ASP C 185
SHEET 1 AB6 4 LEU C 284 GLU C 286 0
SHEET 2 AB6 4 GLN C 238 GLU C 240 -1 N MET C 239 O ILE C 285
SHEET 3 AB6 4 LYS C 227 GLU C 231 -1 N GLU C 231 O GLN C 238
SHEET 4 AB6 4 ILE C 333 LEU C 336 -1 O ILE C 333 N PHE C 230
SHEET 1 AB7 2 VAL C 296 VAL C 297 0
SHEET 2 AB7 2 MET C 315 GLU C 316 -1 O MET C 315 N VAL C 297
SHEET 1 AB8 2 TYR C 301 ILE C 302 0
SHEET 2 AB8 2 LEU C 309 CYS C 311 -1 O CYS C 311 N TYR C 301
SHEET 1 AB9 3 GLN C 580 THR C 581 0
SHEET 2 AB9 3 LEU C 587 VAL C 594 -1 O GLU C 588 N GLN C 580
SHEET 3 AB9 3 VAL C 599 SER C 607 -1 O THR C 600 N LYS C 593
SHEET 1 AC1 3 GLN C 580 THR C 581 0
SHEET 2 AC1 3 LEU C 587 VAL C 594 -1 O GLU C 588 N GLN C 580
SHEET 3 AC1 3 TYR C 652 ASP C 654 -1 O MET C 653 N ARG C 592
SHEET 1 AC2 2 LEU C 633 ARG C 637 0
SHEET 2 AC2 2 SER C 642 SER C 646 -1 O PHE C 645 N VAL C 634
SHEET 1 AC3 3 ALA C 716 VAL C 717 0
SHEET 2 AC3 3 VAL C 782 ASP C 785 -1 O LEU C 783 N ALA C 716
SHEET 3 AC3 3 MET C 768 PRO C 769 -1 N MET C 768 O ASP C 785
SHEET 1 AC4 4 ILE C 748 ASN C 752 0
SHEET 2 AC4 4 ARG C 731 VAL C 736 -1 N ILE C 734 O ASP C 749
SHEET 3 AC4 4 GLY C 722 VAL C 727 -1 N VAL C 723 O LYS C 735
SHEET 4 AC4 4 PRO C 776 VAL C 777 -1 O VAL C 777 N GLY C 722
SHEET 1 AC5 2 THR C 757 ARG C 758 0
SHEET 2 AC5 2 CYS C 764 ILE C 765 -1 O ILE C 765 N THR C 757
SHEET 1 AC6 2 THR C 789 ASP C 790 0
SHEET 2 AC6 2 GLU C 793 LEU C 794 -1 O GLU C 793 N ASP C 790
SHEET 1 AC7 8 GLN C1209 ILE C1210 0
SHEET 2 AC7 8 VAL C1225 LYS C1234 -1 O VAL C1225 N ILE C1210
SHEET 3 AC7 8 LYS C1065 ALA C1067 -1 N ALA C1067 O LEU C1233
SHEET 4 AC7 8 LYS C1073 ASN C1080 -1 O GLY C1074 N MET C1066
SHEET 5 AC7 8 ILE C 816 SER C 819 1 N ILE C 816 O VAL C1075
SHEET 6 AC7 8 ILE C1096 LEU C1098 -1 O VAL C1097 N LEU C 817
SHEET 7 AC7 8 GLN C 798 PHE C 804 1 N ARG C 801 O ILE C1096
SHEET 8 AC7 8 VAL C1225 LYS C1234 -1 O MET C1230 N MET C 800
SHEET 1 AC8 3 THR C 830 ARG C 841 0
SHEET 2 AC8 3 VAL C1046 ARG C1058 -1 O ARG C1058 N THR C 830
SHEET 3 AC8 3 THR C 927 THR C 935 -1 N ASP C 930 O TYR C1053
SHEET 1 AC9 2 ILE C 882 VAL C 884 0
SHEET 2 AC9 2 LEU C 918 ARG C 919 -1 O LEU C 918 N LEU C 883
SHEET 1 AD1 8 HIS C1244 ARG C1246 0
SHEET 2 AD1 8 SER D 350 VAL D 357 -1 O ARG D 352 N HIS C1244
SHEET 3 AD1 8 GLN D 465 HIS D 469 -1 O MET D 466 N SER D 353
SHEET 4 AD1 8 VAL D 421 ARG D 425 -1 N ASN D 424 O ALA D 467
SHEET 5 AD1 8 ILE D 434 ILE D 442 -1 O GLN D 435 N LEU D 423
SHEET 6 AD1 8 GLN D 365 PRO D 369 1 N LEU D 368 O VAL D 440
SHEET 7 AD1 8 ILE D 447 LEU D 449 -1 O GLN D 448 N GLY D 367
SHEET 8 AD1 8 SER D 350 VAL D 357 1 N THR D 356 O LEU D 449
SHEET 1 AD2 2 GLN C1268 PHE C1270 0
SHEET 2 AD2 2 LYS D 345 VAL D 347 -1 O VAL D 347 N GLN C1268
SHEET 1 AD3 3 ILE C1335 LEU C1339 0
SHEET 2 AD3 3 ILE D 20 LEU D 24 -1 O ALA D 23 N ASN C1336
SHEET 3 AD3 3 ARG D1341 ASP D1342 -1 O ASP D1342 N ILE D 20
SHEET 1 AD4 3 SER D 34 GLU D 37 0
SHEET 2 AD4 3 MET D 102 ALA D 112 1 O MET D 102 N PHE D 35
SHEET 3 AD4 3 ILE D 238 VAL D 244 -1 O LEU D 242 N ILE D 105
SHEET 1 AD5 3 ILE D 159 LEU D 160 0
SHEET 2 AD5 3 TYR D 144 ILE D 147 -1 N TYR D 144 O LEU D 160
SHEET 3 AD5 3 ASP D 177 LYS D 179 -1 O ASP D 177 N ILE D 147
SHEET 1 AD6 2 ALA D 261 THR D 262 0
SHEET 2 AD6 2 ILE F 505 SER F 506 1 O ILE F 505 N THR D 262
SHEET 1 AD7 2 LYS D 549 ASP D 558 0
SHEET 2 AD7 2 GLU D 562 ASP D 571 -1 O LYS D 566 N GLU D 554
SHEET 1 AD8 2 VAL D 706 ARG D 709 0
SHEET 2 AD8 2 GLN D 712 LYS D 715 -1 O GLN D 712 N ARG D 709
SHEET 1 AD9 2 VAL D 809 GLU D 811 0
SHEET 2 AD9 2 VAL D 894 CYS D 895 1 O VAL D 894 N THR D 810
SHEET 1 AE1 2 ILE D 820 MET D 822 0
SHEET 2 AE1 2 VAL D 880 VAL D 882 -1 O VAL D 882 N ILE D 820
SHEET 1 AE2 2 ILE D 826 GLU D 827 0
SHEET 2 AE2 2 ASP D 830 VAL D 831 -1 N ASP D 830 O GLU D 827
SHEET 1 AE3 4 TYR D 995 LYS D 996 0
SHEET 2 AE3 4 GLU D 981 LEU D 984 -1 N LEU D 982 O TYR D 995
SHEET 3 AE3 4 SER D 957 SER D 961 -1 N LYS D 959 O LYS D 983
SHEET 4 AE3 4 GLU D1009 GLN D1010 -1 N GLU D1009 O ILE D 958
SHEET 1 AE4 2 SER D 965 VAL D 967 0
SHEET 2 AE4 2 LEU D 973 ILE D 975 -1 O VAL D 974 N VAL D 966
SHEET 1 AE5 3 SER D1164 PHE D1165 0
SHEET 2 AE5 3 LEU D1175 VAL D1176 -1 O VAL D1176 N SER D1164
SHEET 3 AE5 3 GLU D1187 GLU D1188 -1 O GLU D1188 N LEU D1175
SHEET 1 AE6 3 GLN D1279 GLU D1281 0
SHEET 2 AE6 3 LYS D1263 ILE D1266 -1 N ALA D1264 O VAL D1280
SHEET 3 AE6 3 TYR D1302 ASP D1305 -1 O ASP D1305 N LYS D1263
SHEET 1 AE7 2 PRO F 510 ILE F 511 0
SHEET 2 AE7 2 GLU F 515 HIS F 518 -1 O SER F 517 N ILE F 511
SHEET 1 AE8 2 THR I 7 PRO I 8 0
SHEET 2 AE8 2 ILE I 13 SER I 14 -1 O SER I 14 N THR I 7
LINK SG CYS D 70 ZN ZN D1502 1555 1555 2.76
LINK SG CYS D 72 ZN ZN D1502 1555 1555 2.33
LINK SG CYS D 85 ZN ZN D1502 1555 1555 2.52
LINK SG CYS D 88 ZN ZN D1502 1555 1555 2.60
LINK OD1 ASP D 460 MG MG D1501 1555 1555 2.31
LINK OD2 ASP D 462 MG MG D1501 1555 1555 2.03
LINK OD1 ASP D 464 MG MG D1501 1555 1555 2.77
LINK OD2 ASP D 464 MG MG D1501 1555 1555 2.81
LINK SG CYS D 814 ZN ZN D1503 1555 1555 2.39
LINK SG CYS D 888 ZN ZN D1503 1555 1555 2.28
LINK SG CYS D 895 ZN ZN D1503 1555 1555 2.27
CISPEP 1 GLU B 29 PRO B 30 0 -0.57
CISPEP 2 PHE C 57 PRO C 58 0 -1.23
CISPEP 3 ASP C 624 GLU C 625 0 -1.05
CISPEP 4 ALA C 746 GLY C 747 0 23.33
CISPEP 5 GLY C 1261 LYS C 1262 0 1.33
CISPEP 6 LYS C 1262 ALA C 1263 0 -3.24
CISPEP 7 ASP D 256 GLY D 257 0 8.70
CISPEP 8 THR D 1135 GLY D 1136 0 -3.27
CISPEP 9 THR F 112 ARG F 113 0 -4.17
CISPEP 10 GLY I 4 PHE I 5 0 -2.85
SITE 1 AC1 5 ASN C 139 GLY C 140 THR C 141 ARG C 758
SITE 2 AC1 5 LYS C1051
SITE 1 AC2 3 ASP D 460 ASP D 462 ASP D 464
SITE 1 AC3 5 CYS D 70 CYS D 72 CYS D 85 LYS D 87
SITE 2 AC3 5 CYS D 88
SITE 1 AC4 4 CYS D 814 CYS D 888 CYS D 895 CYS D 898
SITE 1 AC5 7 TYR D 511 GLN D 594 ALA D 595 LEU D 596
SITE 2 AC5 7 GLY D 597 ALA D 600 ASP D 727
CRYST1 172.888 172.888 385.015 90.00 90.00 90.00 P 41 21 2 16
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 0.005784 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005784 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002597 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
