HEADER TRANSLATION, TRANSFERASE/RNA 18-JAN-12 3VNV
TITLE COMPLEX STRUCTURE OF VIRAL RNA POLYMERASE II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TS, ELONGATION FACTOR TU, LINKER, Q BETA
COMPND 3 REPLICASE;
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RNA (5'-R(*CP*CP*CP*UP*AP*CP*C)-3');
COMPND 8 CHAIN: G;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: RNA (5'-R(*GP*GP*GP*UP*AP*GP*GP*G)-3');
COMPND 12 CHAIN: T;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O157:H7, ESCHERICHIA PHAGE
SOURCE 3 QBETA;
SOURCE 4 ORGANISM_TAXID: 83334, 39803;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 OTHER_DETAILS: SYNTHESIZED RNA;
SOURCE 10 MOL_ID: 3;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: SYNTHESIZED RNA
KEYWDS RNA POLYMERASE, TRANSLATION, TRANSFERASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.TAKESHITA,K.TOMITA
REVDAT 4 08-NOV-23 3VNV 1 REMARK SEQADV LINK
REVDAT 3 28-JUN-17 3VNV 1 SOURCE
REVDAT 2 09-OCT-13 3VNV 1 JRNL
REVDAT 1 08-AUG-12 3VNV 0
JRNL AUTH D.TAKESHITA,S.YAMASHITA,K.TOMITA
JRNL TITL MECHANISM FOR TEMPLATE-INDEPENDENT TERMINAL ADENYLATION
JRNL TITL 2 ACTIVITY OF Q BETA REPLICASE
JRNL REF STRUCTURE V. 20 1661 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22884418
JRNL DOI 10.1016/J.STR.2012.07.004
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 55640
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2821
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 19.9368 - 6.9704 0.99 2783 144 0.2075 0.2444
REMARK 3 2 6.9704 - 5.5724 1.00 2726 135 0.2215 0.2667
REMARK 3 3 5.5724 - 4.8798 1.00 2693 157 0.1935 0.2598
REMARK 3 4 4.8798 - 4.4390 1.00 2645 155 0.1639 0.2304
REMARK 3 5 4.4390 - 4.1239 1.00 2658 158 0.1736 0.2403
REMARK 3 6 4.1239 - 3.8826 1.00 2653 151 0.1830 0.2762
REMARK 3 7 3.8826 - 3.6895 1.00 2685 121 0.1968 0.2751
REMARK 3 8 3.6895 - 3.5298 1.00 2635 144 0.2015 0.2617
REMARK 3 9 3.5298 - 3.3946 1.00 2633 131 0.1997 0.2548
REMARK 3 10 3.3946 - 3.2780 1.00 2664 135 0.2157 0.2676
REMARK 3 11 3.2780 - 3.1759 1.00 2623 137 0.2381 0.3186
REMARK 3 12 3.1759 - 3.0855 1.00 2649 126 0.2420 0.3187
REMARK 3 13 3.0855 - 3.0045 0.99 2632 144 0.2557 0.2758
REMARK 3 14 3.0045 - 2.9314 0.99 2618 129 0.2585 0.3410
REMARK 3 15 2.9314 - 2.8650 0.99 2585 167 0.2799 0.3241
REMARK 3 16 2.8650 - 2.8042 0.99 2615 132 0.2779 0.3595
REMARK 3 17 2.8042 - 2.7482 0.99 2576 156 0.2725 0.3185
REMARK 3 18 2.7482 - 2.6965 0.99 2626 126 0.2928 0.3254
REMARK 3 19 2.6965 - 2.6485 0.99 2595 151 0.3198 0.4007
REMARK 3 20 2.6485 - 2.6037 0.96 2525 122 0.3680 0.4007
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.27
REMARK 3 B_SOL : 22.08
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.81570
REMARK 3 B22 (A**2) : 5.11150
REMARK 3 B33 (A**2) : -3.29590
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 : 0.010 9837
REMARK 3 ANGLE : 1.258 13378
REMARK 3 CHIRALITY : 0.085 1524
REMARK 3 PLANARITY : 0.004 1679
REMARK 3 DIHEDRAL : 18.674 3719
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 3VNV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000095279.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55640
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 3AGP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.2M CALCIUM ACETATE, 0.1M
REMARK 280 HEPES, PH 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 69.86500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 128.02000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 69.86500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 128.02000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 50.86000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 69.86500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 128.02000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 50.86000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 69.86500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 128.02000
REMARK 290 SMTRY3 8 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A3509 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 287
REMARK 465 GLU A 288
REMARK 465 LYS A 289
REMARK 465 ALA A 327
REMARK 465 ALA A 328
REMARK 465 ARG A 329
REMARK 465 ALA A 330
REMARK 465 PHE A 331
REMARK 465 ASP A 332
REMARK 465 GLN A 333
REMARK 465 ILE A 334
REMARK 465 ASP A 335
REMARK 465 ASN A 336
REMARK 465 ALA A 337
REMARK 465 PRO A 338
REMARK 465 GLU A 339
REMARK 465 GLU A 340
REMARK 465 LYS A 341
REMARK 465 ALA A 342
REMARK 465 ARG A 343
REMARK 465 GLY A 344
REMARK 465 ILE A 345
REMARK 465 THR A 346
REMARK 465 ILE A 347
REMARK 465 SER A 681
REMARK 465 GLY A 682
REMARK 465 ALA A 683
REMARK 465 ALA A 684
REMARK 465 GLY A 685
REMARK 465 GLY A 686
REMARK 465 GLY A 687
REMARK 465 GLY A 688
REMARK 465 SER A 689
REMARK 465 GLY A 690
REMARK 465 GLY A 691
REMARK 465 GLY A 692
REMARK 465 GLY A 693
REMARK 465 SER A 694
REMARK 465 MET A 695
REMARK 465 SER A 696
REMARK 465 LYS A 697
REMARK 465 THR A 698
REMARK 465 ALA A 699
REMARK 465 ASP A 1217
REMARK 465 GLY A 1218
REMARK 465 LEU A 1219
REMARK 465 PRO A 1220
REMARK 465 LEU A 1221
REMARK 465 ARG A 1222
REMARK 465 GLY A 1223
REMARK 465 PRO A 1224
REMARK 465 SER A 1225
REMARK 465 GLY A 1226
REMARK 465 CYS A 1227
REMARK 465 ASP A 1228
REMARK 465 SER A 1229
REMARK 465 ALA A 1230
REMARK 465 ASP A 1231
REMARK 465 LEU A 1232
REMARK 465 PHE A 1233
REMARK 465 VAL A 1265
REMARK 465 LEU A 1266
REMARK 465 ALA A 1267
REMARK 465 PRO A 1268
REMARK 465 TYR A 1269
REMARK 465 GLY A 1270
REMARK 465 VAL A 1271
REMARK 465 PHE A 1272
REMARK 465 GLN A 1273
REMARK 465 GLY A 1274
REMARK 465 THR A 1275
REMARK 465 LYS A 1276
REMARK 465 VAL A 1277
REMARK 465 ALA A 1278
REMARK 465 SER A 1279
REMARK 465 LEU A 1280
REMARK 465 HIS A 1281
REMARK 465 GLU A 1282
REMARK 465 ALA A 1283
REMARK 465 HIS A 1284
REMARK 465 HIS A 1285
REMARK 465 HIS A 1286
REMARK 465 HIS A 1287
REMARK 465 HIS A 1288
REMARK 465 HIS A 1289
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 104 CG CD CE NZ
REMARK 470 PHE A 290 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 348 CG OD1 ND2
REMARK 470 ARG A 702 CG CD NE CZ NH1 NH2
REMARK 470 ASN A1216 CG OD1 ND2
REMARK 470 ARG A1264 CG CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 G T 2102 P C5' O3' C2' N9 C5 C6
REMARK 480 G T 2102 C2
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 PRO A1244 C - N - CA ANGL. DEV. = 11.2 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 GLU A 3 -95.30 -118.63
REMARK 500 SER A 7 -7.94 -59.84
REMARK 500 THR A 16 -51.06 -127.31
REMARK 500 ILE A 34 -80.93 -64.46
REMARK 500 ASN A 69 32.67 -162.39
REMARK 500 VAL A 96 -9.64 -53.23
REMARK 500 VAL A 101 -74.11 -76.71
REMARK 500 LYS A 104 95.13 -57.04
REMARK 500 THR A 106 -24.53 -146.32
REMARK 500 ASP A 162 -160.79 -115.54
REMARK 500 GLU A 163 -71.36 -66.81
REMARK 500 SER A 187 100.20 -51.76
REMARK 500 ALA A 188 5.16 -56.35
REMARK 500 PHE A 223 -35.36 -28.12
REMARK 500 GLU A 237 84.69 -177.24
REMARK 500 GLU A 263 124.97 -29.74
REMARK 500 GLU A 266 -47.46 -16.62
REMARK 500 LYS A 267 71.18 52.43
REMARK 500 MET A 285 -112.23 -61.07
REMARK 500 THR A 323 -88.42 -82.37
REMARK 500 TYR A 324 18.46 -67.19
REMARK 500 THR A 349 100.89 69.20
REMARK 500 SER A 350 90.45 45.59
REMARK 500 PRO A 357 -14.63 -45.44
REMARK 500 CYS A 366 62.85 -118.68
REMARK 500 ALA A 381 95.51 -176.23
REMARK 500 ASP A 426 -84.34 -77.19
REMARK 500 ASP A 466 103.63 -51.76
REMARK 500 ARG A 508 18.81 -173.67
REMARK 500 SER A 538 -179.00 -170.31
REMARK 500 GLU A 600 7.45 -65.82
REMARK 500 PHE A 608 -149.42 -143.32
REMARK 500 PHE A 617 -95.58 -91.54
REMARK 500 LEU A 677 -161.83 -108.57
REMARK 500 SER A 701 139.26 -172.07
REMARK 500 ASP A 754 -166.03 -171.02
REMARK 500 LEU A 778 92.82 -57.23
REMARK 500 ILE A 780 37.24 -74.20
REMARK 500 THR A 782 -137.97 -167.38
REMARK 500 GLU A 783 -10.31 -169.91
REMARK 500 TYR A 805 37.45 -95.05
REMARK 500 ARG A 806 7.44 -159.45
REMARK 500 PRO A 807 20.04 -68.80
REMARK 500 PHE A 813 -55.10 -20.87
REMARK 500 SER A 849 127.04 -16.21
REMARK 500 ALA A 868 -62.97 -99.94
REMARK 500 VAL A 904 -166.70 -119.94
REMARK 500 LYS A 908 -79.67 -129.85
REMARK 500 ASN A 962 9.88 46.71
REMARK 500 ALA A 972 -91.59 11.05
REMARK 500
REMARK 500 THIS ENTRY HAS 54 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 SER A 849 GLY A 850 138.46
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 CA A2502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 968 OD2
REMARK 620 2 LEU A 969 O 92.2
REMARK 620 3 ASP A1053 OD2 73.9 74.2
REMARK 620 4 CH1 A2501 O3G 98.9 92.7 164.6
REMARK 620 5 CH1 A2501 O2A 88.3 168.4 94.8 98.6
REMARK 620 6 CH1 A2501 O2B 172.0 91.5 100.3 87.9 86.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 968 OD2
REMARK 620 2 ASP A1053 OD1 81.1
REMARK 620 3 ASP A1054 OD2 125.2 115.6
REMARK 620 4 C G2007 O3' 141.6 75.4 92.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CH1 A 2501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AGP RELATED DB: PDB
REMARK 900 RELATED ID: 3AGQ RELATED DB: PDB
REMARK 900 RELATED ID: 3VNU RELATED DB: PDB
DBREF 3VNV A 1 283 UNP P0A6P3 EFTS_ECO57 1 283
DBREF 3VNV A 285 678 UNP P0A6N3 EFTU_ECO57 1 394
DBREF 3VNV A 679 694 PDB 3VNV 3VNV 679 694
DBREF 3VNV A 695 1283 UNP Q8LTE0 Q8LTE0_BPQBE 1 589
DBREF 3VNV G 2001 2007 PDB 3VNV 3VNV 2001 2007
DBREF 3VNV T 2101 2108 PDB 3VNV 3VNV 2101 2108
SEQADV 3VNV HIS A 284 UNP P0A6P3 LINKER
SEQADV 3VNV HIS A 1284 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNV HIS A 1285 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNV HIS A 1286 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNV HIS A 1287 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNV HIS A 1288 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNV HIS A 1289 UNP Q8LTE0 EXPRESSION TAG
SEQRES 1 A 1289 MET ALA GLU ILE THR ALA SER LEU VAL LYS GLU LEU ARG
SEQRES 2 A 1289 GLU ARG THR GLY ALA GLY MET MET ASP CYS LYS LYS ALA
SEQRES 3 A 1289 LEU THR GLU ALA ASN GLY ASP ILE GLU LEU ALA ILE GLU
SEQRES 4 A 1289 ASN MET ARG LYS SER GLY ALA ILE LYS ALA ALA LYS LYS
SEQRES 5 A 1289 ALA GLY ASN VAL ALA ALA ASP GLY VAL ILE LYS THR LYS
SEQRES 6 A 1289 ILE ASP GLY ASN TYR GLY ILE ILE LEU GLU VAL ASN CYS
SEQRES 7 A 1289 GLN THR ASP PHE VAL ALA LYS ASP ALA GLY PHE GLN ALA
SEQRES 8 A 1289 PHE ALA ASP LYS VAL LEU ASP ALA ALA VAL ALA GLY LYS
SEQRES 9 A 1289 ILE THR ASP VAL GLU VAL LEU LYS ALA GLN PHE GLU GLU
SEQRES 10 A 1289 GLU ARG VAL ALA LEU VAL ALA LYS ILE GLY GLU ASN ILE
SEQRES 11 A 1289 ASN ILE ARG ARG VAL ALA ALA LEU GLU GLY ASP VAL LEU
SEQRES 12 A 1289 GLY SER TYR GLN HIS GLY ALA ARG ILE GLY VAL LEU VAL
SEQRES 13 A 1289 ALA ALA LYS GLY ALA ASP GLU GLU LEU VAL LYS HIS ILE
SEQRES 14 A 1289 ALA MET HIS VAL ALA ALA SER LYS PRO GLU PHE ILE LYS
SEQRES 15 A 1289 PRO GLU ASP VAL SER ALA GLU VAL VAL GLU LYS GLU TYR
SEQRES 16 A 1289 GLN VAL GLN LEU ASP ILE ALA MET GLN SER GLY LYS PRO
SEQRES 17 A 1289 LYS GLU ILE ALA GLU LYS MET VAL GLU GLY ARG MET LYS
SEQRES 18 A 1289 LYS PHE THR GLY GLU VAL SER LEU THR GLY GLN PRO PHE
SEQRES 19 A 1289 VAL MET GLU PRO SER LYS THR VAL GLY GLN LEU LEU LYS
SEQRES 20 A 1289 GLU HIS ASN ALA GLU VAL THR GLY PHE ILE ARG PHE GLU
SEQRES 21 A 1289 VAL GLY GLU GLY ILE GLU LYS VAL GLU THR ASP PHE ALA
SEQRES 22 A 1289 ALA GLU VAL ALA ALA MET SER LYS GLN SER HIS MET SER
SEQRES 23 A 1289 LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN VAL
SEQRES 24 A 1289 GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR LEU
SEQRES 25 A 1289 THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR GLY
SEQRES 26 A 1289 GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA PRO
SEQRES 27 A 1289 GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER HIS
SEQRES 28 A 1289 VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS VAL
SEQRES 29 A 1289 ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET ILE
SEQRES 30 A 1289 THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL VAL
SEQRES 31 A 1289 ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU HIS
SEQRES 32 A 1289 ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE ILE
SEQRES 33 A 1289 VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU GLU
SEQRES 34 A 1289 LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU LEU
SEQRES 35 A 1289 SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE VAL
SEQRES 36 A 1289 ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA GLU
SEQRES 37 A 1289 TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU ASP
SEQRES 38 A 1289 SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS PRO
SEQRES 39 A 1289 PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER GLY
SEQRES 40 A 1289 ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY ILE
SEQRES 41 A 1289 ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE LYS
SEQRES 42 A 1289 GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET PHE
SEQRES 43 A 1289 ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN VAL
SEQRES 44 A 1289 GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE GLU
SEQRES 45 A 1289 ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS PRO
SEQRES 46 A 1289 HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER LYS
SEQRES 47 A 1289 ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY TYR
SEQRES 48 A 1289 ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY
SEQRES 49 A 1289 THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET PRO
SEQRES 50 A 1289 GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS PRO
SEQRES 51 A 1289 ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG GLU
SEQRES 52 A 1289 GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS VAL
SEQRES 53 A 1289 LEU SER GLY ALA SER GLY ALA ALA GLY GLY GLY GLY SER
SEQRES 54 A 1289 GLY GLY GLY GLY SER MET SER LYS THR ALA SER SER ARG
SEQRES 55 A 1289 ASN SER LEU SER ALA GLN LEU ARG ARG ALA ALA ASN THR
SEQRES 56 A 1289 ARG ILE GLU VAL GLU GLY ASN LEU ALA LEU SER ILE ALA
SEQRES 57 A 1289 ASN ASP LEU LEU LEU ALA TYR GLY GLN SER PRO PHE ASN
SEQRES 58 A 1289 SER GLU ALA GLU CYS ILE SER PHE SER PRO ARG PHE ASP
SEQRES 59 A 1289 GLY THR PRO ASP ASP PHE ARG ILE ASN TYR LEU LYS ALA
SEQRES 60 A 1289 GLU ILE MET SER LYS TYR ASP ASP PHE SER LEU GLY ILE
SEQRES 61 A 1289 ASP THR GLU ALA VAL ALA TRP GLU LYS PHE LEU ALA ALA
SEQRES 62 A 1289 GLU ALA GLU CYS ALA LEU THR ASN ALA ARG LEU TYR ARG
SEQRES 63 A 1289 PRO ASP TYR SER GLU ASP PHE ASN PHE SER LEU GLY GLU
SEQRES 64 A 1289 SER CYS ILE HIS MET ALA ARG ARG LYS ILE ALA LYS LEU
SEQRES 65 A 1289 ILE GLY ASP VAL PRO SER VAL GLU GLY MET LEU ARG HIS
SEQRES 66 A 1289 CYS ARG PHE SER GLY GLY ALA THR THR THR ASN ASN ARG
SEQRES 67 A 1289 SER TYR GLY HIS PRO SER PHE LYS PHE ALA LEU PRO GLN
SEQRES 68 A 1289 ALA CYS THR PRO ARG ALA LEU LYS TYR VAL LEU ALA LEU
SEQRES 69 A 1289 ARG ALA SER THR HIS PHE ASP ILE ARG ILE SER ASP ILE
SEQRES 70 A 1289 SER PRO PHE ASN LYS ALA VAL THR VAL PRO LYS ASN SER
SEQRES 71 A 1289 LYS THR ASP ARG CYS ILE ALA ILE GLU PRO GLY TRP ASN
SEQRES 72 A 1289 MET PHE PHE GLN LEU GLY ILE GLY GLY ILE LEU ARG ASP
SEQRES 73 A 1289 ARG LEU ARG CYS TRP GLY ILE ASP LEU ASN ASP GLN THR
SEQRES 74 A 1289 ILE ASN GLN ARG ARG ALA HIS GLU GLY SER VAL THR ASN
SEQRES 75 A 1289 ASN LEU ALA THR VAL ASP LEU SER ALA ALA SER ASP SER
SEQRES 76 A 1289 ILE SER LEU ALA LEU CYS GLU LEU LEU LEU PRO PRO GLY
SEQRES 77 A 1289 TRP PHE GLU VAL LEU MET ASP LEU ARG SER PRO LYS GLY
SEQRES 78 A 1289 ARG LEU PRO ASP GLY SER VAL VAL THR TYR GLU LYS ILE
SEQRES 79 A 1289 SER SER MET GLY ASN GLY TYR THR PHE GLU LEU GLU SER
SEQRES 80 A 1289 LEU ILE PHE ALA SER LEU ALA ARG SER VAL CYS GLU ILE
SEQRES 81 A 1289 LEU ASP LEU ASP SER SER GLU VAL THR VAL TYR GLY ASP
SEQRES 82 A 1289 ASP ILE ILE LEU PRO SER CYS ALA VAL PRO ALA LEU ARG
SEQRES 83 A 1289 GLU VAL PHE LYS TYR VAL GLY PHE THR THR ASN THR LYS
SEQRES 84 A 1289 LYS THR PHE SER GLU GLY PRO PHE ARG GLU SER CYS GLY
SEQRES 85 A 1289 LYS HIS TYR TYR SER GLY VAL ASP VAL THR PRO PHE TYR
SEQRES 86 A 1289 ILE ARG HIS ARG ILE VAL SER PRO ALA ASP LEU ILE LEU
SEQRES 87 A 1289 VAL LEU ASN ASN LEU TYR ARG TRP ALA THR ILE ASP GLY
SEQRES 88 A 1289 VAL TRP ASP PRO ARG ALA HIS SER VAL TYR LEU LYS TYR
SEQRES 89 A 1289 ARG LYS LEU LEU PRO LYS GLN LEU GLN ARG ASN THR ILE
SEQRES 90 A 1289 PRO ASP GLY TYR GLY ASP GLY ALA LEU VAL GLY SER VAL
SEQRES 91 A 1289 LEU ILE ASN PRO PHE ALA LYS ASN ARG GLY TRP ILE ARG
SEQRES 92 A 1289 TYR VAL PRO VAL ILE THR ASP HIS THR ARG ASP ARG GLU
SEQRES 93 A 1289 ARG ALA GLU LEU GLY SER TYR LEU TYR ASP LEU PHE SER
SEQRES 94 A 1289 ARG CYS LEU SER GLU SER ASN ASP GLY LEU PRO LEU ARG
SEQRES 95 A 1289 GLY PRO SER GLY CYS ASP SER ALA ASP LEU PHE ALA ILE
SEQRES 96 A 1289 ASP GLN LEU ILE CYS ARG SER ASN PRO THR LYS ILE SER
SEQRES 97 A 1289 ARG SER THR GLY LYS PHE ASP ILE GLN TYR ILE ALA CYS
SEQRES 98 A 1289 SER SER ARG VAL LEU ALA PRO TYR GLY VAL PHE GLN GLY
SEQRES 99 A 1289 THR LYS VAL ALA SER LEU HIS GLU ALA HIS HIS HIS HIS
SEQRES 100 A 1289 HIS HIS
SEQRES 1 G 7 C C C U A C C
SEQRES 1 T 8 G G G U A G G G
HET CH1 A2501 28
HET CA A2502 1
HET CA A2503 1
HETNAM CH1 3'-DEOXY-CYTIDINE-5'-TRIPHOSPHATE
HETNAM CA CALCIUM ION
FORMUL 4 CH1 C9 H16 N3 O13 P3
FORMUL 5 CA 2(CA 2+)
FORMUL 7 HOH *47(H2 O)
HELIX 1 1 THR A 5 ARG A 15 1 11
HELIX 2 2 GLY A 19 GLU A 29 1 11
HELIX 3 3 ASP A 33 LYS A 43 1 11
HELIX 4 4 SER A 44 ALA A 50 1 7
HELIX 5 5 THR A 80 LYS A 85 1 6
HELIX 6 6 ASP A 86 ALA A 102 1 17
HELIX 7 7 ASP A 107 GLN A 114 1 8
HELIX 8 8 PHE A 115 GLY A 127 1 13
HELIX 9 9 ASP A 162 LYS A 177 1 16
HELIX 10 10 LYS A 182 VAL A 186 5 5
HELIX 11 11 GLU A 194 GLN A 204 1 11
HELIX 12 12 PRO A 208 VAL A 227 1 20
HELIX 13 13 SER A 228 GLN A 232 5 5
HELIX 14 14 THR A 241 GLU A 248 1 8
HELIX 15 15 PHE A 272 LYS A 281 1 10
HELIX 16 16 GLN A 282 HIS A 284 5 3
HELIX 17 17 GLY A 308 THR A 323 1 16
HELIX 18 18 GLY A 368 THR A 378 1 11
HELIX 19 19 GLN A 399 GLY A 411 1 13
HELIX 20 20 LYS A 421 VAL A 425 5 5
HELIX 21 21 ASP A 427 TYR A 445 1 19
HELIX 22 22 PRO A 448 THR A 452 5 5
HELIX 23 23 SER A 458 GLU A 464 1 7
HELIX 24 24 TRP A 469 ILE A 484 1 16
HELIX 25 25 ARG A 489 LYS A 493 5 5
HELIX 26 26 LYS A 567 ILE A 571 5 5
HELIX 27 27 ARG A 702 ASN A 714 1 13
HELIX 28 28 ASN A 722 TYR A 735 1 14
HELIX 29 29 SER A 742 ILE A 747 1 6
HELIX 30 30 THR A 756 ILE A 769 1 14
HELIX 31 31 GLU A 783 TYR A 805 1 23
HELIX 32 32 SER A 816 GLY A 834 1 19
HELIX 33 33 SER A 838 CYS A 846 1 9
HELIX 34 34 ASN A 857 GLY A 861 5 5
HELIX 35 35 HIS A 862 PHE A 867 1 6
HELIX 36 36 THR A 874 ARG A 876 5 3
HELIX 37 37 ALA A 877 ALA A 886 1 10
HELIX 38 38 PRO A 920 LEU A 938 1 19
HELIX 39 39 ARG A 939 GLY A 942 5 4
HELIX 40 40 GLN A 948 ASN A 962 1 15
HELIX 41 41 ALA A 971 SER A 975 5 5
HELIX 42 42 SER A 977 LEU A 985 1 9
HELIX 43 43 PRO A 986 ARG A 997 1 12
HELIX 44 44 TYR A 1021 LEU A 1041 1 21
HELIX 45 45 ASP A 1044 VAL A 1048 5 5
HELIX 46 46 ALA A 1061 VAL A 1072 1 12
HELIX 47 47 SER A 1112 ALA A 1127 1 16
HELIX 48 48 ASP A 1134 LYS A 1146 1 13
HELIX 49 49 PRO A 1149 ASN A 1155 1 7
HELIX 50 50 SER A 1169 ASN A 1173 5 5
HELIX 51 51 ALA A 1198 SER A 1215 1 18
HELIX 52 52 ASP A 1236 CYS A 1240 5 5
SHEET 1 A 3 ASP A 59 ASP A 67 0
SHEET 2 A 3 TYR A 70 CYS A 78 -1 O TYR A 70 N ASP A 67
SHEET 3 A 3 ASN A 131 GLU A 139 -1 O ARG A 133 N GLU A 75
SHEET 1 B 3 VAL A 142 HIS A 148 0
SHEET 2 B 3 ILE A 152 LYS A 159 -1 O VAL A 156 N GLY A 144
SHEET 3 B 3 GLU A 252 GLU A 260 -1 O GLY A 255 N ALA A 157
SHEET 1 C 6 VAL A 352 THR A 356 0
SHEET 2 C 6 ARG A 359 ASP A 365 -1 O HIS A 363 N VAL A 352
SHEET 3 C 6 HIS A 296 GLY A 303 1 N VAL A 299 O ALA A 362
SHEET 4 C 6 GLY A 385 ALA A 391 1 O VAL A 389 N ILE A 302
SHEET 5 C 6 ILE A 415 ASN A 420 1 O ASN A 420 N VAL A 390
SHEET 6 C 6 ILE A 454 ARG A 456 1 O VAL A 455 N VAL A 417
SHEET 1 D 7 LEU A 496 PRO A 498 0
SHEET 2 D 7 VAL A 576 ALA A 578 -1 O LEU A 577 N LEU A 497
SHEET 3 D 7 GLU A 526 VAL A 530 -1 N GLU A 528 O ALA A 578
SHEET 4 D 7 GLN A 536 GLU A 544 -1 O GLN A 536 N ILE A 529
SHEET 5 D 7 ASN A 558 LEU A 563 -1 O LEU A 562 N THR A 541
SHEET 6 D 7 THR A 510 ARG A 515 -1 N VAL A 512 O VAL A 561
SHEET 7 D 7 ASP A 501 SER A 504 -1 N PHE A 503 O VAL A 511
SHEET 1 E 5 LEU A 496 PRO A 498 0
SHEET 2 E 5 VAL A 576 ALA A 578 -1 O LEU A 577 N LEU A 497
SHEET 3 E 5 GLU A 526 VAL A 530 -1 N GLU A 528 O ALA A 578
SHEET 4 E 5 GLN A 536 GLU A 544 -1 O GLN A 536 N ILE A 529
SHEET 5 E 5 LEU A 549 LEU A 550 -1 O LEU A 550 N VAL A 543
SHEET 1 F 2 ILE A 520 LYS A 522 0
SHEET 2 F 2 GLU A 552 ARG A 554 -1 O GLY A 553 N ILE A 521
SHEET 1 G 7 PRO A 585 ILE A 595 0
SHEET 2 G 7 ASN A 640 ALA A 652 -1 O ILE A 641 N VAL A 593
SHEET 3 G 7 ASP A 621 GLU A 627 -1 N THR A 625 O THR A 646
SHEET 4 G 7 GLN A 614 TYR A 616 -1 N PHE A 615 O VAL A 622
SHEET 5 G 7 ARG A 658 GLU A 663 -1 O ARG A 662 N GLN A 614
SHEET 6 G 7 ARG A 666 VAL A 676 -1 O VAL A 668 N ILE A 661
SHEET 7 G 7 PRO A 585 ILE A 595 -1 N GLU A 590 O ALA A 674
SHEET 1 H 2 GLN A 871 CYS A 873 0
SHEET 2 H 2 ILE A 894 ILE A 897 1 O ASP A 896 N CYS A 873
SHEET 1 I 4 THR A 912 ILE A 918 0
SHEET 2 I 4 PHE A 900 ASN A 909 -1 N VAL A 906 O ARG A 914
SHEET 3 I 4 LYS A1000 ARG A1002 1 O ARG A1002 N ASN A 901
SHEET 4 I 4 VAL A1008 THR A1010 -1 O VAL A1009 N GLY A1001
SHEET 1 J 3 LEU A 964 VAL A 967 0
SHEET 2 J 3 ASP A1054 PRO A1058 -1 O LEU A1057 N ALA A 965
SHEET 3 J 3 THR A1049 TYR A1051 -1 N THR A1049 O ILE A1056
SHEET 1 K 3 PHE A1087 SER A1090 0
SHEET 2 K 3 LYS A1093 TYR A1096 -1 O TYR A1095 N ARG A1088
SHEET 3 K 3 VAL A1099 ASP A1100 -1 O VAL A1099 N TYR A1096
SHEET 1 L 2 THR A1128 ILE A1129 0
SHEET 2 L 2 VAL A1132 TRP A1133 -1 O VAL A1132 N ILE A1129
SHEET 1 M 2 THR A1156 ILE A1157 0
SHEET 2 M 2 LEU A1166 VAL A1167 1 O LEU A1166 N ILE A1157
SHEET 1 N 3 LYS A1177 ARG A1179 0
SHEET 2 N 3 ILE A1182 ASP A1194 -1 O TYR A1184 N LYS A1177
SHEET 3 N 3 SER A1248 CYS A1261 -1 O ASP A1255 N THR A1189
LINK OD2 ASP A 968 CA CA A2502 1555 1555 2.67
LINK OD2 ASP A 968 CA CA A2503 1555 1555 2.72
LINK O LEU A 969 CA CA A2502 1555 1555 2.31
LINK OD2 ASP A1053 CA CA A2502 1555 1555 2.73
LINK OD1 ASP A1053 CA CA A2503 1555 1555 2.88
LINK OD2 ASP A1054 CA CA A2503 1555 1555 2.68
LINK O3G CH1 A2501 CA CA A2502 1555 1555 2.52
LINK O2A CH1 A2501 CA CA A2502 1555 1555 2.56
LINK O2B CH1 A2501 CA CA A2502 1555 1555 2.64
LINK CA CA A2503 O3' C G2007 1555 1555 2.70
SITE 1 AC1 17 LYS A 908 ARG A 914 ASP A 968 LEU A 969
SITE 2 AC1 17 SER A 970 ALA A 971 ALA A 972 SER A 973
SITE 3 AC1 17 MET A1017 GLU A1026 ASP A1053 CA A2502
SITE 4 AC1 17 CA A2503 HOH A3510 C G2007 G T2101
SITE 5 AC1 17 G T2102
SITE 1 AC2 4 ASP A 968 LEU A 969 ASP A1053 CH1 A2501
SITE 1 AC3 5 ASP A 968 ASP A1053 ASP A1054 CH1 A2501
SITE 2 AC3 5 C G2007
CRYST1 139.730 256.040 101.720 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007157 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009831 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
