HEADER TRANSLATION, TRANSFERASE/RNA 18-JAN-12 3VNU
TITLE COMPLEX STRUCTURE OF VIRAL RNA POLYMERASE I
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*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 3VNU 1 REMARK SEQADV LINK
REVDAT 3 28-JUN-17 3VNU 1 SOURCE
REVDAT 2 09-OCT-13 3VNU 1 JRNL
REVDAT 1 08-AUG-12 3VNU 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. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.480
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 27520
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.276
REMARK 3 R VALUE (WORKING SET) : 0.274
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1441
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1700
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.4700
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.4900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9287
REMARK 3 NUCLEIC ACID ATOMS : 252
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.25000
REMARK 3 B22 (A**2) : 1.25000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.617
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.497
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.105
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.871
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.839
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9770 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13274 ; 1.330 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1198 ; 5.583 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 415 ;40.998 ;23.831
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1645 ;19.851 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;16.159 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1499 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7239 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3VNU 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_1000095278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-10
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 : 31696
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
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 (%): 59.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
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 50.71250
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 50.71250
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 69.50250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 127.75300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 69.50250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 127.75300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 50.71250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 69.50250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 127.75300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 50.71250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 69.50250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 127.75300
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: 4120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 A3108 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 465 C G 2001
REMARK 465 C G 2002
REMARK 465 G T 2107
REMARK 465 G T 2108
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 470 C G2008 O3'
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLU A 260 OE1 GLU A 263 1.08
REMARK 500 O GLU A 260 CD GLU A 263 1.25
REMARK 500 C GLU A 260 OE1 GLU A 263 1.51
REMARK 500 NH1 ARG A 508 OE1 GLU A 544 1.51
REMARK 500 O LEU A 246 O HIS A 249 1.52
REMARK 500 N GLU A 260 OE2 GLU A 263 1.54
REMARK 500 CA GLU A 260 OE2 GLU A 263 1.57
REMARK 500 O GLU A 260 OE2 GLU A 263 1.62
REMARK 500 C GLU A 260 OE2 GLU A 263 1.73
REMARK 500 C GLU A 260 CD GLU A 263 1.77
REMARK 500 NH1 ARG A 508 CD GLU A 544 1.81
REMARK 500 NH1 ARG A 508 OE2 GLU A 544 1.87
REMARK 500 CB GLU A 260 OE2 GLU A 263 1.95
REMARK 500 O GLN A 244 CG GLU A 248 2.10
REMARK 500 N VAL A 261 OE1 GLU A 263 2.10
REMARK 500 O VAL A 261 OE1 GLU A 263 2.12
REMARK 500 C VAL A 261 OE1 GLU A 263 2.12
REMARK 500 O GLU A 768 OG SER A 771 2.13
REMARK 500 O GLY A 303 NZ LYS A 309 2.17
REMARK 500 OD1 ASP A 1206 NH1 ARG A 1210 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A1159 CB - CG - OD1 ANGL. DEV. = 6.1 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 -92.91 -120.28
REMARK 500 SER A 7 -73.46 -57.87
REMARK 500 ARG A 13 -70.77 -92.98
REMARK 500 ALA A 30 -6.84 -147.83
REMARK 500 ASN A 69 51.89 -150.88
REMARK 500 GLU A 75 40.69 -149.55
REMARK 500 CYS A 78 -153.83 -115.25
REMARK 500 ALA A 87 22.52 -79.83
REMARK 500 LYS A 104 67.74 -63.52
REMARK 500 THR A 106 57.55 -112.69
REMARK 500 ILE A 126 -81.24 -99.92
REMARK 500 ASN A 129 64.08 -65.15
REMARK 500 ILE A 130 94.26 -69.06
REMARK 500 ARG A 133 -68.83 -106.35
REMARK 500 ASP A 141 -77.12 -62.39
REMARK 500 ALA A 158 -162.26 -108.18
REMARK 500 LYS A 159 84.27 -163.60
REMARK 500 ASP A 162 -155.75 -145.06
REMARK 500 LEU A 165 -58.21 -126.09
REMARK 500 LYS A 177 69.79 36.96
REMARK 500 PRO A 208 162.56 -49.66
REMARK 500 LYS A 209 -71.27 -44.91
REMARK 500 GLU A 210 13.25 -68.98
REMARK 500 ILE A 211 -61.57 -100.41
REMARK 500 THR A 230 -76.29 -57.51
REMARK 500 PRO A 233 107.03 -50.42
REMARK 500 PHE A 256 139.41 -170.53
REMARK 500 GLU A 266 -128.41 59.81
REMARK 500 LYS A 267 -175.01 87.35
REMARK 500 THR A 323 -97.58 -105.07
REMARK 500 LYS A 374 30.12 -82.03
REMARK 500 ASN A 375 -38.62 -141.61
REMARK 500 ALA A 381 81.78 -160.76
REMARK 500 LYS A 421 71.66 55.69
REMARK 500 PRO A 448 64.92 -67.66
REMARK 500 ASP A 466 90.28 -63.68
REMARK 500 SER A 482 -51.01 -131.27
REMARK 500 GLU A 488 99.22 -61.15
REMARK 500 MET A 545 -151.31 -114.23
REMARK 500 PHE A 546 -70.42 -82.96
REMARK 500 LEU A 550 -169.38 -77.62
REMARK 500 HIS A 604 31.93 -77.32
REMARK 500 PHE A 608 -137.17 -118.49
REMARK 500 PHE A 617 -81.07 -95.79
REMARK 500 THR A 619 -38.74 -137.76
REMARK 500 PRO A 650 152.30 -45.26
REMARK 500 ARG A 658 99.35 -63.88
REMARK 500 GLU A 720 84.30 -65.51
REMARK 500 SER A 748 12.32 -158.79
REMARK 500 PHE A 753 66.61 -104.88
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
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 OD1
REMARK 620 2 LEU A 969 O 87.8
REMARK 620 3 ASP A1053 OD2 59.1 95.4
REMARK 620 4 ATP A2501 O2A 73.2 145.9 98.6
REMARK 620 5 ATP A2501 O2B 138.4 132.9 114.2 67.2
REMARK 620 6 ATP A2501 O2G 89.1 70.7 146.3 80.7 96.7
REMARK 620 7 ATP A2501 O3B 132.0 94.5 165.5 78.8 51.5 47.8
REMARK 620 N 1 2 3 4 5 6
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 OD1
REMARK 620 2 ASP A1053 OD1 61.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP 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: 3VNV RELATED DB: PDB
DBREF 3VNU A 1 283 UNP P0A6P3 EFTS_ECO57 1 283
DBREF 3VNU A 285 678 UNP P0A6N3 EFTU_ECO57 1 394
DBREF 3VNU A 679 694 PDB 3VNU 3VNU 679 694
DBREF 3VNU A 695 1283 UNP Q8LTE0 Q8LTE0_BPQBE 1 589
DBREF 3VNU G 2001 2008 PDB 3VNU 3VNU 2001 2008
DBREF 3VNU T 2101 2108 PDB 3VNU 3VNU 2101 2108
SEQADV 3VNU HIS A 284 UNP P0A6P3 LINKER
SEQADV 3VNU HIS A 1284 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNU HIS A 1285 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNU HIS A 1286 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNU HIS A 1287 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNU HIS A 1288 UNP Q8LTE0 EXPRESSION TAG
SEQADV 3VNU 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 8 C C C U A C C C
SEQRES 1 T 8 G G G U A G G G
HET ATP A2501 31
HET CA A2502 1
HET CA A2503 1
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM CA CALCIUM ION
FORMUL 4 ATP C10 H16 N5 O13 P3
FORMUL 5 CA 2(CA 2+)
FORMUL 7 HOH *12(H2 O)
HELIX 1 1 ALA A 6 LYS A 10 5 5
HELIX 2 2 MET A 20 LYS A 25 1 6
HELIX 3 3 ILE A 34 SER A 44 1 11
HELIX 4 4 GLY A 45 LYS A 52 1 8
HELIX 5 5 THR A 80 LYS A 85 1 6
HELIX 6 6 GLY A 88 ASP A 94 1 7
HELIX 7 7 ASP A 98 GLY A 103 1 6
HELIX 8 8 ASP A 107 PHE A 115 1 9
HELIX 9 9 PHE A 115 ALA A 124 1 10
HELIX 10 10 LEU A 165 LYS A 177 1 13
HELIX 11 11 SER A 187 GLY A 206 1 20
HELIX 12 12 PRO A 208 SER A 228 1 21
HELIX 13 13 THR A 241 HIS A 249 1 9
HELIX 14 14 ASP A 271 MET A 285 1 15
HELIX 15 15 VAL A 305 HIS A 307 5 3
HELIX 16 16 GLY A 308 THR A 323 1 16
HELIX 17 17 HIS A 369 ILE A 377 1 9
HELIX 18 18 GLN A 399 GLN A 409 1 11
HELIX 19 19 ASP A 427 GLN A 444 1 18
HELIX 20 20 PRO A 448 THR A 452 5 5
HELIX 21 21 SER A 458 GLU A 464 1 7
HELIX 22 22 ASP A 466 GLY A 478 1 13
HELIX 23 23 LYS A 567 ILE A 571 5 5
HELIX 24 24 SER A 597 GLY A 601 5 5
HELIX 25 25 ARG A 702 ASN A 714 1 13
HELIX 26 26 ASN A 722 LEU A 733 1 12
HELIX 27 27 ALA A 734 GLY A 736 5 3
HELIX 28 28 ALA A 744 SER A 748 5 5
HELIX 29 29 THR A 756 MET A 770 1 15
HELIX 30 30 GLU A 783 LEU A 804 1 22
HELIX 31 31 SER A 816 GLY A 834 1 19
HELIX 32 32 VAL A 839 ARG A 844 1 6
HELIX 33 33 PRO A 863 ALA A 868 1 6
HELIX 34 34 THR A 874 ARG A 876 5 3
HELIX 35 35 ALA A 877 ALA A 886 1 10
HELIX 36 36 PRO A 920 ARG A 937 1 18
HELIX 37 37 LEU A 938 CYS A 940 5 3
HELIX 38 38 GLN A 948 ASN A 962 1 15
HELIX 39 39 ALA A 971 ILE A 976 1 6
HELIX 40 40 SER A 977 LEU A 985 1 9
HELIX 41 41 PRO A 986 LEU A 996 1 11
HELIX 42 42 TYR A 1021 ILE A 1040 1 20
HELIX 43 43 ASP A 1044 VAL A 1048 5 5
HELIX 44 44 ALA A 1061 VAL A 1072 1 12
HELIX 45 45 SER A 1112 ALA A 1127 1 16
HELIX 46 46 ASP A 1134 LYS A 1146 1 13
HELIX 47 47 LYS A 1150 ASN A 1155 1 6
HELIX 48 48 ALA A 1198 SER A 1213 1 16
SHEET 1 A 3 THR A 64 ILE A 66 0
SHEET 2 A 3 TYR A 70 ASN A 77 -1 O ILE A 72 N LYS A 65
SHEET 3 A 3 ASN A 131 GLU A 139 -1 O ALA A 136 N ILE A 73
SHEET 1 B 3 VAL A 142 GLY A 144 0
SHEET 2 B 3 ILE A 152 ALA A 158 -1 O ALA A 158 N VAL A 142
SHEET 3 B 3 GLN A 147 HIS A 148 -1 N HIS A 148 O ILE A 152
SHEET 1 C 3 VAL A 142 GLY A 144 0
SHEET 2 C 3 ILE A 152 ALA A 158 -1 O ALA A 158 N VAL A 142
SHEET 3 C 3 GLY A 255 GLU A 260 -1 O ILE A 257 N LEU A 155
SHEET 1 D 6 HIS A 351 VAL A 352 0
SHEET 2 D 6 HIS A 360 ASP A 365 -1 O HIS A 363 N VAL A 352
SHEET 3 D 6 HIS A 296 GLY A 303 1 N VAL A 299 O ALA A 362
SHEET 4 D 6 GLY A 385 ALA A 391 1 O ILE A 387 N GLY A 300
SHEET 5 D 6 ILE A 416 ASN A 420 1 O ILE A 416 N LEU A 388
SHEET 6 D 6 ILE A 454 ARG A 456 1 O VAL A 455 N LEU A 419
SHEET 1 E 7 LEU A 496 PRO A 498 0
SHEET 2 E 7 VAL A 576 ALA A 578 -1 O LEU A 577 N LEU A 497
SHEET 3 E 7 GLU A 526 VAL A 530 -1 N VAL A 530 O VAL A 576
SHEET 4 E 7 GLN A 536 GLU A 544 -1 O SER A 538 N VAL A 527
SHEET 5 E 7 GLU A 557 LEU A 563 -1 O LEU A 562 N GLY A 542
SHEET 6 E 7 GLY A 509 VAL A 516 -1 N THR A 510 O LEU A 563
SHEET 7 E 7 ASP A 501 ILE A 505 -1 N PHE A 503 O VAL A 511
SHEET 1 F 2 ILE A 521 LYS A 522 0
SHEET 2 F 2 GLU A 552 GLY A 553 -1 O GLY A 553 N ILE A 521
SHEET 1 G 5 GLY A 624 THR A 625 0
SHEET 2 G 5 ASN A 640 MET A 653 -1 O THR A 646 N THR A 625
SHEET 3 G 5 LYS A 584 ILE A 595 -1 N SER A 591 O MET A 643
SHEET 4 G 5 ARG A 666 VAL A 676 -1 O LYS A 675 N GLU A 590
SHEET 5 G 5 ARG A 658 GLU A 663 -1 N GLU A 663 O ARG A 666
SHEET 1 H 2 LYS A 902 ALA A 903 0
SHEET 2 H 2 ALA A 917 ILE A 918 -1 O ILE A 918 N LYS A 902
SHEET 1 I 3 LEU A 964 VAL A 967 0
SHEET 2 I 3 ASP A1054 PRO A1058 -1 O ILE A1055 N VAL A 967
SHEET 3 I 3 THR A1049 TYR A1051 -1 N THR A1049 O ILE A1056
SHEET 1 J 2 LYS A1000 ARG A1002 0
SHEET 2 J 2 VAL A1008 THR A1010 -1 O VAL A1009 N GLY A1001
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 ARG A1195 -1 O TYR A1184 N LYS A1177
SHEET 3 N 3 ILE A1247 ALA A1260 -1 O ASP A1255 N THR A1189
LINK OD1 ASP A 968 CA CA A2502 1555 1555 2.50
LINK OD1 ASP A 968 CA CA A2503 1555 1555 2.78
LINK O LEU A 969 CA CA A2502 1555 1555 2.73
LINK OD2 ASP A1053 CA CA A2502 1555 1555 2.90
LINK OD1 ASP A1053 CA CA A2503 1555 1555 2.82
LINK O2A ATP A2501 CA CA A2502 1555 1555 2.55
LINK O2B ATP A2501 CA CA A2502 1555 1555 2.63
LINK O2G ATP A2501 CA CA A2502 1555 1555 2.99
LINK O3B ATP A2501 CA CA A2502 1555 1555 3.18
SITE 1 AC1 16 ARG A 914 ILE A 916 ASP A 968 LEU A 969
SITE 2 AC1 16 SER A 970 ALA A 971 ALA A 972 SER A 973
SITE 3 AC1 16 MET A1017 GLY A1018 GLU A1026 ASP A1053
SITE 4 AC1 16 ASN A1077 CA A2502 C G2008 G T2101
SITE 1 AC2 4 ASP A 968 LEU A 969 ASP A1053 ATP A2501
SITE 1 AC3 3 ASP A 968 ASP A1053 C G2008
CRYST1 139.005 255.506 101.425 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 0.007194 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003914 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009860 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
