HEADER TRANSFERASE/RNA 27-MAY-04 1TFW
TITLE HOW CCA IS ADDED TO THE 3' END OF IMMATURE TRNA WITHOUT THE USE OF AN
TITLE 2 OLIGONUCLEOTIDE TEMPLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-R(*GP*CP*GP*GP*AP*UP*CP*CP*GP*CP*AP*C)-3';
COMPND 3 CHAIN: E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-R(*GP*CP*GP*GP*AP*UP*CP*CP*GP*CP*AP*CP*C)-3';
COMPND 7 CHAIN: H, I, G;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: 5'-R(*GP*CP*GP*GP*AP*CP*CP*CP*GP*CP*AP*C)-3';
COMPND 11 CHAIN: F;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: 5'-R(*CP*GP*CP*GP*GP*AP*UP*CP*CP*GP*CP*AP*C)-3';
COMPND 15 CHAIN: J;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 5;
COMPND 18 MOLECULE: TRNA NUCLEOTIDYLTRANSFERASE;
COMPND 19 CHAIN: A, B, C, D;
COMPND 20 SYNONYM: TRNA ADENYLYLTRANSFERASE, TRNA CCA-PYROPHOSPHORYLASE, CCA-
COMPND 21 ADDING ENZYME;
COMPND 22 EC: 2.7.7.25;
COMPND 23 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 MOL_ID: 4;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 MOL_ID: 5;
SOURCE 10 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 11 ORGANISM_TAXID: 2234;
SOURCE 12 GENE: CCA, AF2156;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS CCA-ADDING COMPLEX, TRANSFERASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XIONG,T.A.STEITZ
REVDAT 4 23-AUG-23 1TFW 1 REMARK LINK
REVDAT 3 13-JUL-11 1TFW 1 VERSN
REVDAT 2 24-FEB-09 1TFW 1 VERSN
REVDAT 1 10-AUG-04 1TFW 0
JRNL AUTH Y.XIONG,T.A.STEITZ
JRNL TITL MECHANISM OF TRANSFER RNA MATURATION BY CCA-ADDING ENZYME
JRNL TITL 2 WITHOUT USING AN OLIGONUCLEOTIDE TEMPLATE.
JRNL REF NATURE V. 430 640 2004
JRNL REFN ISSN 0028-0836
JRNL PMID 15295590
JRNL DOI 10.1038/NATURE02711
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 122568
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6447
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.35
REMARK 3 REFLECTION IN BIN (WORKING SET) : 21803
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 1125
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14520
REMARK 3 NUCLEIC ACID ATOMS : 1598
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 1059
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -0.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.245
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.203
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.938
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16697 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 14375 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22820 ; 1.165 ; 2.096
REMARK 3 BOND ANGLES OTHERS (DEGREES): 33528 ; 0.956 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1744 ; 5.465 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 776 ;32.431 ;22.784
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2780 ;16.543 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 160 ;16.813 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2454 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17182 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3372 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3237 ; 0.187 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 14494 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7693 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 9024 ; 0.077 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 833 ; 0.147 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.032 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.070 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.120 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 37 ; 0.212 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.097 ; 0.200
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): 11403 ; 1.272 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3540 ; 0.292 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14056 ; 1.450 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9912 ; 2.450 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8764 ; 3.329 ; 8.000
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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 135 5
REMARK 3 1 D 1 D 135 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 B (A): 795 ; 0.25 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 B (A): 1378 ; 0.77 ; 5.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 795 ; 0.25 ; 2.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1378 ; 0.71 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 90 2
REMARK 3 1 C 1 C 90 2
REMARK 3 2 A 101 A 135 5
REMARK 3 2 C 101 C 135 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 531 ; 0.03 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 A (A): 1137 ; 0.35 ; 0.50
REMARK 3 LOOSE POSITIONAL 2 A (A): 336 ; 0.60 ; 5.00
REMARK 3 TIGHT THERMAL 2 A (A**2): 531 ; 0.09 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 1137 ; 0.48 ; 2.00
REMARK 3 LOOSE THERMAL 2 A (A**2): 336 ; 0.91 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 136 A 437 5
REMARK 3 1 B 136 B 437 5
REMARK 3 1 C 136 C 437 5
REMARK 3 1 D 136 D 437 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 1781 ; 0.29 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 B (A): 1781 ; 0.19 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 C (A): 1781 ; 0.36 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 D (A): 1781 ; 0.39 ; 0.50
REMARK 3 LOOSE POSITIONAL 3 A (A): 3110 ; 0.60 ; 5.00
REMARK 3 LOOSE POSITIONAL 3 B (A): 3110 ; 0.59 ; 5.00
REMARK 3 LOOSE POSITIONAL 3 C (A): 3110 ; 0.71 ; 5.00
REMARK 3 LOOSE POSITIONAL 3 D (A): 3110 ; 0.76 ; 5.00
REMARK 3 MEDIUM THERMAL 3 A (A**2): 1781 ; 0.56 ; 2.00
REMARK 3 MEDIUM THERMAL 3 B (A**2): 1781 ; 0.58 ; 2.00
REMARK 3 MEDIUM THERMAL 3 C (A**2): 1781 ; 0.69 ; 2.00
REMARK 3 MEDIUM THERMAL 3 D (A**2): 1781 ; 0.62 ; 2.00
REMARK 3 LOOSE THERMAL 3 A (A**2): 3110 ; 1.55 ; 10.00
REMARK 3 LOOSE THERMAL 3 B (A**2): 3110 ; 1.60 ; 10.00
REMARK 3 LOOSE THERMAL 3 C (A**2): 3110 ; 1.73 ; 10.00
REMARK 3 LOOSE THERMAL 3 D (A**2): 3110 ; 1.84 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 1 E 12 5
REMARK 3 1 F 1 F 12 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 4 E (A): 322 ; 0.28 ; 5.00
REMARK 3 LOOSE THERMAL 4 E (A**2): 322 ; 1.83 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 17 A 124
REMARK 3 ORIGIN FOR THE GROUP (A): 77.7445 32.6165 35.4538
REMARK 3 T TENSOR
REMARK 3 T11: -0.1479 T22: -0.0729
REMARK 3 T33: 0.0121 T12: -0.0457
REMARK 3 T13: 0.0799 T23: 0.0805
REMARK 3 L TENSOR
REMARK 3 L11: 12.5969 L22: 3.5513
REMARK 3 L33: 4.3872 L12: -3.7920
REMARK 3 L13: -1.0773 L23: -0.5811
REMARK 3 S TENSOR
REMARK 3 S11: 0.1841 S12: -0.6854 S13: 0.9710
REMARK 3 S21: 0.0023 S22: -0.1097 S23: -0.5199
REMARK 3 S31: -0.1588 S32: 0.3430 S33: -0.0744
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 125 A 258
REMARK 3 RESIDUE RANGE : A 1 A 16
REMARK 3 ORIGIN FOR THE GROUP (A): 54.0302 33.4959 45.9387
REMARK 3 T TENSOR
REMARK 3 T11: -0.3102 T22: -0.1216
REMARK 3 T33: -0.2355 T12: -0.0331
REMARK 3 T13: -0.0207 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 1.9808 L22: 2.3821
REMARK 3 L33: 2.9676 L12: -0.1528
REMARK 3 L13: -0.5699 L23: 1.0346
REMARK 3 S TENSOR
REMARK 3 S11: 0.1060 S12: 0.2581 S13: 0.1501
REMARK 3 S21: -0.1784 S22: -0.2291 S23: 0.0134
REMARK 3 S31: -0.0077 S32: -0.4362 S33: 0.1231
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 259 A 437
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0057 53.3518 77.4628
REMARK 3 T TENSOR
REMARK 3 T11: -0.2184 T22: -0.2299
REMARK 3 T33: -0.0725 T12: -0.0557
REMARK 3 T13: -0.0627 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 1.5268 L22: 0.5603
REMARK 3 L33: 3.1554 L12: -0.1312
REMARK 3 L13: -0.9623 L23: 0.2552
REMARK 3 S TENSOR
REMARK 3 S11: 0.0632 S12: -0.0697 S13: 0.1569
REMARK 3 S21: 0.0116 S22: 0.0746 S23: -0.2299
REMARK 3 S31: -0.3391 S32: 0.1507 S33: -0.1378
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 17 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9274 39.5329 131.3273
REMARK 3 T TENSOR
REMARK 3 T11: 0.4717 T22: 0.4921
REMARK 3 T33: 0.1831 T12: 0.3865
REMARK 3 T13: 0.3438 T23: 0.3464
REMARK 3 L TENSOR
REMARK 3 L11: 7.1872 L22: 3.2277
REMARK 3 L33: 10.3753 L12: 0.6353
REMARK 3 L13: 2.6205 L23: 0.3812
REMARK 3 S TENSOR
REMARK 3 S11: -0.1788 S12: -0.8034 S13: 0.0812
REMARK 3 S21: 0.9991 S22: 0.4790 S23: 0.8453
REMARK 3 S31: -0.2771 S32: -1.2438 S33: -0.3002
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 125 B 258
REMARK 3 RESIDUE RANGE : B 1 B 16
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5938 37.3197 123.6952
REMARK 3 T TENSOR
REMARK 3 T11: 0.2461 T22: 0.1281
REMARK 3 T33: -0.2543 T12: 0.1793
REMARK 3 T13: -0.0728 T23: 0.1112
REMARK 3 L TENSOR
REMARK 3 L11: 2.6131 L22: 3.6780
REMARK 3 L33: 4.9382 L12: -0.3699
REMARK 3 L13: 0.3246 L23: -1.9503
REMARK 3 S TENSOR
REMARK 3 S11: -0.1856 S12: -0.5374 S13: -0.0004
REMARK 3 S21: 0.9544 S22: 0.2163 S23: -0.0800
REMARK 3 S31: -0.4550 S32: -0.0516 S33: -0.0307
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 259 B 437
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3399 54.3871 90.8262
REMARK 3 T TENSOR
REMARK 3 T11: -0.1713 T22: -0.1682
REMARK 3 T33: -0.1951 T12: 0.0798
REMARK 3 T13: -0.0248 T23: 0.0700
REMARK 3 L TENSOR
REMARK 3 L11: 2.0524 L22: 0.9286
REMARK 3 L33: 3.0665 L12: -0.3845
REMARK 3 L13: -0.9475 L23: 0.2702
REMARK 3 S TENSOR
REMARK 3 S11: -0.0674 S12: -0.1660 S13: 0.0621
REMARK 3 S21: 0.2689 S22: 0.1405 S23: -0.0055
REMARK 3 S31: -0.3854 S32: -0.2250 S33: -0.0731
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 17 C 124
REMARK 3 ORIGIN FOR THE GROUP (A): 67.4005 24.1667 97.8409
REMARK 3 T TENSOR
REMARK 3 T11: -0.0807 T22: 0.1328
REMARK 3 T33: 0.0288 T12: 0.0714
REMARK 3 T13: -0.0009 T23: 0.0928
REMARK 3 L TENSOR
REMARK 3 L11: 3.5768 L22: 10.4886
REMARK 3 L33: 3.4552 L12: -3.8411
REMARK 3 L13: -1.9117 L23: 3.2568
REMARK 3 S TENSOR
REMARK 3 S11: -0.2565 S12: -0.3117 S13: 0.1770
REMARK 3 S21: -0.1577 S22: 0.4167 S23: -0.8871
REMARK 3 S31: 0.0296 S32: 0.4126 S33: -0.1602
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 125 C 258
REMARK 3 RESIDUE RANGE : C 1 C 16
REMARK 3 ORIGIN FOR THE GROUP (A): 69.0406 4.6025 81.1417
REMARK 3 T TENSOR
REMARK 3 T11: -0.2175 T22: -0.2421
REMARK 3 T33: 0.0456 T12: -0.0273
REMARK 3 T13: 0.0914 T23: 0.1184
REMARK 3 L TENSOR
REMARK 3 L11: 3.4851 L22: 3.1103
REMARK 3 L33: 2.7692 L12: -0.8419
REMARK 3 L13: -1.0134 L23: 0.5775
REMARK 3 S TENSOR
REMARK 3 S11: -0.2476 S12: -0.1953 S13: -0.6319
REMARK 3 S21: 0.3945 S22: 0.0846 S23: 0.4464
REMARK 3 S31: 0.3184 S32: -0.2224 S33: 0.1630
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 259 C 437
REMARK 3 ORIGIN FOR THE GROUP (A): 98.3427 18.5962 60.8408
REMARK 3 T TENSOR
REMARK 3 T11: -0.2830 T22: -0.3360
REMARK 3 T33: -0.1018 T12: -0.0021
REMARK 3 T13: 0.0068 T23: 0.0623
REMARK 3 L TENSOR
REMARK 3 L11: 1.3355 L22: 1.1129
REMARK 3 L33: 1.4478 L12: -0.2265
REMARK 3 L13: -0.0755 L23: 0.3030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0827 S12: 0.0169 S13: 0.1391
REMARK 3 S21: 0.0449 S22: -0.1075 S23: -0.2223
REMARK 3 S31: 0.0448 S32: 0.2075 S33: 0.0248
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 17 D 124
REMARK 3 ORIGIN FOR THE GROUP (A): 98.8265 -2.1139 -2.7093
REMARK 3 T TENSOR
REMARK 3 T11: 0.6203 T22: 0.5651
REMARK 3 T33: 0.3047 T12: 0.3039
REMARK 3 T13: -0.0027 T23: -0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 0.3121 L22: 7.2228
REMARK 3 L33: 10.6714 L12: 0.5024
REMARK 3 L13: -1.6687 L23: 0.6628
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: 0.9176 S13: -0.5259
REMARK 3 S21: -0.6146 S22: 0.1033 S23: -0.3464
REMARK 3 S31: 1.2371 S32: -0.0684 S33: -0.1304
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 125 D 258
REMARK 3 RESIDUE RANGE : D 1 D 16
REMARK 3 ORIGIN FOR THE GROUP (A): 96.0592 19.1483 10.0893
REMARK 3 T TENSOR
REMARK 3 T11: 0.1251 T22: 0.3379
REMARK 3 T33: -0.1204 T12: 0.3278
REMARK 3 T13: 0.1722 T23: 0.3226
REMARK 3 L TENSOR
REMARK 3 L11: 2.3524 L22: 2.8110
REMARK 3 L33: 6.1937 L12: -0.7123
REMARK 3 L13: 0.9539 L23: -1.0271
REMARK 3 S TENSOR
REMARK 3 S11: 0.3073 S12: 0.8674 S13: 0.2747
REMARK 3 S21: -0.6757 S22: -0.3329 S23: -0.2555
REMARK 3 S31: 0.6611 S32: 0.6343 S33: 0.0255
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 259 D 437
REMARK 3 ORIGIN FOR THE GROUP (A): 102.1580 1.0177 42.7292
REMARK 3 T TENSOR
REMARK 3 T11: 0.0514 T22: -0.1706
REMARK 3 T33: -0.1252 T12: 0.2261
REMARK 3 T13: 0.0307 T23: 0.0714
REMARK 3 L TENSOR
REMARK 3 L11: 1.1760 L22: 2.1143
REMARK 3 L33: 3.4860 L12: 0.0313
REMARK 3 L13: -0.6754 L23: -1.2930
REMARK 3 S TENSOR
REMARK 3 S11: 0.1002 S12: 0.3179 S13: -0.0214
REMARK 3 S21: -0.7398 S22: -0.3123 S23: -0.1741
REMARK 3 S31: 0.7884 S32: 0.4394 S33: 0.2121
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 12
REMARK 3 RESIDUE RANGE : H 63 H 75
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1157 34.1053 97.9671
REMARK 3 T TENSOR
REMARK 3 T11: 0.1624 T22: 0.1508
REMARK 3 T33: 0.0430 T12: -0.0385
REMARK 3 T13: -0.0042 T23: 0.1358
REMARK 3 L TENSOR
REMARK 3 L11: 4.2054 L22: 4.3356
REMARK 3 L33: 7.0187 L12: 0.2252
REMARK 3 L13: 3.2440 L23: -3.3449
REMARK 3 S TENSOR
REMARK 3 S11: 0.1149 S12: 0.2741 S13: -0.6683
REMARK 3 S21: -0.7312 S22: 0.4252 S23: 0.4585
REMARK 3 S31: 1.4569 S32: -0.4038 S33: -0.5401
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 12
REMARK 3 RESIDUE RANGE : I 63 I 75
REMARK 3 ORIGIN FOR THE GROUP (A): 84.3061 -5.0264 27.9400
REMARK 3 T TENSOR
REMARK 3 T11: 0.4309 T22: 0.1173
REMARK 3 T33: 0.1097 T12: -0.0672
REMARK 3 T13: -0.2059 T23: 0.0934
REMARK 3 L TENSOR
REMARK 3 L11: 3.5837 L22: 8.4797
REMARK 3 L33: 15.3298 L12: 1.6960
REMARK 3 L13: -1.2973 L23: -5.8958
REMARK 3 S TENSOR
REMARK 3 S11: 0.5319 S12: 0.1692 S13: -0.0475
REMARK 3 S21: -0.3571 S22: 0.4634 S23: 0.9829
REMARK 3 S31: 1.2071 S32: -1.5190 S33: -0.9953
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 14
REMARK 3 RESIDUE RANGE : J 61 J 73
REMARK 3 ORIGIN FOR THE GROUP (A): 75.5865 29.6286 68.2222
REMARK 3 T TENSOR
REMARK 3 T11: -0.2350 T22: -0.1937
REMARK 3 T33: -0.1416 T12: -0.0210
REMARK 3 T13: -0.0319 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 2.2497 L22: 8.8305
REMARK 3 L33: 2.0124 L12: -2.0323
REMARK 3 L13: 0.3741 L23: -4.0029
REMARK 3 S TENSOR
REMARK 3 S11: -0.1493 S12: -0.1765 S13: 0.0916
REMARK 3 S21: -0.0635 S22: -0.0912 S23: -0.4834
REMARK 3 S31: 0.1842 S32: 0.3039 S33: 0.2405
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1TFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022613.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122568
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 47.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.07200
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1R89
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 42.38500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, G, J, A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, I, C, D
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 A G 6 O5' A G 6 C5' -0.063
REMARK 500 U G 7 O3' C G 8 P 0.141
REMARK 500 GLU B 387 CG GLU B 387 CD 0.102
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 C G 9 C2 - N3 - C4 ANGL. DEV. = 4.1 DEGREES
REMARK 500 C J 61 N1 - C2 - O2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 G J 64 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 G J 64 N9 - C4 - C5 ANGL. DEV. = 2.4 DEGREES
REMARK 500 C J 69 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 G J 70 C3' - O3' - P ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG B 343 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 299 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG C 299 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG C 302 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 373 NE - CZ - NH1 ANGL. DEV. = 3.4 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 TYR A 94 158.03 61.87
REMARK 500 GLU A 96 -91.98 123.93
REMARK 500 LEU A 117 130.52 70.86
REMARK 500 LEU A 186 -60.16 92.99
REMARK 500 VAL A 203 -63.10 -25.88
REMARK 500 ASP A 221 99.99 -162.34
REMARK 500 ALA A 248 79.50 -157.29
REMARK 500 PRO A 259 154.89 -34.55
REMARK 500 GLU A 261 90.62 59.78
REMARK 500 LYS B 2 119.74 112.30
REMARK 500 VAL B 14 -35.54 -132.16
REMARK 500 SER B 57 46.09 -144.13
REMARK 500 GLU B 69 47.96 -93.19
REMARK 500 SER B 71 159.92 87.47
REMARK 500 GLU B 96 -67.47 -142.38
REMARK 500 LEU B 117 139.14 64.51
REMARK 500 PRO B 120 39.78 -83.55
REMARK 500 ALA B 126 -25.22 139.44
REMARK 500 LEU B 186 -59.79 92.43
REMARK 500 ALA B 248 81.57 -156.22
REMARK 500 PRO B 259 154.95 -48.67
REMARK 500 GLU B 261 93.13 46.43
REMARK 500 LEU B 400 39.26 -93.81
REMARK 500 LYS C 2 70.58 51.01
REMARK 500 TYR C 94 70.72 -111.75
REMARK 500 ALA C 95 -75.21 -69.14
REMARK 500 GLU C 96 -48.73 -136.57
REMARK 500 LEU C 117 128.13 63.84
REMARK 500 LYS C 121 -39.10 -176.62
REMARK 500 LEU C 186 -58.53 95.70
REMARK 500 ALA C 248 73.96 -150.89
REMARK 500 GLU C 261 75.37 45.47
REMARK 500 LYS D 2 123.49 97.75
REMARK 500 GLU D 68 43.01 -87.12
REMARK 500 GLU D 96 -61.83 -138.19
REMARK 500 CYS D 114 -140.53 -152.46
REMARK 500 LYS D 116 -75.84 -72.34
REMARK 500 LEU D 117 134.13 61.55
REMARK 500 LYS D 118 -78.29 -75.61
REMARK 500 LEU D 186 -59.16 93.36
REMARK 500 ALA D 248 74.79 -154.79
REMARK 500 GLU D 261 94.11 63.79
REMARK 500 LEU D 316 -65.96 -92.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 59 OE2
REMARK 620 2 ASP B 61 OD2 74.4
REMARK 620 3 ATP B1501 O3G 109.4 165.7
REMARK 620 4 ATP B1501 O2B 164.0 89.6 86.0
REMARK 620 5 ATP B1501 O1A 95.5 70.1 95.7 77.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 59 OE1
REMARK 620 2 ASP D 61 OD2 80.7
REMARK 620 3 ATP D1502 O1A 104.7 86.4
REMARK 620 4 ATP D1502 O3G 116.8 157.7 101.1
REMARK 620 5 ATP D1502 O2B 157.5 79.5 84.5 80.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 1502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SZ1 RELATED DB: PDB
REMARK 900 RELATED ID: 1TFY RELATED DB: PDB
DBREF 1TFW A 1 437 UNP O28126 CCA_ARCFU 1 437
DBREF 1TFW B 1 437 UNP O28126 CCA_ARCFU 1 437
DBREF 1TFW C 1 437 UNP O28126 CCA_ARCFU 1 437
DBREF 1TFW D 1 437 UNP O28126 CCA_ARCFU 1 437
DBREF 1TFW E 1 12 PDB 1TFW 1TFW 1 12
DBREF 1TFW H 63 75 PDB 1TFW 1TFW 63 75
DBREF 1TFW F 1 12 PDB 1TFW 1TFW 1 12
DBREF 1TFW I 63 75 PDB 1TFW 1TFW 63 75
DBREF 1TFW G 2 14 PDB 1TFW 1TFW 2 14
DBREF 1TFW J 61 73 PDB 1TFW 1TFW 61 73
SEQRES 1 E 12 G C G G A U C C G C A C
SEQRES 1 H 13 G C G G A U C C G C A C C
SEQRES 1 F 12 G C G G A C C C G C A C
SEQRES 1 I 13 G C G G A U C C G C A C C
SEQRES 1 G 13 G C G G A U C C G C A C C
SEQRES 1 J 13 C G C G G A U C C G C A C
SEQRES 1 A 437 MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU
SEQRES 2 A 437 VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU
SEQRES 3 A 437 ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY
SEQRES 4 A 437 VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR
SEQRES 5 A 437 TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU
SEQRES 6 A 437 PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG
SEQRES 7 A 437 GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU
SEQRES 8 A 437 ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL
SEQRES 9 A 437 LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU
SEQRES 10 A 437 LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR
SEQRES 11 A 437 PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY
SEQRES 12 A 437 LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS
SEQRES 13 A 437 ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY
SEQRES 14 A 437 PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR
SEQRES 15 A 437 GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP
SEQRES 16 A 437 THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL
SEQRES 17 A 437 ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP
SEQRES 18 A 437 GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN
SEQRES 19 A 437 LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU
SEQRES 20 A 437 ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU
SEQRES 21 A 437 GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU
SEQRES 22 A 437 ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO
SEQRES 23 A 437 ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG
SEQRES 24 A 437 ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN
SEQRES 25 A 437 PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU
SEQRES 26 A 437 PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE
SEQRES 27 A 437 SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP
SEQRES 28 A 437 GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA
SEQRES 29 A 437 PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE
SEQRES 30 A 437 GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG
SEQRES 31 A 437 SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN
SEQRES 32 A 437 VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER
SEQRES 33 A 437 GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU
SEQRES 34 A 437 CYS GLU MET MET GLY VAL LYS ASP
SEQRES 1 B 437 MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU
SEQRES 2 B 437 VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU
SEQRES 3 B 437 ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY
SEQRES 4 B 437 VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR
SEQRES 5 B 437 TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU
SEQRES 6 B 437 PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG
SEQRES 7 B 437 GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU
SEQRES 8 B 437 ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL
SEQRES 9 B 437 LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU
SEQRES 10 B 437 LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR
SEQRES 11 B 437 PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY
SEQRES 12 B 437 LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS
SEQRES 13 B 437 ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY
SEQRES 14 B 437 PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR
SEQRES 15 B 437 GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP
SEQRES 16 B 437 THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL
SEQRES 17 B 437 ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP
SEQRES 18 B 437 GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN
SEQRES 19 B 437 LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU
SEQRES 20 B 437 ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU
SEQRES 21 B 437 GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU
SEQRES 22 B 437 ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO
SEQRES 23 B 437 ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG
SEQRES 24 B 437 ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN
SEQRES 25 B 437 PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU
SEQRES 26 B 437 PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE
SEQRES 27 B 437 SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP
SEQRES 28 B 437 GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA
SEQRES 29 B 437 PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE
SEQRES 30 B 437 GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG
SEQRES 31 B 437 SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN
SEQRES 32 B 437 VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER
SEQRES 33 B 437 GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU
SEQRES 34 B 437 CYS GLU MET MET GLY VAL LYS ASP
SEQRES 1 C 437 MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU
SEQRES 2 C 437 VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU
SEQRES 3 C 437 ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY
SEQRES 4 C 437 VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR
SEQRES 5 C 437 TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU
SEQRES 6 C 437 PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG
SEQRES 7 C 437 GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU
SEQRES 8 C 437 ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL
SEQRES 9 C 437 LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU
SEQRES 10 C 437 LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR
SEQRES 11 C 437 PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY
SEQRES 12 C 437 LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS
SEQRES 13 C 437 ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY
SEQRES 14 C 437 PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR
SEQRES 15 C 437 GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP
SEQRES 16 C 437 THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL
SEQRES 17 C 437 ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP
SEQRES 18 C 437 GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN
SEQRES 19 C 437 LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU
SEQRES 20 C 437 ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU
SEQRES 21 C 437 GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU
SEQRES 22 C 437 ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO
SEQRES 23 C 437 ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG
SEQRES 24 C 437 ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN
SEQRES 25 C 437 PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU
SEQRES 26 C 437 PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE
SEQRES 27 C 437 SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP
SEQRES 28 C 437 GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA
SEQRES 29 C 437 PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE
SEQRES 30 C 437 GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG
SEQRES 31 C 437 SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN
SEQRES 32 C 437 VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER
SEQRES 33 C 437 GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU
SEQRES 34 C 437 CYS GLU MET MET GLY VAL LYS ASP
SEQRES 1 D 437 MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU
SEQRES 2 D 437 VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU
SEQRES 3 D 437 ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY
SEQRES 4 D 437 VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR
SEQRES 5 D 437 TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU
SEQRES 6 D 437 PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG
SEQRES 7 D 437 GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU
SEQRES 8 D 437 ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL
SEQRES 9 D 437 LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU
SEQRES 10 D 437 LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR
SEQRES 11 D 437 PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY
SEQRES 12 D 437 LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS
SEQRES 13 D 437 ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY
SEQRES 14 D 437 PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR
SEQRES 15 D 437 GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP
SEQRES 16 D 437 THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL
SEQRES 17 D 437 ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP
SEQRES 18 D 437 GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN
SEQRES 19 D 437 LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU
SEQRES 20 D 437 ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU
SEQRES 21 D 437 GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU
SEQRES 22 D 437 ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO
SEQRES 23 D 437 ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG
SEQRES 24 D 437 ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN
SEQRES 25 D 437 PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU
SEQRES 26 D 437 PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE
SEQRES 27 D 437 SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP
SEQRES 28 D 437 GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA
SEQRES 29 D 437 PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE
SEQRES 30 D 437 GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG
SEQRES 31 D 437 SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN
SEQRES 32 D 437 VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER
SEQRES 33 D 437 GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU
SEQRES 34 D 437 CYS GLU MET MET GLY VAL LYS ASP
HET MG B1601 1
HET ATP B1501 31
HET MG D1602 1
HET ATP D1502 31
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 11 MG 2(MG 2+)
FORMUL 12 ATP 2(C10 H16 N5 O13 P3)
FORMUL 15 HOH *1059(H2 O)
HELIX 1 1 LYS A 2 LEU A 13 1 12
HELIX 2 2 ASP A 17 LEU A 38 1 22
HELIX 3 3 GLY A 46 ARG A 50 1 5
HELIX 4 4 SER A 71 LEU A 87 1 17
HELIX 5 5 GLU A 119 ILE A 123 5 5
HELIX 6 6 ARG A 129 GLU A 138 1 10
HELIX 7 7 LYS A 144 ASN A 158 1 15
HELIX 8 8 SER A 171 GLY A 183 1 13
HELIX 9 9 LEU A 186 ARG A 193 1 8
HELIX 10 10 SER A 231 ALA A 248 1 18
HELIX 11 11 SER A 250 LYS A 255 5 6
HELIX 12 12 GLU A 263 GLY A 275 1 13
HELIX 13 13 VAL A 289 GLU A 311 1 23
HELIX 14 14 ASP A 351 ARG A 361 1 11
HELIX 15 15 THR A 384 HIS A 396 1 13
HELIX 16 16 TRP A 397 LEU A 400 5 4
HELIX 17 17 GLY A 401 TYR A 411 1 11
HELIX 18 18 GLY A 417 LYS A 422 1 6
HELIX 19 19 VAL A 425 GLY A 434 1 10
HELIX 20 20 LYS B 2 LEU B 13 1 12
HELIX 21 21 ASP B 17 GLY B 39 1 23
HELIX 22 22 GLY B 46 ARG B 50 1 5
HELIX 23 23 SER B 71 LEU B 87 1 17
HELIX 24 24 ARG B 129 GLU B 138 1 10
HELIX 25 25 LYS B 144 ASN B 158 1 15
HELIX 26 26 SER B 171 GLY B 183 1 13
HELIX 27 27 LEU B 186 ARG B 193 1 8
HELIX 28 28 SER B 231 ALA B 248 1 18
HELIX 29 29 SER B 250 LYS B 255 5 6
HELIX 30 30 GLU B 263 GLY B 275 1 13
HELIX 31 31 VAL B 289 GLU B 311 1 23
HELIX 32 32 ASP B 351 ARG B 361 1 11
HELIX 33 33 THR B 384 HIS B 396 1 13
HELIX 34 34 TRP B 397 LEU B 400 5 4
HELIX 35 35 GLY B 401 TYR B 411 1 11
HELIX 36 36 GLY B 417 PHE B 421 1 5
HELIX 37 37 VAL B 425 GLY B 434 1 10
HELIX 38 38 LYS C 2 LEU C 13 1 12
HELIX 39 39 ASP C 17 LEU C 38 1 22
HELIX 40 40 GLY C 46 ARG C 50 1 5
HELIX 41 41 SER C 71 LEU C 87 1 17
HELIX 42 42 SER C 125 GLU C 138 1 14
HELIX 43 43 LYS C 144 ASN C 158 1 15
HELIX 44 44 SER C 171 GLY C 183 1 13
HELIX 45 45 LEU C 186 ARG C 193 1 8
HELIX 46 46 SER C 231 ALA C 248 1 18
HELIX 47 47 SER C 250 LYS C 255 5 6
HELIX 48 48 GLU C 263 GLY C 275 1 13
HELIX 49 49 VAL C 289 GLU C 311 1 23
HELIX 50 50 ASP C 351 ARG C 361 1 11
HELIX 51 51 THR C 384 HIS C 396 1 13
HELIX 52 52 TRP C 397 LEU C 400 5 4
HELIX 53 53 GLY C 401 TYR C 411 1 11
HELIX 54 54 GLY C 417 LYS C 422 1 6
HELIX 55 55 VAL C 425 GLY C 434 1 10
HELIX 56 56 LYS D 2 LEU D 11 1 10
HELIX 57 57 ASP D 17 GLY D 39 1 23
HELIX 58 58 GLY D 46 ARG D 50 1 5
HELIX 59 59 SER D 71 VAL D 86 1 16
HELIX 60 60 ARG D 129 GLU D 138 1 10
HELIX 61 61 LYS D 144 ASN D 158 1 15
HELIX 62 62 SER D 171 GLY D 183 1 13
HELIX 63 63 LEU D 186 ARG D 193 1 8
HELIX 64 64 SER D 231 ALA D 248 1 18
HELIX 65 65 SER D 250 LYS D 255 5 6
HELIX 66 66 GLU D 263 GLY D 275 1 13
HELIX 67 67 VAL D 289 GLU D 311 1 23
HELIX 68 68 ASP D 351 ARG D 361 1 11
HELIX 69 69 THR D 384 HIS D 396 1 13
HELIX 70 70 TRP D 397 LEU D 400 5 4
HELIX 71 71 GLY D 401 TYR D 411 1 11
HELIX 72 72 GLU D 418 GLU D 423 5 6
HELIX 73 73 VAL D 425 GLY D 434 1 10
SHEET 1 A 5 TYR A 42 VAL A 45 0
SHEET 2 A 5 GLU A 59 PHE A 66 -1 O PHE A 63 N VAL A 43
SHEET 3 A 5 VAL A 107 TYR A 115 1 O VAL A 112 N LEU A 64
SHEET 4 A 5 TYR A 99 VAL A 104 -1 N GLY A 102 O VAL A 109
SHEET 5 A 5 SER A 89 ARG A 93 -1 N GLU A 91 O HIS A 101
SHEET 1 B 4 GLU A 207 LYS A 210 0
SHEET 2 B 4 THR A 199 ASP A 202 -1 N ASP A 202 O GLU A 207
SHEET 3 B 4 PHE A 215 ASP A 218 1 O PHE A 215 N ILE A 201
SHEET 4 B 4 ASP A 221 ASN A 225 -1 O ARG A 224 N ASP A 218
SHEET 1 C 4 PRO A 315 ALA A 322 0
SHEET 2 C 4 PHE A 326 CYS A 333 -1 O GLU A 332 N LEU A 316
SHEET 3 C 4 ALA A 277 ARG A 284 -1 N PHE A 283 O CYS A 327
SHEET 4 C 4 GLU A 413 SER A 416 -1 O GLU A 413 N LYS A 282
SHEET 1 D 3 VAL A 341 GLN A 348 0
SHEET 2 D 3 ARG A 373 MET A 379 -1 O ALA A 376 N ARG A 344
SHEET 3 D 3 PHE A 368 GLU A 370 -1 N GLU A 370 O ARG A 373
SHEET 1 E 5 TYR B 42 VAL B 45 0
SHEET 2 E 5 GLU B 59 PHE B 66 -1 O PHE B 63 N VAL B 43
SHEET 3 E 5 VAL B 107 TYR B 115 1 O VAL B 112 N VAL B 62
SHEET 4 E 5 VAL B 100 VAL B 104 -1 N VAL B 100 O VAL B 111
SHEET 5 E 5 SER B 89 GLU B 91 -1 N GLU B 91 O HIS B 101
SHEET 1 F 4 GLU B 207 LYS B 210 0
SHEET 2 F 4 THR B 199 ASP B 202 -1 N VAL B 200 O ARG B 209
SHEET 3 F 4 PHE B 215 ASP B 218 1 O PHE B 215 N ILE B 201
SHEET 4 F 4 ASP B 221 ASN B 225 -1 O ARG B 224 N ASP B 218
SHEET 1 G 4 PRO B 315 ALA B 322 0
SHEET 2 G 4 PHE B 326 CYS B 333 -1 O GLU B 332 N LEU B 316
SHEET 3 G 4 ALA B 277 ARG B 284 -1 N PHE B 283 O CYS B 327
SHEET 4 G 4 GLU B 413 SER B 416 -1 O GLU B 413 N LYS B 282
SHEET 1 H 3 VAL B 341 GLN B 348 0
SHEET 2 H 3 ARG B 373 MET B 379 -1 O ALA B 376 N ARG B 344
SHEET 3 H 3 PHE B 368 GLU B 370 -1 N GLU B 370 O ARG B 373
SHEET 1 I 5 TYR C 42 VAL C 45 0
SHEET 2 I 5 GLU C 59 PHE C 66 -1 O PHE C 63 N VAL C 43
SHEET 3 I 5 VAL C 107 TYR C 115 1 O VAL C 112 N VAL C 62
SHEET 4 I 5 TYR C 99 VAL C 104 -1 N VAL C 100 O VAL C 111
SHEET 5 I 5 SER C 89 ARG C 93 -1 N GLU C 91 O HIS C 101
SHEET 1 J 4 GLU C 207 LYS C 210 0
SHEET 2 J 4 THR C 199 ASP C 202 -1 N VAL C 200 O ARG C 209
SHEET 3 J 4 PHE C 215 ASP C 218 1 O PHE C 215 N ILE C 201
SHEET 4 J 4 ASP C 221 ASN C 225 -1 O ARG C 224 N ASP C 218
SHEET 1 K 4 PRO C 315 ALA C 322 0
SHEET 2 K 4 PHE C 326 CYS C 333 -1 O GLU C 332 N LEU C 316
SHEET 3 K 4 ALA C 277 ARG C 284 -1 N PHE C 283 O CYS C 327
SHEET 4 K 4 GLU C 413 SER C 416 -1 O GLU C 413 N LYS C 282
SHEET 1 L 3 VAL C 341 GLN C 348 0
SHEET 2 L 3 ARG C 373 MET C 379 -1 O ALA C 376 N ARG C 344
SHEET 3 L 3 PHE C 368 GLU C 370 -1 N PHE C 368 O TRP C 375
SHEET 1 M 5 TYR D 42 VAL D 45 0
SHEET 2 M 5 GLU D 59 LEU D 64 -1 O PHE D 63 N VAL D 43
SHEET 3 M 5 VAL D 107 PRO D 113 1 O VAL D 112 N VAL D 62
SHEET 4 M 5 VAL D 100 VAL D 104 -1 N GLY D 102 O VAL D 109
SHEET 5 M 5 TYR D 90 GLU D 91 -1 N GLU D 91 O HIS D 101
SHEET 1 N 4 GLU D 207 LYS D 210 0
SHEET 2 N 4 THR D 199 ASP D 202 -1 N VAL D 200 O ARG D 209
SHEET 3 N 4 PHE D 215 ASP D 218 1 O PHE D 215 N ILE D 201
SHEET 4 N 4 ASP D 221 ASN D 225 -1 O ARG D 224 N ASP D 218
SHEET 1 O 4 PRO D 315 ALA D 322 0
SHEET 2 O 4 PHE D 326 CYS D 333 -1 O LEU D 330 N ALA D 319
SHEET 3 O 4 ALA D 277 ARG D 284 -1 N PHE D 283 O CYS D 327
SHEET 4 O 4 GLU D 413 SER D 416 -1 O GLU D 413 N LYS D 282
SHEET 1 P 3 VAL D 341 GLN D 348 0
SHEET 2 P 3 ARG D 373 MET D 379 -1 O ALA D 376 N ARG D 344
SHEET 3 P 3 PHE D 368 GLU D 370 -1 N GLU D 370 O ARG D 373
LINK OE2 GLU B 59 MG MG B1601 1555 1555 2.22
LINK OD2 ASP B 61 MG MG B1601 1555 1555 2.60
LINK O3G ATP B1501 MG MG B1601 1555 1555 1.89
LINK O2B ATP B1501 MG MG B1601 1555 1555 2.11
LINK O1A ATP B1501 MG MG B1601 1555 1555 2.31
LINK OE1 GLU D 59 MG MG D1602 1555 1555 2.48
LINK OD2 ASP D 61 MG MG D1602 1555 1555 2.52
LINK O1A ATP D1502 MG MG D1602 1555 1555 1.98
LINK O3G ATP D1502 MG MG D1602 1555 1555 2.11
LINK O2B ATP D1502 MG MG D1602 1555 1555 2.18
SITE 1 AC1 4 SER B 47 GLU B 59 ASP B 61 ATP B1501
SITE 1 AC2 3 GLU D 59 ASP D 61 ATP D1502
SITE 1 AC3 16 GLY B 46 SER B 47 ARG B 50 GLU B 59
SITE 2 AC3 16 ASP B 61 THR B 130 HIS B 133 LYS B 152
SITE 3 AC3 16 TYR B 161 ARG B 224 MG B1601 HOH B1647
SITE 4 AC3 16 HOH B1685 A H 73 C H 74 C H 75
SITE 1 AC4 17 GLY D 46 SER D 47 ARG D 50 GLU D 59
SITE 2 AC4 17 ASP D 61 THR D 130 HIS D 133 LYS D 152
SITE 3 AC4 17 TYR D 161 ARG D 224 MG D1602 HOH D1675
SITE 4 AC4 17 HOH D1753 HOH D1767 A I 73 C I 74
SITE 5 AC4 17 C I 75
CRYST1 116.641 84.770 135.813 90.00 104.66 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008573 0.000000 0.002243 0.00000
SCALE2 0.000000 0.011797 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007611 0.00000
(ATOM LINES ARE NOT SHOWN.)
END