HEADER TRANSPORT PROTEIN 12-JUN-09 3HU2
TITLE STRUCTURE OF P97 N-D1 R86A MUTANT IN COMPLEX WITH ATPGS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: RESIDUES 1-481;
COMPND 5 SYNONYM: TER ATPASE, 15S MG(2+)-ATPASE P97 SUBUNIT, VALOSIN-
COMPND 6 CONTAINING PROTEIN, VCP;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: HUMAN;
SOURCE 6 GENE: P97, VCP;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS P97, VCP, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.-K.TANG
REVDAT 6 21-FEB-24 3HU2 1 REMARK LINK
REVDAT 5 26-FEB-20 3HU2 1 REMARK SEQADV
REVDAT 4 15-FEB-12 3HU2 1 HET HETATM HETNAM
REVDAT 3 13-JUL-11 3HU2 1 VERSN
REVDAT 2 18-AUG-10 3HU2 1 JRNL
REVDAT 1 16-JUN-10 3HU2 0
JRNL AUTH W.K.TANG,D.LI,C.C.LI,L.ESSER,R.DAI,L.GUO,D.XIA
JRNL TITL A NOVEL ATP-DEPENDENT CONFORMATION IN P97 N-D1 FRAGMENT
JRNL TITL 2 REVEALED BY CRYSTAL STRUCTURES OF DISEASE-RELATED MUTANTS.
JRNL REF EMBO J. V. 29 2217 2010
JRNL REFN ISSN 0261-4189
JRNL PMID 20512113
JRNL DOI 10.1038/EMBOJ.2010.104
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 79168
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) : 0.259
REMARK 3 R VALUE (WORKING SET) : 0.258
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4194
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) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4484
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.3470
REMARK 3 BIN FREE R VALUE SET COUNT : 267
REMARK 3 BIN FREE R VALUE : 0.3920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 21168
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 93
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) : 70.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.47000
REMARK 3 B22 (A**2) : -0.62000
REMARK 3 B33 (A**2) : -3.49000
REMARK 3 B12 (A**2) : -0.14000
REMARK 3 B13 (A**2) : 0.90000
REMARK 3 B23 (A**2) : -2.48000
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): 0.449
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.385
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.334
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 21690 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 29358 ; 1.520 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2706 ; 6.074 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 990 ;40.298 ;24.303
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3972 ;19.527 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 192 ;16.891 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3360 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16182 ; 0.015 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9474 ; 0.161 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 14525 ; 0.264 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 599 ; 0.107 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 12 ; 0.211 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 79 ; 0.222 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.325 ; 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): 14042 ; 0.433 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21906 ; 0.650 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8567 ; 1.124 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7452 ; 1.646 ; 4.500
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 : 5
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 12 A 166 1
REMARK 3 1 B 12 B 166 1
REMARK 3 1 C 12 C 166 1
REMARK 3 1 D 12 D 166 1
REMARK 3 1 E 12 E 166 1
REMARK 3 1 F 12 F 166 1
REMARK 3 2 A 168 A 189 1
REMARK 3 2 B 168 B 189 1
REMARK 3 2 C 168 C 189 1
REMARK 3 2 D 168 D 189 1
REMARK 3 2 E 168 E 189 1
REMARK 3 2 F 168 F 189 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1399 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1399 ; 0.10 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1399 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1399 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 1399 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 F (A): 1399 ; 0.07 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 1399 ; 0.15 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1399 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1399 ; 0.14 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1399 ; 0.12 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 1399 ; 0.13 ; 0.50
REMARK 3 TIGHT THERMAL 1 F (A**2): 1399 ; 0.13 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 190 A 201 1
REMARK 3 1 B 190 B 201 1
REMARK 3 1 C 190 C 201 1
REMARK 3 1 D 190 D 201 1
REMARK 3 1 E 190 E 201 1
REMARK 3 1 F 190 F 201 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 102 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 B (A): 102 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 C (A): 102 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 102 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 E (A): 102 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 F (A): 102 ; 0.05 ; 0.05
REMARK 3 TIGHT THERMAL 2 A (A**2): 102 ; 0.11 ; 0.50
REMARK 3 TIGHT THERMAL 2 B (A**2): 102 ; 0.15 ; 0.50
REMARK 3 TIGHT THERMAL 2 C (A**2): 102 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 102 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 2 E (A**2): 102 ; 0.11 ; 0.50
REMARK 3 TIGHT THERMAL 2 F (A**2): 102 ; 0.10 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 202 A 371 1
REMARK 3 1 B 202 B 371 1
REMARK 3 1 C 202 C 371 1
REMARK 3 1 D 202 D 371 1
REMARK 3 1 E 202 E 371 1
REMARK 3 1 F 202 F 371 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 1318 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 B (A): 1318 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 C (A): 1318 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 D (A): 1318 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 E (A): 1318 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 F (A): 1318 ; 0.08 ; 0.05
REMARK 3 TIGHT THERMAL 3 A (A**2): 1318 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 3 B (A**2): 1318 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 3 C (A**2): 1318 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 3 D (A**2): 1318 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 3 E (A**2): 1318 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 3 F (A**2): 1318 ; 0.21 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 372 A 403 1
REMARK 3 1 B 372 B 403 1
REMARK 3 1 C 372 C 403 1
REMARK 3 1 D 372 D 403 1
REMARK 3 1 E 372 E 403 1
REMARK 3 1 F 372 F 403 1
REMARK 3 2 A 405 A 462 1
REMARK 3 2 B 405 B 462 1
REMARK 3 2 C 405 C 462 1
REMARK 3 2 D 405 D 462 1
REMARK 3 2 E 405 E 462 1
REMARK 3 2 F 405 F 462 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 685 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 B (A): 685 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 C (A): 685 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 D (A): 685 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 E (A): 685 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 F (A): 685 ; 0.09 ; 0.05
REMARK 3 TIGHT THERMAL 4 A (A**2): 685 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 4 B (A**2): 685 ; 0.17 ; 0.50
REMARK 3 TIGHT THERMAL 4 C (A**2): 685 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 4 D (A**2): 685 ; 0.15 ; 0.50
REMARK 3 TIGHT THERMAL 4 E (A**2): 685 ; 0.17 ; 0.50
REMARK 3 TIGHT THERMAL 4 F (A**2): 685 ; 0.19 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 800 A 801 1
REMARK 3 1 B 800 B 801 1
REMARK 3 1 C 800 C 801 1
REMARK 3 1 D 800 D 801 1
REMARK 3 1 E 800 E 801 1
REMARK 3 1 F 800 F 801 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 32 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 5 B (A): 32 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 5 C (A): 32 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 5 D (A): 32 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 5 E (A): 32 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 5 F (A): 32 ; 0.06 ; 0.05
REMARK 3 TIGHT THERMAL 5 A (A**2): 32 ; 0.24 ; 0.50
REMARK 3 TIGHT THERMAL 5 B (A**2): 32 ; 0.23 ; 0.50
REMARK 3 TIGHT THERMAL 5 C (A**2): 32 ; 0.28 ; 0.50
REMARK 3 TIGHT THERMAL 5 D (A**2): 32 ; 0.33 ; 0.50
REMARK 3 TIGHT THERMAL 5 E (A**2): 32 ; 0.36 ; 0.50
REMARK 3 TIGHT THERMAL 5 F (A**2): 32 ; 0.25 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
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 16 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2462 81.3463 0.9905
REMARK 3 T TENSOR
REMARK 3 T11: 0.1386 T22: -0.0627
REMARK 3 T33: 0.2883 T12: 0.1254
REMARK 3 T13: 0.2560 T23: 0.0560
REMARK 3 L TENSOR
REMARK 3 L11: 2.3962 L22: 6.5255
REMARK 3 L33: 7.8241 L12: -0.9637
REMARK 3 L13: 0.7299 L23: -1.0591
REMARK 3 S TENSOR
REMARK 3 S11: 0.3508 S12: -0.4319 S13: 0.7511
REMARK 3 S21: 0.7907 S22: -0.0471 S23: -0.0048
REMARK 3 S31: -0.8546 S32: -0.6454 S33: -0.3037
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 108 A 189
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8956 82.9860 -19.3136
REMARK 3 T TENSOR
REMARK 3 T11: -0.1926 T22: -0.1007
REMARK 3 T33: 0.1232 T12: 0.0796
REMARK 3 T13: 0.1591 T23: 0.2459
REMARK 3 L TENSOR
REMARK 3 L11: 7.8999 L22: 10.5661
REMARK 3 L33: 11.4952 L12: -1.0197
REMARK 3 L13: -0.5504 L23: 1.4474
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: 0.5178 S13: 0.2675
REMARK 3 S21: -0.2249 S22: 0.0870 S23: 0.2586
REMARK 3 S31: -0.6951 S32: 0.4597 S33: -0.0817
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 190 A 201
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5473 64.7642 -15.9650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0821 T22: 0.1128
REMARK 3 T33: 0.6206 T12: -0.2028
REMARK 3 T13: 0.0133 T23: 0.2126
REMARK 3 L TENSOR
REMARK 3 L11: 3.1607 L22: 18.5763
REMARK 3 L33: 50.2094 L12: -7.6625
REMARK 3 L13: 12.5975 L23: -30.5402
REMARK 3 S TENSOR
REMARK 3 S11: -0.3443 S12: -0.9054 S13: -0.8342
REMARK 3 S21: -0.2234 S22: 0.4316 S23: -0.4215
REMARK 3 S31: 1.1316 S32: -2.5810 S33: -0.0874
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 : A 202 A 371
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4121 50.9448 3.0607
REMARK 3 T TENSOR
REMARK 3 T11: -0.2525 T22: -0.2561
REMARK 3 T33: -0.2144 T12: 0.0459
REMARK 3 T13: -0.0255 T23: 0.0784
REMARK 3 L TENSOR
REMARK 3 L11: 3.8250 L22: 4.2090
REMARK 3 L33: 4.1275 L12: 0.5651
REMARK 3 L13: -0.4058 L23: 1.5345
REMARK 3 S TENSOR
REMARK 3 S11: 0.1280 S12: 0.0311 S13: 0.0745
REMARK 3 S21: 0.2720 S22: 0.0001 S23: -0.2984
REMARK 3 S31: -0.0253 S32: 0.3047 S33: -0.1281
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 372 A 460
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8136 50.6650 -13.1368
REMARK 3 T TENSOR
REMARK 3 T11: -0.4468 T22: 0.0667
REMARK 3 T33: 0.1655 T12: 0.0524
REMARK 3 T13: -0.0072 T23: 0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 4.2106 L22: 4.4235
REMARK 3 L33: 12.1778 L12: -0.3820
REMARK 3 L13: 1.1530 L23: 0.1610
REMARK 3 S TENSOR
REMARK 3 S11: -0.1091 S12: -0.0401 S13: 0.3602
REMARK 3 S21: -0.3971 S22: 0.1470 S23: 0.3931
REMARK 3 S31: -0.3519 S32: -1.1040 S33: -0.0380
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 16 B 107
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1570 49.8070 -52.4140
REMARK 3 T TENSOR
REMARK 3 T11: -0.3559 T22: 0.4190
REMARK 3 T33: 0.0819 T12: 0.1098
REMARK 3 T13: -0.1138 T23: 0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 4.5219 L22: 6.7922
REMARK 3 L33: 10.5640 L12: -0.6216
REMARK 3 L13: -3.1040 L23: -1.0679
REMARK 3 S TENSOR
REMARK 3 S11: -0.0064 S12: 0.7702 S13: 0.0004
REMARK 3 S21: 0.4840 S22: 0.1359 S23: 1.0047
REMARK 3 S31: -0.5305 S32: -1.6929 S33: -0.1296
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 : B 108 B 189
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5440 49.6926 -63.1953
REMARK 3 T TENSOR
REMARK 3 T11: -0.3752 T22: -0.0431
REMARK 3 T33: -0.2474 T12: -0.0880
REMARK 3 T13: -0.0366 T23: 0.1044
REMARK 3 L TENSOR
REMARK 3 L11: 8.4848 L22: 9.4855
REMARK 3 L33: 11.0699 L12: -1.3827
REMARK 3 L13: -0.8165 L23: 1.8160
REMARK 3 S TENSOR
REMARK 3 S11: 0.0229 S12: 0.2015 S13: -0.0200
REMARK 3 S21: -0.6242 S22: 0.1414 S23: -0.4713
REMARK 3 S31: 0.2256 S32: -0.0112 S33: -0.1643
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 190 B 201
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9989 35.2223 -50.4037
REMARK 3 T TENSOR
REMARK 3 T11: 0.3026 T22: 0.2084
REMARK 3 T33: 0.0730 T12: -0.1940
REMARK 3 T13: 0.0342 T23: 0.1888
REMARK 3 L TENSOR
REMARK 3 L11: 20.9823 L22: 0.8763
REMARK 3 L33: 37.7678 L12: 4.2881
REMARK 3 L13: -28.1506 L23: -5.7530
REMARK 3 S TENSOR
REMARK 3 S11: -0.3677 S12: -0.3021 S13: -1.9398
REMARK 3 S21: -0.3536 S22: 0.0656 S23: -0.0443
REMARK 3 S31: 0.6383 S32: 0.6193 S33: 0.3021
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 : B 202 B 371
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6754 40.8699 -23.6824
REMARK 3 T TENSOR
REMARK 3 T11: -0.2393 T22: -0.2623
REMARK 3 T33: -0.2803 T12: 0.0414
REMARK 3 T13: 0.0273 T23: 0.0946
REMARK 3 L TENSOR
REMARK 3 L11: 4.4245 L22: 5.1371
REMARK 3 L33: 3.4581 L12: 0.1062
REMARK 3 L13: 0.1676 L23: 0.6623
REMARK 3 S TENSOR
REMARK 3 S11: -0.0835 S12: -0.1078 S13: 0.1727
REMARK 3 S21: 0.3575 S22: 0.1622 S23: -0.0243
REMARK 3 S31: -0.1631 S32: -0.0609 S33: -0.0786
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 : B 372 B 460
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5986 15.3582 -45.2910
REMARK 3 T TENSOR
REMARK 3 T11: -0.2718 T22: 0.0993
REMARK 3 T33: 0.2306 T12: -0.1676
REMARK 3 T13: -0.1141 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 5.1732 L22: 6.3889
REMARK 3 L33: 8.3245 L12: -2.4122
REMARK 3 L13: -3.3200 L23: 3.9031
REMARK 3 S TENSOR
REMARK 3 S11: -0.2796 S12: 0.9038 S13: -0.6085
REMARK 3 S21: -0.2699 S22: -0.4058 S23: 0.7258
REMARK 3 S31: 0.4998 S32: -0.6057 S33: 0.6854
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 16 C 107
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6992 -0.8073 -68.3240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1528 T22: -0.1212
REMARK 3 T33: 0.0068 T12: -0.0467
REMARK 3 T13: 0.0010 T23: -0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 9.3139 L22: 3.9640
REMARK 3 L33: 6.8530 L12: -0.6170
REMARK 3 L13: -0.5416 L23: 1.6009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0525 S12: 0.6232 S13: -0.4534
REMARK 3 S21: -0.3180 S22: 0.1623 S23: 0.3681
REMARK 3 S31: -0.3478 S32: -0.6218 S33: -0.1098
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 : C 108 C 189
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6769 6.9431 -66.6921
REMARK 3 T TENSOR
REMARK 3 T11: 0.3651 T22: -0.0472
REMARK 3 T33: 0.1714 T12: -0.2870
REMARK 3 T13: 0.1829 T23: -0.1565
REMARK 3 L TENSOR
REMARK 3 L11: 8.7146 L22: 6.2466
REMARK 3 L33: 7.4293 L12: -1.0268
REMARK 3 L13: 1.3409 L23: -2.4791
REMARK 3 S TENSOR
REMARK 3 S11: -0.0348 S12: 0.5912 S13: 0.0507
REMARK 3 S21: -0.3108 S22: -0.0206 S23: -0.7372
REMARK 3 S31: -0.2822 S32: 1.1290 S33: 0.0554
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 190 C 201
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7727 1.0122 -49.3516
REMARK 3 T TENSOR
REMARK 3 T11: 0.5911 T22: 0.6210
REMARK 3 T33: 0.5512 T12: 0.0256
REMARK 3 T13: -0.1467 T23: -0.1578
REMARK 3 L TENSOR
REMARK 3 L11: 61.5612 L22: 1.9631
REMARK 3 L33: 7.0934 L12: -10.9931
REMARK 3 L13: -20.8969 L23: 3.7316
REMARK 3 S TENSOR
REMARK 3 S11: 0.4763 S12: -1.8199 S13: -1.3759
REMARK 3 S21: -0.3130 S22: 0.6166 S23: -0.6459
REMARK 3 S31: -0.6074 S32: -0.7035 S33: -1.0929
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 202 C 371
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8795 16.4375 -37.3151
REMARK 3 T TENSOR
REMARK 3 T11: -0.2709 T22: -0.2801
REMARK 3 T33: -0.2149 T12: 0.0647
REMARK 3 T13: 0.0020 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 3.3027 L22: 5.5814
REMARK 3 L33: 4.1117 L12: -0.1315
REMARK 3 L13: 0.4435 L23: -0.4441
REMARK 3 S TENSOR
REMARK 3 S11: -0.1393 S12: 0.0414 S13: 0.1933
REMARK 3 S21: -0.0293 S22: 0.0809 S23: 0.0395
REMARK 3 S31: -0.2633 S32: -0.2512 S33: 0.0584
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 372 C 460
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3028 -16.4433 -36.2690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0424 T22: -0.1833
REMARK 3 T33: 0.0033 T12: -0.0575
REMARK 3 T13: 0.0579 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 7.4313 L22: 5.8740
REMARK 3 L33: 4.5344 L12: -3.2586
REMARK 3 L13: 1.4017 L23: 1.2350
REMARK 3 S TENSOR
REMARK 3 S11: -0.2111 S12: 0.2681 S13: -0.7999
REMARK 3 S21: 0.1712 S22: 0.2660 S23: 0.0382
REMARK 3 S31: 0.5611 S32: 0.5122 S33: -0.0549
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 16 D 107
REMARK 3 ORIGIN FOR THE GROUP (A): 60.5329 -21.2114 -29.0058
REMARK 3 T TENSOR
REMARK 3 T11: -0.0472 T22: 0.0698
REMARK 3 T33: 0.3449 T12: 0.1725
REMARK 3 T13: -0.0044 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 8.6745 L22: 7.8046
REMARK 3 L33: 8.3774 L12: 1.0723
REMARK 3 L13: -0.1031 L23: 3.3023
REMARK 3 S TENSOR
REMARK 3 S11: 0.1977 S12: 0.8492 S13: -1.2580
REMARK 3 S21: -0.2034 S22: -0.3266 S23: -0.3489
REMARK 3 S31: 0.5962 S32: -0.3588 S33: 0.1289
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 108 D 189
REMARK 3 ORIGIN FOR THE GROUP (A): 73.7991 -3.3564 -26.1325
REMARK 3 T TENSOR
REMARK 3 T11: 0.4425 T22: 0.1374
REMARK 3 T33: 0.6657 T12: -0.0504
REMARK 3 T13: 0.2125 T23: 0.3124
REMARK 3 L TENSOR
REMARK 3 L11: 8.3120 L22: 6.9497
REMARK 3 L33: 13.1671 L12: -1.5181
REMARK 3 L13: 1.6526 L23: 3.2307
REMARK 3 S TENSOR
REMARK 3 S11: 0.0419 S12: 0.4080 S13: 0.6644
REMARK 3 S21: -0.4317 S22: 0.1861 S23: -1.5156
REMARK 3 S31: -1.9331 S32: 1.0001 S33: -0.2279
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 190 D 201
REMARK 3 ORIGIN FOR THE GROUP (A): 58.6830 -2.2834 -14.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.3783 T22: 0.6682
REMARK 3 T33: 0.4217 T12: -0.1974
REMARK 3 T13: -0.0343 T23: 0.2342
REMARK 3 L TENSOR
REMARK 3 L11: 24.2879 L22: 0.0640
REMARK 3 L33: 0.0002 L12: 1.2463
REMARK 3 L13: 0.0637 L23: 0.0033
REMARK 3 S TENSOR
REMARK 3 S11: 1.9328 S12: -0.9598 S13: 0.4120
REMARK 3 S21: 1.0375 S22: -1.2714 S23: -0.5258
REMARK 3 S31: -0.6531 S32: -0.1909 S33: -0.6614
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 202 D 371
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4175 1.8838 -23.9337
REMARK 3 T TENSOR
REMARK 3 T11: -0.2585 T22: -0.1561
REMARK 3 T33: -0.1427 T12: 0.1011
REMARK 3 T13: -0.0520 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 2.5469 L22: 3.4162
REMARK 3 L33: 5.0598 L12: 0.3415
REMARK 3 L13: -0.1544 L23: -0.0007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0206 S12: 0.4448 S13: -0.0761
REMARK 3 S21: -0.0600 S22: -0.0733 S23: 0.0650
REMARK 3 S31: -0.0371 S32: -0.0213 S33: 0.0528
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 372 D 460
REMARK 3 ORIGIN FOR THE GROUP (A): 49.2276 -12.2271 4.0568
REMARK 3 T TENSOR
REMARK 3 T11: 0.0574 T22: -0.1621
REMARK 3 T33: -0.0077 T12: 0.1320
REMARK 3 T13: 0.0097 T23: 0.1598
REMARK 3 L TENSOR
REMARK 3 L11: 9.0090 L22: 3.6690
REMARK 3 L33: 7.6675 L12: 0.4555
REMARK 3 L13: 3.0830 L23: 1.4017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0959 S12: -0.6636 S13: -0.1754
REMARK 3 S21: 0.1559 S22: 0.0791 S23: -0.1912
REMARK 3 S31: 0.6796 S32: 0.5082 S33: -0.1750
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 16 E 107
REMARK 3 ORIGIN FOR THE GROUP (A): 72.4095 10.9642 25.8271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.2862
REMARK 3 T33: 0.3091 T12: 0.0054
REMARK 3 T13: -0.2181 T23: -0.0768
REMARK 3 L TENSOR
REMARK 3 L11: 7.5286 L22: 8.0758
REMARK 3 L33: 2.7362 L12: -0.2144
REMARK 3 L13: 3.6575 L23: 0.2816
REMARK 3 S TENSOR
REMARK 3 S11: 0.1961 S12: 0.4553 S13: -0.9105
REMARK 3 S21: 1.1510 S22: 0.0806 S23: -0.9484
REMARK 3 S31: 0.7759 S32: 0.4222 S33: -0.2766
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 108 E 189
REMARK 3 ORIGIN FOR THE GROUP (A): 75.5916 32.4096 20.2041
REMARK 3 T TENSOR
REMARK 3 T11: 0.0138 T22: 0.5055
REMARK 3 T33: 0.0191 T12: -0.2631
REMARK 3 T13: -0.1396 T23: 0.1069
REMARK 3 L TENSOR
REMARK 3 L11: 8.2768 L22: 14.6074
REMARK 3 L33: 8.2975 L12: -1.5859
REMARK 3 L13: -1.0667 L23: 3.5806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0970 S12: 0.3555 S13: 0.2298
REMARK 3 S21: -1.0059 S22: 0.3292 S23: -0.9208
REMARK 3 S31: -1.1340 S32: 0.8376 S33: -0.4262
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 190 E 201
REMARK 3 ORIGIN FOR THE GROUP (A): 56.7710 28.9180 21.1929
REMARK 3 T TENSOR
REMARK 3 T11: 0.6017 T22: 0.5796
REMARK 3 T33: 0.3186 T12: -0.3302
REMARK 3 T13: 0.0061 T23: 0.2644
REMARK 3 L TENSOR
REMARK 3 L11: 20.7049 L22: 21.4528
REMARK 3 L33: 2.3531 L12: 21.0755
REMARK 3 L13: 6.9801 L23: 7.1050
REMARK 3 S TENSOR
REMARK 3 S11: -0.5167 S12: 0.2308 S13: 0.7522
REMARK 3 S21: 1.5784 S22: 1.0680 S23: 2.2946
REMARK 3 S31: -2.4714 S32: -0.5496 S33: -0.5513
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 202 E 371
REMARK 3 ORIGIN FOR THE GROUP (A): 44.6588 12.0482 2.8313
REMARK 3 T TENSOR
REMARK 3 T11: -0.3749 T22: -0.1869
REMARK 3 T33: -0.1706 T12: 0.0155
REMARK 3 T13: -0.0600 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 3.5738 L22: 3.6740
REMARK 3 L33: 4.4205 L12: -0.5871
REMARK 3 L13: -1.3268 L23: 0.2362
REMARK 3 S TENSOR
REMARK 3 S11: 0.1813 S12: 0.4531 S13: -0.2230
REMARK 3 S21: -0.2925 S22: -0.1450 S23: -0.0792
REMARK 3 S31: 0.0041 S32: 0.2251 S33: -0.0363
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 372 E 460
REMARK 3 ORIGIN FOR THE GROUP (A): 40.1793 23.7128 35.8067
REMARK 3 T TENSOR
REMARK 3 T11: -0.1518 T22: -0.0459
REMARK 3 T33: -0.1473 T12: 0.0140
REMARK 3 T13: -0.1319 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 4.6499 L22: 11.0069
REMARK 3 L33: 4.8682 L12: -1.1931
REMARK 3 L13: -0.5507 L23: 1.4376
REMARK 3 S TENSOR
REMARK 3 S11: -0.0916 S12: -0.6544 S13: 0.5719
REMARK 3 S21: 0.8253 S22: -0.0691 S23: -0.1611
REMARK 3 S31: 0.0028 S32: 0.1874 S33: 0.1607
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 16 F 107
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7745 62.5285 40.9934
REMARK 3 T TENSOR
REMARK 3 T11: 0.1021 T22: 0.0340
REMARK 3 T33: 0.1632 T12: -0.0487
REMARK 3 T13: -0.0086 T23: -0.2199
REMARK 3 L TENSOR
REMARK 3 L11: 4.0424 L22: 8.9255
REMARK 3 L33: 6.6815 L12: -0.6382
REMARK 3 L13: 2.6784 L23: -2.2005
REMARK 3 S TENSOR
REMARK 3 S11: 0.1399 S12: -0.3874 S13: -0.0978
REMARK 3 S21: 1.0245 S22: 0.2559 S23: -0.7785
REMARK 3 S31: -0.5382 S32: 0.2598 S33: -0.3958
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 108 F 189
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0361 76.3524 23.3950
REMARK 3 T TENSOR
REMARK 3 T11: 0.5531 T22: 0.0252
REMARK 3 T33: 0.5013 T12: -0.3298
REMARK 3 T13: 0.4810 T23: -0.1052
REMARK 3 L TENSOR
REMARK 3 L11: 13.0223 L22: 7.7723
REMARK 3 L33: 10.9453 L12: -4.7103
REMARK 3 L13: 4.0686 L23: -2.1386
REMARK 3 S TENSOR
REMARK 3 S11: 0.1197 S12: 0.4408 S13: 1.1365
REMARK 3 S21: -0.7076 S22: -0.0435 S23: -1.2921
REMARK 3 S31: -1.2132 S32: 0.3435 S33: -0.0762
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 190 F 201
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5804 62.8063 19.9039
REMARK 3 T TENSOR
REMARK 3 T11: 0.7502 T22: 0.2384
REMARK 3 T33: 0.4500 T12: -0.1196
REMARK 3 T13: 0.1877 T23: -0.2069
REMARK 3 L TENSOR
REMARK 3 L11: 0.9237 L22: 59.1956
REMARK 3 L33: 19.9576 L12: 7.3945
REMARK 3 L13: -4.2935 L23: -34.3715
REMARK 3 S TENSOR
REMARK 3 S11: -0.3257 S12: 1.6172 S13: -0.9880
REMARK 3 S21: -1.7457 S22: 1.0540 S23: 0.5384
REMARK 3 S31: -0.3149 S32: -1.4521 S33: -0.7283
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 202 F 371
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1236 36.6797 16.3968
REMARK 3 T TENSOR
REMARK 3 T11: -0.3652 T22: -0.2944
REMARK 3 T33: -0.1268 T12: 0.0187
REMARK 3 T13: -0.0189 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 4.6196 L22: 3.6962
REMARK 3 L33: 4.2565 L12: 0.0801
REMARK 3 L13: -0.2031 L23: 0.0523
REMARK 3 S TENSOR
REMARK 3 S11: 0.1947 S12: 0.1947 S13: -0.0946
REMARK 3 S21: -0.0996 S22: -0.0668 S23: -0.5139
REMARK 3 S31: 0.0462 S32: 0.3047 S33: -0.1278
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 372 F 460
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3325 55.2935 27.0031
REMARK 3 T TENSOR
REMARK 3 T11: -0.1072 T22: -0.1605
REMARK 3 T33: -0.1497 T12: -0.0470
REMARK 3 T13: 0.0330 T23: -0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 5.5176 L22: 6.5538
REMARK 3 L33: 3.1754 L12: -3.2576
REMARK 3 L13: -0.0603 L23: -0.8046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0401 S13: 0.3605
REMARK 3 S21: 0.0162 S22: 0.1076 S23: 0.2797
REMARK 3 S31: -0.6340 S32: -0.2091 S33: -0.0856
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: NULL
REMARK 4
REMARK 4 3HU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053582.
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 : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85163
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NACL, 4% BENZAMIDINE, 100MM
REMARK 280 CITRATE, PH 5.8, 16.5% PEG3350 AND 20% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 116560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 ALA A 5
REMARK 465 ASP A 6
REMARK 465 SER A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 ASP A 10
REMARK 465 ASP A 11
REMARK 465 LEU A 464
REMARK 465 ARG A 465
REMARK 465 GLU A 466
REMARK 465 THR A 467
REMARK 465 VAL A 468
REMARK 465 VAL A 469
REMARK 465 GLU A 470
REMARK 465 VAL A 471
REMARK 465 PRO A 472
REMARK 465 GLN A 473
REMARK 465 VAL A 474
REMARK 465 THR A 475
REMARK 465 TRP A 476
REMARK 465 GLU A 477
REMARK 465 ASP A 478
REMARK 465 ILE A 479
REMARK 465 GLY A 480
REMARK 465 GLY A 481
REMARK 465 ARG A 482
REMARK 465 SER A 483
REMARK 465 HIS A 484
REMARK 465 HIS A 485
REMARK 465 HIS A 486
REMARK 465 HIS A 487
REMARK 465 HIS A 488
REMARK 465 HIS A 489
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLY B 4
REMARK 465 ALA B 5
REMARK 465 ASP B 6
REMARK 465 SER B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 ASP B 10
REMARK 465 ASP B 11
REMARK 465 LEU B 464
REMARK 465 ARG B 465
REMARK 465 GLU B 466
REMARK 465 THR B 467
REMARK 465 VAL B 468
REMARK 465 VAL B 469
REMARK 465 GLU B 470
REMARK 465 VAL B 471
REMARK 465 PRO B 472
REMARK 465 GLN B 473
REMARK 465 VAL B 474
REMARK 465 THR B 475
REMARK 465 TRP B 476
REMARK 465 GLU B 477
REMARK 465 ASP B 478
REMARK 465 ILE B 479
REMARK 465 GLY B 480
REMARK 465 GLY B 481
REMARK 465 ARG B 482
REMARK 465 SER B 483
REMARK 465 HIS B 484
REMARK 465 HIS B 485
REMARK 465 HIS B 486
REMARK 465 HIS B 487
REMARK 465 HIS B 488
REMARK 465 HIS B 489
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 SER C 3
REMARK 465 GLY C 4
REMARK 465 ALA C 5
REMARK 465 ASP C 6
REMARK 465 SER C 7
REMARK 465 LYS C 8
REMARK 465 GLY C 9
REMARK 465 ASP C 10
REMARK 465 ASP C 11
REMARK 465 LEU C 464
REMARK 465 ARG C 465
REMARK 465 GLU C 466
REMARK 465 THR C 467
REMARK 465 VAL C 468
REMARK 465 VAL C 469
REMARK 465 GLU C 470
REMARK 465 VAL C 471
REMARK 465 PRO C 472
REMARK 465 GLN C 473
REMARK 465 VAL C 474
REMARK 465 THR C 475
REMARK 465 TRP C 476
REMARK 465 GLU C 477
REMARK 465 ASP C 478
REMARK 465 ILE C 479
REMARK 465 GLY C 480
REMARK 465 GLY C 481
REMARK 465 ARG C 482
REMARK 465 SER C 483
REMARK 465 HIS C 484
REMARK 465 HIS C 485
REMARK 465 HIS C 486
REMARK 465 HIS C 487
REMARK 465 HIS C 488
REMARK 465 HIS C 489
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 SER D 3
REMARK 465 GLY D 4
REMARK 465 ALA D 5
REMARK 465 ASP D 6
REMARK 465 SER D 7
REMARK 465 LYS D 8
REMARK 465 GLY D 9
REMARK 465 ASP D 10
REMARK 465 ASP D 11
REMARK 465 LEU D 464
REMARK 465 ARG D 465
REMARK 465 GLU D 466
REMARK 465 THR D 467
REMARK 465 VAL D 468
REMARK 465 VAL D 469
REMARK 465 GLU D 470
REMARK 465 VAL D 471
REMARK 465 PRO D 472
REMARK 465 GLN D 473
REMARK 465 VAL D 474
REMARK 465 THR D 475
REMARK 465 TRP D 476
REMARK 465 GLU D 477
REMARK 465 ASP D 478
REMARK 465 ILE D 479
REMARK 465 GLY D 480
REMARK 465 GLY D 481
REMARK 465 ARG D 482
REMARK 465 SER D 483
REMARK 465 HIS D 484
REMARK 465 HIS D 485
REMARK 465 HIS D 486
REMARK 465 HIS D 487
REMARK 465 HIS D 488
REMARK 465 HIS D 489
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 SER E 3
REMARK 465 GLY E 4
REMARK 465 ALA E 5
REMARK 465 ASP E 6
REMARK 465 SER E 7
REMARK 465 LYS E 8
REMARK 465 GLY E 9
REMARK 465 ASP E 10
REMARK 465 ASP E 11
REMARK 465 LEU E 464
REMARK 465 ARG E 465
REMARK 465 GLU E 466
REMARK 465 THR E 467
REMARK 465 VAL E 468
REMARK 465 VAL E 469
REMARK 465 GLU E 470
REMARK 465 VAL E 471
REMARK 465 PRO E 472
REMARK 465 GLN E 473
REMARK 465 VAL E 474
REMARK 465 THR E 475
REMARK 465 TRP E 476
REMARK 465 GLU E 477
REMARK 465 ASP E 478
REMARK 465 ILE E 479
REMARK 465 GLY E 480
REMARK 465 GLY E 481
REMARK 465 ARG E 482
REMARK 465 SER E 483
REMARK 465 HIS E 484
REMARK 465 HIS E 485
REMARK 465 HIS E 486
REMARK 465 HIS E 487
REMARK 465 HIS E 488
REMARK 465 HIS E 489
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 SER F 3
REMARK 465 GLY F 4
REMARK 465 ALA F 5
REMARK 465 ASP F 6
REMARK 465 SER F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 ASP F 10
REMARK 465 ASP F 11
REMARK 465 LEU F 464
REMARK 465 ARG F 465
REMARK 465 GLU F 466
REMARK 465 THR F 467
REMARK 465 VAL F 468
REMARK 465 VAL F 469
REMARK 465 GLU F 470
REMARK 465 VAL F 471
REMARK 465 PRO F 472
REMARK 465 GLN F 473
REMARK 465 VAL F 474
REMARK 465 THR F 475
REMARK 465 TRP F 476
REMARK 465 GLU F 477
REMARK 465 ASP F 478
REMARK 465 ILE F 479
REMARK 465 GLY F 480
REMARK 465 GLY F 481
REMARK 465 ARG F 482
REMARK 465 SER F 483
REMARK 465 HIS F 484
REMARK 465 HIS F 485
REMARK 465 HIS F 486
REMARK 465 HIS F 487
REMARK 465 HIS F 488
REMARK 465 HIS F 489
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 O2G AGS C 800 MG MG C 801 1.61
REMARK 500 O2G AGS D 800 MG MG D 801 1.66
REMARK 500 O2G AGS F 800 MG MG F 801 1.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS C 415 CB CYS C 415 SG -0.127
REMARK 500 CYS F 415 CB CYS F 415 SG -0.104
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 LYS A 20 105.55 63.19
REMARK 500 ARG A 64 -17.34 74.95
REMARK 500 ILE A 126 95.47 30.51
REMARK 500 SER A 171 -71.60 -45.08
REMARK 500 ASN A 199 30.03 -92.89
REMARK 500 HIS A 226 58.60 -142.27
REMARK 500 ALA A 297 -87.93 -4.18
REMARK 500 ARG A 313 -17.52 -47.42
REMARK 500 ARG A 362 -126.96 -90.56
REMARK 500 LEU A 445 102.03 -58.47
REMARK 500 THR B 14 -9.04 -54.72
REMARK 500 LYS B 20 109.68 58.56
REMARK 500 ARG B 64 -15.64 75.92
REMARK 500 ILE B 126 96.65 33.95
REMARK 500 SER B 171 -77.36 -37.92
REMARK 500 CYS B 184 12.25 -140.46
REMARK 500 ASN B 199 34.69 -96.92
REMARK 500 HIS B 226 55.85 -144.38
REMARK 500 ALA B 297 -83.48 -9.72
REMARK 500 ALA B 310 58.29 -119.68
REMARK 500 ARG B 338 13.03 -66.91
REMARK 500 ARG B 362 -131.96 -96.03
REMARK 500 LEU B 445 98.41 -57.84
REMARK 500 SER B 462 42.55 -81.65
REMARK 500 ALA C 15 -35.29 -37.57
REMARK 500 LYS C 20 105.03 62.03
REMARK 500 ARG C 64 -22.33 72.75
REMARK 500 ILE C 126 95.96 39.84
REMARK 500 CYS C 184 15.98 -140.30
REMARK 500 ASN C 199 34.70 -93.87
REMARK 500 VAL C 220 -54.54 -121.66
REMARK 500 HIS C 226 54.51 -141.69
REMARK 500 ALA C 297 -84.15 -7.34
REMARK 500 ARG C 313 -18.91 -45.17
REMARK 500 ARG C 362 -128.59 -94.73
REMARK 500 THR C 403 66.90 -102.04
REMARK 500 LYS D 20 108.99 62.93
REMARK 500 ARG D 64 -25.41 74.96
REMARK 500 ILE D 126 96.39 38.67
REMARK 500 LEU D 140 108.26 -52.73
REMARK 500 ASN D 199 34.51 -94.96
REMARK 500 HIS D 226 55.96 -140.74
REMARK 500 ALA D 297 -82.93 -14.46
REMARK 500 GLU D 305 60.14 60.69
REMARK 500 ARG D 313 -17.55 -45.33
REMARK 500 ARG D 362 -123.72 -90.70
REMARK 500 THR D 403 51.54 -119.06
REMARK 500 LYS E 20 101.35 63.40
REMARK 500 ARG E 64 -24.53 75.74
REMARK 500 VAL E 123 14.81 -149.84
REMARK 500
REMARK 500 THIS ENTRY HAS 70 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 MG A 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 252 OG1
REMARK 620 2 AGS A 800 O2G 175.3
REMARK 620 3 AGS A 800 O1B 84.4 98.7
REMARK 620 4 HOH A 802 O 85.0 91.3 93.0
REMARK 620 5 HOH A 803 O 75.8 101.2 160.2 87.0
REMARK 620 6 HOH A 804 O 90.6 92.6 95.3 170.1 83.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 252 OG1
REMARK 620 2 AGS B 800 O2G 177.9
REMARK 620 3 AGS B 800 O1B 81.7 96.6
REMARK 620 4 HOH B 802 O 81.1 100.5 105.0
REMARK 620 5 HOH B 803 O 83.9 97.7 165.1 76.5
REMARK 620 6 HOH B 804 O 72.5 106.5 91.3 146.6 80.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 252 OG1
REMARK 620 2 AGS C 800 O1B 73.6
REMARK 620 3 HOH C 802 O 83.2 93.1
REMARK 620 4 HOH C 803 O 78.5 150.4 73.7
REMARK 620 5 HOH C 804 O 76.1 79.1 159.2 103.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 252 OG1
REMARK 620 2 AGS D 800 O1B 80.4
REMARK 620 3 HOH D 803 O 73.4 153.8
REMARK 620 4 HOH D 804 O 75.0 92.4 79.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 252 OG1
REMARK 620 2 AGS E 800 O2G 178.2
REMARK 620 3 AGS E 800 O1B 80.5 97.8
REMARK 620 4 HOH E 802 O 79.7 100.1 106.5
REMARK 620 5 HOH E 803 O 75.6 106.1 154.2 78.9
REMARK 620 6 HOH E 804 O 71.6 109.1 87.1 145.7 76.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 252 OG1
REMARK 620 2 AGS F 800 O1B 80.7
REMARK 620 3 HOH F 802 O 77.9 102.7
REMARK 620 4 HOH F 803 O 73.1 152.9 65.4
REMARK 620 5 HOH F 804 O 82.8 102.7 144.9 81.1
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 AGS A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS D 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS E 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS F 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HU1 RELATED DB: PDB
REMARK 900 STRUCTURE OF P97 N-D1 R95G MUTANT IN COMPLEX WITH ATPGS
REMARK 900 RELATED ID: 3HU3 RELATED DB: PDB
REMARK 900 STRUCTURE OF P97 N-D1 R155H MUTANT IN COMPLEX WITH ATPGS
DBREF 3HU2 A 1 481 UNP P55072 TERA_HUMAN 1 481
DBREF 3HU2 B 1 481 UNP P55072 TERA_HUMAN 1 481
DBREF 3HU2 C 1 481 UNP P55072 TERA_HUMAN 1 481
DBREF 3HU2 D 1 481 UNP P55072 TERA_HUMAN 1 481
DBREF 3HU2 E 1 481 UNP P55072 TERA_HUMAN 1 481
DBREF 3HU2 F 1 481 UNP P55072 TERA_HUMAN 1 481
SEQADV 3HU2 ALA A 86 UNP P55072 ARG 86 ENGINEERED MUTATION
SEQADV 3HU2 ARG A 482 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 SER A 483 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS A 484 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS A 485 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS A 486 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS A 487 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS A 488 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS A 489 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 ALA B 86 UNP P55072 ARG 86 ENGINEERED MUTATION
SEQADV 3HU2 ARG B 482 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 SER B 483 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS B 484 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS B 485 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS B 486 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS B 487 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS B 488 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS B 489 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 ALA C 86 UNP P55072 ARG 86 ENGINEERED MUTATION
SEQADV 3HU2 ARG C 482 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 SER C 483 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS C 484 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS C 485 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS C 486 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS C 487 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS C 488 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS C 489 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 ALA D 86 UNP P55072 ARG 86 ENGINEERED MUTATION
SEQADV 3HU2 ARG D 482 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 SER D 483 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS D 484 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS D 485 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS D 486 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS D 487 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS D 488 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS D 489 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 ALA E 86 UNP P55072 ARG 86 ENGINEERED MUTATION
SEQADV 3HU2 ARG E 482 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 SER E 483 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS E 484 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS E 485 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS E 486 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS E 487 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS E 488 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS E 489 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 ALA F 86 UNP P55072 ARG 86 ENGINEERED MUTATION
SEQADV 3HU2 ARG F 482 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 SER F 483 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS F 484 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS F 485 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS F 486 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS F 487 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS F 488 UNP P55072 EXPRESSION TAG
SEQADV 3HU2 HIS F 489 UNP P55072 EXPRESSION TAG
SEQRES 1 A 489 MET ALA SER GLY ALA ASP SER LYS GLY ASP ASP LEU SER
SEQRES 2 A 489 THR ALA ILE LEU LYS GLN LYS ASN ARG PRO ASN ARG LEU
SEQRES 3 A 489 ILE VAL ASP GLU ALA ILE ASN GLU ASP ASN SER VAL VAL
SEQRES 4 A 489 SER LEU SER GLN PRO LYS MET ASP GLU LEU GLN LEU PHE
SEQRES 5 A 489 ARG GLY ASP THR VAL LEU LEU LYS GLY LYS LYS ARG ARG
SEQRES 6 A 489 GLU ALA VAL CYS ILE VAL LEU SER ASP ASP THR CYS SER
SEQRES 7 A 489 ASP GLU LYS ILE ARG MET ASN ALA VAL VAL ARG ASN ASN
SEQRES 8 A 489 LEU ARG VAL ARG LEU GLY ASP VAL ILE SER ILE GLN PRO
SEQRES 9 A 489 CYS PRO ASP VAL LYS TYR GLY LYS ARG ILE HIS VAL LEU
SEQRES 10 A 489 PRO ILE ASP ASP THR VAL GLU GLY ILE THR GLY ASN LEU
SEQRES 11 A 489 PHE GLU VAL TYR LEU LYS PRO TYR PHE LEU GLU ALA TYR
SEQRES 12 A 489 ARG PRO ILE ARG LYS GLY ASP ILE PHE LEU VAL ARG GLY
SEQRES 13 A 489 GLY MET ARG ALA VAL GLU PHE LYS VAL VAL GLU THR ASP
SEQRES 14 A 489 PRO SER PRO TYR CYS ILE VAL ALA PRO ASP THR VAL ILE
SEQRES 15 A 489 HIS CYS GLU GLY GLU PRO ILE LYS ARG GLU ASP GLU GLU
SEQRES 16 A 489 GLU SER LEU ASN GLU VAL GLY TYR ASP ASP ILE GLY GLY
SEQRES 17 A 489 CYS ARG LYS GLN LEU ALA GLN ILE LYS GLU MET VAL GLU
SEQRES 18 A 489 LEU PRO LEU ARG HIS PRO ALA LEU PHE LYS ALA ILE GLY
SEQRES 19 A 489 VAL LYS PRO PRO ARG GLY ILE LEU LEU TYR GLY PRO PRO
SEQRES 20 A 489 GLY THR GLY LYS THR LEU ILE ALA ARG ALA VAL ALA ASN
SEQRES 21 A 489 GLU THR GLY ALA PHE PHE PHE LEU ILE ASN GLY PRO GLU
SEQRES 22 A 489 ILE MET SER LYS LEU ALA GLY GLU SER GLU SER ASN LEU
SEQRES 23 A 489 ARG LYS ALA PHE GLU GLU ALA GLU LYS ASN ALA PRO ALA
SEQRES 24 A 489 ILE ILE PHE ILE ASP GLU LEU ASP ALA ILE ALA PRO LYS
SEQRES 25 A 489 ARG GLU LYS THR HIS GLY GLU VAL GLU ARG ARG ILE VAL
SEQRES 26 A 489 SER GLN LEU LEU THR LEU MET ASP GLY LEU LYS GLN ARG
SEQRES 27 A 489 ALA HIS VAL ILE VAL MET ALA ALA THR ASN ARG PRO ASN
SEQRES 28 A 489 SER ILE ASP PRO ALA LEU ARG ARG PHE GLY ARG PHE ASP
SEQRES 29 A 489 ARG GLU VAL ASP ILE GLY ILE PRO ASP ALA THR GLY ARG
SEQRES 30 A 489 LEU GLU ILE LEU GLN ILE HIS THR LYS ASN MET LYS LEU
SEQRES 31 A 489 ALA ASP ASP VAL ASP LEU GLU GLN VAL ALA ASN GLU THR
SEQRES 32 A 489 HIS GLY HIS VAL GLY ALA ASP LEU ALA ALA LEU CYS SER
SEQRES 33 A 489 GLU ALA ALA LEU GLN ALA ILE ARG LYS LYS MET ASP LEU
SEQRES 34 A 489 ILE ASP LEU GLU ASP GLU THR ILE ASP ALA GLU VAL MET
SEQRES 35 A 489 ASN SER LEU ALA VAL THR MET ASP ASP PHE ARG TRP ALA
SEQRES 36 A 489 LEU SER GLN SER ASN PRO SER ALA LEU ARG GLU THR VAL
SEQRES 37 A 489 VAL GLU VAL PRO GLN VAL THR TRP GLU ASP ILE GLY GLY
SEQRES 38 A 489 ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 489 MET ALA SER GLY ALA ASP SER LYS GLY ASP ASP LEU SER
SEQRES 2 B 489 THR ALA ILE LEU LYS GLN LYS ASN ARG PRO ASN ARG LEU
SEQRES 3 B 489 ILE VAL ASP GLU ALA ILE ASN GLU ASP ASN SER VAL VAL
SEQRES 4 B 489 SER LEU SER GLN PRO LYS MET ASP GLU LEU GLN LEU PHE
SEQRES 5 B 489 ARG GLY ASP THR VAL LEU LEU LYS GLY LYS LYS ARG ARG
SEQRES 6 B 489 GLU ALA VAL CYS ILE VAL LEU SER ASP ASP THR CYS SER
SEQRES 7 B 489 ASP GLU LYS ILE ARG MET ASN ALA VAL VAL ARG ASN ASN
SEQRES 8 B 489 LEU ARG VAL ARG LEU GLY ASP VAL ILE SER ILE GLN PRO
SEQRES 9 B 489 CYS PRO ASP VAL LYS TYR GLY LYS ARG ILE HIS VAL LEU
SEQRES 10 B 489 PRO ILE ASP ASP THR VAL GLU GLY ILE THR GLY ASN LEU
SEQRES 11 B 489 PHE GLU VAL TYR LEU LYS PRO TYR PHE LEU GLU ALA TYR
SEQRES 12 B 489 ARG PRO ILE ARG LYS GLY ASP ILE PHE LEU VAL ARG GLY
SEQRES 13 B 489 GLY MET ARG ALA VAL GLU PHE LYS VAL VAL GLU THR ASP
SEQRES 14 B 489 PRO SER PRO TYR CYS ILE VAL ALA PRO ASP THR VAL ILE
SEQRES 15 B 489 HIS CYS GLU GLY GLU PRO ILE LYS ARG GLU ASP GLU GLU
SEQRES 16 B 489 GLU SER LEU ASN GLU VAL GLY TYR ASP ASP ILE GLY GLY
SEQRES 17 B 489 CYS ARG LYS GLN LEU ALA GLN ILE LYS GLU MET VAL GLU
SEQRES 18 B 489 LEU PRO LEU ARG HIS PRO ALA LEU PHE LYS ALA ILE GLY
SEQRES 19 B 489 VAL LYS PRO PRO ARG GLY ILE LEU LEU TYR GLY PRO PRO
SEQRES 20 B 489 GLY THR GLY LYS THR LEU ILE ALA ARG ALA VAL ALA ASN
SEQRES 21 B 489 GLU THR GLY ALA PHE PHE PHE LEU ILE ASN GLY PRO GLU
SEQRES 22 B 489 ILE MET SER LYS LEU ALA GLY GLU SER GLU SER ASN LEU
SEQRES 23 B 489 ARG LYS ALA PHE GLU GLU ALA GLU LYS ASN ALA PRO ALA
SEQRES 24 B 489 ILE ILE PHE ILE ASP GLU LEU ASP ALA ILE ALA PRO LYS
SEQRES 25 B 489 ARG GLU LYS THR HIS GLY GLU VAL GLU ARG ARG ILE VAL
SEQRES 26 B 489 SER GLN LEU LEU THR LEU MET ASP GLY LEU LYS GLN ARG
SEQRES 27 B 489 ALA HIS VAL ILE VAL MET ALA ALA THR ASN ARG PRO ASN
SEQRES 28 B 489 SER ILE ASP PRO ALA LEU ARG ARG PHE GLY ARG PHE ASP
SEQRES 29 B 489 ARG GLU VAL ASP ILE GLY ILE PRO ASP ALA THR GLY ARG
SEQRES 30 B 489 LEU GLU ILE LEU GLN ILE HIS THR LYS ASN MET LYS LEU
SEQRES 31 B 489 ALA ASP ASP VAL ASP LEU GLU GLN VAL ALA ASN GLU THR
SEQRES 32 B 489 HIS GLY HIS VAL GLY ALA ASP LEU ALA ALA LEU CYS SER
SEQRES 33 B 489 GLU ALA ALA LEU GLN ALA ILE ARG LYS LYS MET ASP LEU
SEQRES 34 B 489 ILE ASP LEU GLU ASP GLU THR ILE ASP ALA GLU VAL MET
SEQRES 35 B 489 ASN SER LEU ALA VAL THR MET ASP ASP PHE ARG TRP ALA
SEQRES 36 B 489 LEU SER GLN SER ASN PRO SER ALA LEU ARG GLU THR VAL
SEQRES 37 B 489 VAL GLU VAL PRO GLN VAL THR TRP GLU ASP ILE GLY GLY
SEQRES 38 B 489 ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 C 489 MET ALA SER GLY ALA ASP SER LYS GLY ASP ASP LEU SER
SEQRES 2 C 489 THR ALA ILE LEU LYS GLN LYS ASN ARG PRO ASN ARG LEU
SEQRES 3 C 489 ILE VAL ASP GLU ALA ILE ASN GLU ASP ASN SER VAL VAL
SEQRES 4 C 489 SER LEU SER GLN PRO LYS MET ASP GLU LEU GLN LEU PHE
SEQRES 5 C 489 ARG GLY ASP THR VAL LEU LEU LYS GLY LYS LYS ARG ARG
SEQRES 6 C 489 GLU ALA VAL CYS ILE VAL LEU SER ASP ASP THR CYS SER
SEQRES 7 C 489 ASP GLU LYS ILE ARG MET ASN ALA VAL VAL ARG ASN ASN
SEQRES 8 C 489 LEU ARG VAL ARG LEU GLY ASP VAL ILE SER ILE GLN PRO
SEQRES 9 C 489 CYS PRO ASP VAL LYS TYR GLY LYS ARG ILE HIS VAL LEU
SEQRES 10 C 489 PRO ILE ASP ASP THR VAL GLU GLY ILE THR GLY ASN LEU
SEQRES 11 C 489 PHE GLU VAL TYR LEU LYS PRO TYR PHE LEU GLU ALA TYR
SEQRES 12 C 489 ARG PRO ILE ARG LYS GLY ASP ILE PHE LEU VAL ARG GLY
SEQRES 13 C 489 GLY MET ARG ALA VAL GLU PHE LYS VAL VAL GLU THR ASP
SEQRES 14 C 489 PRO SER PRO TYR CYS ILE VAL ALA PRO ASP THR VAL ILE
SEQRES 15 C 489 HIS CYS GLU GLY GLU PRO ILE LYS ARG GLU ASP GLU GLU
SEQRES 16 C 489 GLU SER LEU ASN GLU VAL GLY TYR ASP ASP ILE GLY GLY
SEQRES 17 C 489 CYS ARG LYS GLN LEU ALA GLN ILE LYS GLU MET VAL GLU
SEQRES 18 C 489 LEU PRO LEU ARG HIS PRO ALA LEU PHE LYS ALA ILE GLY
SEQRES 19 C 489 VAL LYS PRO PRO ARG GLY ILE LEU LEU TYR GLY PRO PRO
SEQRES 20 C 489 GLY THR GLY LYS THR LEU ILE ALA ARG ALA VAL ALA ASN
SEQRES 21 C 489 GLU THR GLY ALA PHE PHE PHE LEU ILE ASN GLY PRO GLU
SEQRES 22 C 489 ILE MET SER LYS LEU ALA GLY GLU SER GLU SER ASN LEU
SEQRES 23 C 489 ARG LYS ALA PHE GLU GLU ALA GLU LYS ASN ALA PRO ALA
SEQRES 24 C 489 ILE ILE PHE ILE ASP GLU LEU ASP ALA ILE ALA PRO LYS
SEQRES 25 C 489 ARG GLU LYS THR HIS GLY GLU VAL GLU ARG ARG ILE VAL
SEQRES 26 C 489 SER GLN LEU LEU THR LEU MET ASP GLY LEU LYS GLN ARG
SEQRES 27 C 489 ALA HIS VAL ILE VAL MET ALA ALA THR ASN ARG PRO ASN
SEQRES 28 C 489 SER ILE ASP PRO ALA LEU ARG ARG PHE GLY ARG PHE ASP
SEQRES 29 C 489 ARG GLU VAL ASP ILE GLY ILE PRO ASP ALA THR GLY ARG
SEQRES 30 C 489 LEU GLU ILE LEU GLN ILE HIS THR LYS ASN MET LYS LEU
SEQRES 31 C 489 ALA ASP ASP VAL ASP LEU GLU GLN VAL ALA ASN GLU THR
SEQRES 32 C 489 HIS GLY HIS VAL GLY ALA ASP LEU ALA ALA LEU CYS SER
SEQRES 33 C 489 GLU ALA ALA LEU GLN ALA ILE ARG LYS LYS MET ASP LEU
SEQRES 34 C 489 ILE ASP LEU GLU ASP GLU THR ILE ASP ALA GLU VAL MET
SEQRES 35 C 489 ASN SER LEU ALA VAL THR MET ASP ASP PHE ARG TRP ALA
SEQRES 36 C 489 LEU SER GLN SER ASN PRO SER ALA LEU ARG GLU THR VAL
SEQRES 37 C 489 VAL GLU VAL PRO GLN VAL THR TRP GLU ASP ILE GLY GLY
SEQRES 38 C 489 ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 D 489 MET ALA SER GLY ALA ASP SER LYS GLY ASP ASP LEU SER
SEQRES 2 D 489 THR ALA ILE LEU LYS GLN LYS ASN ARG PRO ASN ARG LEU
SEQRES 3 D 489 ILE VAL ASP GLU ALA ILE ASN GLU ASP ASN SER VAL VAL
SEQRES 4 D 489 SER LEU SER GLN PRO LYS MET ASP GLU LEU GLN LEU PHE
SEQRES 5 D 489 ARG GLY ASP THR VAL LEU LEU LYS GLY LYS LYS ARG ARG
SEQRES 6 D 489 GLU ALA VAL CYS ILE VAL LEU SER ASP ASP THR CYS SER
SEQRES 7 D 489 ASP GLU LYS ILE ARG MET ASN ALA VAL VAL ARG ASN ASN
SEQRES 8 D 489 LEU ARG VAL ARG LEU GLY ASP VAL ILE SER ILE GLN PRO
SEQRES 9 D 489 CYS PRO ASP VAL LYS TYR GLY LYS ARG ILE HIS VAL LEU
SEQRES 10 D 489 PRO ILE ASP ASP THR VAL GLU GLY ILE THR GLY ASN LEU
SEQRES 11 D 489 PHE GLU VAL TYR LEU LYS PRO TYR PHE LEU GLU ALA TYR
SEQRES 12 D 489 ARG PRO ILE ARG LYS GLY ASP ILE PHE LEU VAL ARG GLY
SEQRES 13 D 489 GLY MET ARG ALA VAL GLU PHE LYS VAL VAL GLU THR ASP
SEQRES 14 D 489 PRO SER PRO TYR CYS ILE VAL ALA PRO ASP THR VAL ILE
SEQRES 15 D 489 HIS CYS GLU GLY GLU PRO ILE LYS ARG GLU ASP GLU GLU
SEQRES 16 D 489 GLU SER LEU ASN GLU VAL GLY TYR ASP ASP ILE GLY GLY
SEQRES 17 D 489 CYS ARG LYS GLN LEU ALA GLN ILE LYS GLU MET VAL GLU
SEQRES 18 D 489 LEU PRO LEU ARG HIS PRO ALA LEU PHE LYS ALA ILE GLY
SEQRES 19 D 489 VAL LYS PRO PRO ARG GLY ILE LEU LEU TYR GLY PRO PRO
SEQRES 20 D 489 GLY THR GLY LYS THR LEU ILE ALA ARG ALA VAL ALA ASN
SEQRES 21 D 489 GLU THR GLY ALA PHE PHE PHE LEU ILE ASN GLY PRO GLU
SEQRES 22 D 489 ILE MET SER LYS LEU ALA GLY GLU SER GLU SER ASN LEU
SEQRES 23 D 489 ARG LYS ALA PHE GLU GLU ALA GLU LYS ASN ALA PRO ALA
SEQRES 24 D 489 ILE ILE PHE ILE ASP GLU LEU ASP ALA ILE ALA PRO LYS
SEQRES 25 D 489 ARG GLU LYS THR HIS GLY GLU VAL GLU ARG ARG ILE VAL
SEQRES 26 D 489 SER GLN LEU LEU THR LEU MET ASP GLY LEU LYS GLN ARG
SEQRES 27 D 489 ALA HIS VAL ILE VAL MET ALA ALA THR ASN ARG PRO ASN
SEQRES 28 D 489 SER ILE ASP PRO ALA LEU ARG ARG PHE GLY ARG PHE ASP
SEQRES 29 D 489 ARG GLU VAL ASP ILE GLY ILE PRO ASP ALA THR GLY ARG
SEQRES 30 D 489 LEU GLU ILE LEU GLN ILE HIS THR LYS ASN MET LYS LEU
SEQRES 31 D 489 ALA ASP ASP VAL ASP LEU GLU GLN VAL ALA ASN GLU THR
SEQRES 32 D 489 HIS GLY HIS VAL GLY ALA ASP LEU ALA ALA LEU CYS SER
SEQRES 33 D 489 GLU ALA ALA LEU GLN ALA ILE ARG LYS LYS MET ASP LEU
SEQRES 34 D 489 ILE ASP LEU GLU ASP GLU THR ILE ASP ALA GLU VAL MET
SEQRES 35 D 489 ASN SER LEU ALA VAL THR MET ASP ASP PHE ARG TRP ALA
SEQRES 36 D 489 LEU SER GLN SER ASN PRO SER ALA LEU ARG GLU THR VAL
SEQRES 37 D 489 VAL GLU VAL PRO GLN VAL THR TRP GLU ASP ILE GLY GLY
SEQRES 38 D 489 ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 E 489 MET ALA SER GLY ALA ASP SER LYS GLY ASP ASP LEU SER
SEQRES 2 E 489 THR ALA ILE LEU LYS GLN LYS ASN ARG PRO ASN ARG LEU
SEQRES 3 E 489 ILE VAL ASP GLU ALA ILE ASN GLU ASP ASN SER VAL VAL
SEQRES 4 E 489 SER LEU SER GLN PRO LYS MET ASP GLU LEU GLN LEU PHE
SEQRES 5 E 489 ARG GLY ASP THR VAL LEU LEU LYS GLY LYS LYS ARG ARG
SEQRES 6 E 489 GLU ALA VAL CYS ILE VAL LEU SER ASP ASP THR CYS SER
SEQRES 7 E 489 ASP GLU LYS ILE ARG MET ASN ALA VAL VAL ARG ASN ASN
SEQRES 8 E 489 LEU ARG VAL ARG LEU GLY ASP VAL ILE SER ILE GLN PRO
SEQRES 9 E 489 CYS PRO ASP VAL LYS TYR GLY LYS ARG ILE HIS VAL LEU
SEQRES 10 E 489 PRO ILE ASP ASP THR VAL GLU GLY ILE THR GLY ASN LEU
SEQRES 11 E 489 PHE GLU VAL TYR LEU LYS PRO TYR PHE LEU GLU ALA TYR
SEQRES 12 E 489 ARG PRO ILE ARG LYS GLY ASP ILE PHE LEU VAL ARG GLY
SEQRES 13 E 489 GLY MET ARG ALA VAL GLU PHE LYS VAL VAL GLU THR ASP
SEQRES 14 E 489 PRO SER PRO TYR CYS ILE VAL ALA PRO ASP THR VAL ILE
SEQRES 15 E 489 HIS CYS GLU GLY GLU PRO ILE LYS ARG GLU ASP GLU GLU
SEQRES 16 E 489 GLU SER LEU ASN GLU VAL GLY TYR ASP ASP ILE GLY GLY
SEQRES 17 E 489 CYS ARG LYS GLN LEU ALA GLN ILE LYS GLU MET VAL GLU
SEQRES 18 E 489 LEU PRO LEU ARG HIS PRO ALA LEU PHE LYS ALA ILE GLY
SEQRES 19 E 489 VAL LYS PRO PRO ARG GLY ILE LEU LEU TYR GLY PRO PRO
SEQRES 20 E 489 GLY THR GLY LYS THR LEU ILE ALA ARG ALA VAL ALA ASN
SEQRES 21 E 489 GLU THR GLY ALA PHE PHE PHE LEU ILE ASN GLY PRO GLU
SEQRES 22 E 489 ILE MET SER LYS LEU ALA GLY GLU SER GLU SER ASN LEU
SEQRES 23 E 489 ARG LYS ALA PHE GLU GLU ALA GLU LYS ASN ALA PRO ALA
SEQRES 24 E 489 ILE ILE PHE ILE ASP GLU LEU ASP ALA ILE ALA PRO LYS
SEQRES 25 E 489 ARG GLU LYS THR HIS GLY GLU VAL GLU ARG ARG ILE VAL
SEQRES 26 E 489 SER GLN LEU LEU THR LEU MET ASP GLY LEU LYS GLN ARG
SEQRES 27 E 489 ALA HIS VAL ILE VAL MET ALA ALA THR ASN ARG PRO ASN
SEQRES 28 E 489 SER ILE ASP PRO ALA LEU ARG ARG PHE GLY ARG PHE ASP
SEQRES 29 E 489 ARG GLU VAL ASP ILE GLY ILE PRO ASP ALA THR GLY ARG
SEQRES 30 E 489 LEU GLU ILE LEU GLN ILE HIS THR LYS ASN MET LYS LEU
SEQRES 31 E 489 ALA ASP ASP VAL ASP LEU GLU GLN VAL ALA ASN GLU THR
SEQRES 32 E 489 HIS GLY HIS VAL GLY ALA ASP LEU ALA ALA LEU CYS SER
SEQRES 33 E 489 GLU ALA ALA LEU GLN ALA ILE ARG LYS LYS MET ASP LEU
SEQRES 34 E 489 ILE ASP LEU GLU ASP GLU THR ILE ASP ALA GLU VAL MET
SEQRES 35 E 489 ASN SER LEU ALA VAL THR MET ASP ASP PHE ARG TRP ALA
SEQRES 36 E 489 LEU SER GLN SER ASN PRO SER ALA LEU ARG GLU THR VAL
SEQRES 37 E 489 VAL GLU VAL PRO GLN VAL THR TRP GLU ASP ILE GLY GLY
SEQRES 38 E 489 ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 F 489 MET ALA SER GLY ALA ASP SER LYS GLY ASP ASP LEU SER
SEQRES 2 F 489 THR ALA ILE LEU LYS GLN LYS ASN ARG PRO ASN ARG LEU
SEQRES 3 F 489 ILE VAL ASP GLU ALA ILE ASN GLU ASP ASN SER VAL VAL
SEQRES 4 F 489 SER LEU SER GLN PRO LYS MET ASP GLU LEU GLN LEU PHE
SEQRES 5 F 489 ARG GLY ASP THR VAL LEU LEU LYS GLY LYS LYS ARG ARG
SEQRES 6 F 489 GLU ALA VAL CYS ILE VAL LEU SER ASP ASP THR CYS SER
SEQRES 7 F 489 ASP GLU LYS ILE ARG MET ASN ALA VAL VAL ARG ASN ASN
SEQRES 8 F 489 LEU ARG VAL ARG LEU GLY ASP VAL ILE SER ILE GLN PRO
SEQRES 9 F 489 CYS PRO ASP VAL LYS TYR GLY LYS ARG ILE HIS VAL LEU
SEQRES 10 F 489 PRO ILE ASP ASP THR VAL GLU GLY ILE THR GLY ASN LEU
SEQRES 11 F 489 PHE GLU VAL TYR LEU LYS PRO TYR PHE LEU GLU ALA TYR
SEQRES 12 F 489 ARG PRO ILE ARG LYS GLY ASP ILE PHE LEU VAL ARG GLY
SEQRES 13 F 489 GLY MET ARG ALA VAL GLU PHE LYS VAL VAL GLU THR ASP
SEQRES 14 F 489 PRO SER PRO TYR CYS ILE VAL ALA PRO ASP THR VAL ILE
SEQRES 15 F 489 HIS CYS GLU GLY GLU PRO ILE LYS ARG GLU ASP GLU GLU
SEQRES 16 F 489 GLU SER LEU ASN GLU VAL GLY TYR ASP ASP ILE GLY GLY
SEQRES 17 F 489 CYS ARG LYS GLN LEU ALA GLN ILE LYS GLU MET VAL GLU
SEQRES 18 F 489 LEU PRO LEU ARG HIS PRO ALA LEU PHE LYS ALA ILE GLY
SEQRES 19 F 489 VAL LYS PRO PRO ARG GLY ILE LEU LEU TYR GLY PRO PRO
SEQRES 20 F 489 GLY THR GLY LYS THR LEU ILE ALA ARG ALA VAL ALA ASN
SEQRES 21 F 489 GLU THR GLY ALA PHE PHE PHE LEU ILE ASN GLY PRO GLU
SEQRES 22 F 489 ILE MET SER LYS LEU ALA GLY GLU SER GLU SER ASN LEU
SEQRES 23 F 489 ARG LYS ALA PHE GLU GLU ALA GLU LYS ASN ALA PRO ALA
SEQRES 24 F 489 ILE ILE PHE ILE ASP GLU LEU ASP ALA ILE ALA PRO LYS
SEQRES 25 F 489 ARG GLU LYS THR HIS GLY GLU VAL GLU ARG ARG ILE VAL
SEQRES 26 F 489 SER GLN LEU LEU THR LEU MET ASP GLY LEU LYS GLN ARG
SEQRES 27 F 489 ALA HIS VAL ILE VAL MET ALA ALA THR ASN ARG PRO ASN
SEQRES 28 F 489 SER ILE ASP PRO ALA LEU ARG ARG PHE GLY ARG PHE ASP
SEQRES 29 F 489 ARG GLU VAL ASP ILE GLY ILE PRO ASP ALA THR GLY ARG
SEQRES 30 F 489 LEU GLU ILE LEU GLN ILE HIS THR LYS ASN MET LYS LEU
SEQRES 31 F 489 ALA ASP ASP VAL ASP LEU GLU GLN VAL ALA ASN GLU THR
SEQRES 32 F 489 HIS GLY HIS VAL GLY ALA ASP LEU ALA ALA LEU CYS SER
SEQRES 33 F 489 GLU ALA ALA LEU GLN ALA ILE ARG LYS LYS MET ASP LEU
SEQRES 34 F 489 ILE ASP LEU GLU ASP GLU THR ILE ASP ALA GLU VAL MET
SEQRES 35 F 489 ASN SER LEU ALA VAL THR MET ASP ASP PHE ARG TRP ALA
SEQRES 36 F 489 LEU SER GLN SER ASN PRO SER ALA LEU ARG GLU THR VAL
SEQRES 37 F 489 VAL GLU VAL PRO GLN VAL THR TRP GLU ASP ILE GLY GLY
SEQRES 38 F 489 ARG SER HIS HIS HIS HIS HIS HIS
HET AGS A 800 31
HET MG A 801 1
HET AGS B 800 31
HET MG B 801 1
HET AGS C 800 31
HET MG C 801 1
HET AGS D 800 31
HET MG D 801 1
HET AGS E 800 31
HET MG E 801 1
HET AGS F 800 31
HET MG F 801 1
HETNAM AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETSYN AGS ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE);
HETSYN 2 AGS ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-
HETSYN 3 AGS DIPHOSPHATE MONOTHIOPHOSPHATE
FORMUL 7 AGS 6(C10 H16 N5 O12 P3 S)
FORMUL 8 MG 6(MG 2+)
FORMUL 19 HOH *93(H2 O)
HELIX 1 1 SER A 13 LYS A 18 5 6
HELIX 2 2 SER A 42 LEU A 49 1 8
HELIX 3 3 ASN A 85 LEU A 92 1 8
HELIX 4 4 ASP A 120 VAL A 123 5 4
HELIX 5 5 ASN A 129 TYR A 134 1 6
HELIX 6 6 TYR A 134 LEU A 140 1 7
HELIX 7 7 LYS A 190 ASN A 199 1 10
HELIX 8 8 GLY A 202 ILE A 206 5 5
HELIX 9 9 CYS A 209 VAL A 220 1 12
HELIX 10 10 VAL A 220 HIS A 226 1 7
HELIX 11 11 HIS A 226 GLY A 234 1 9
HELIX 12 12 GLY A 250 THR A 262 1 13
HELIX 13 13 GLY A 271 SER A 276 1 6
HELIX 14 14 GLY A 280 ASN A 296 1 17
HELIX 15 15 GLU A 305 ALA A 310 1 6
HELIX 16 16 GLY A 318 LEU A 335 1 18
HELIX 17 17 LYS A 336 ALA A 339 5 4
HELIX 18 18 ARG A 349 ILE A 353 5 5
HELIX 19 19 ASP A 354 ARG A 359 5 6
HELIX 20 20 ASP A 373 THR A 385 1 13
HELIX 21 21 ASP A 395 THR A 403 1 9
HELIX 22 22 VAL A 407 LYS A 426 1 20
HELIX 23 23 ASP A 438 LEU A 445 1 8
HELIX 24 24 THR A 448 SER A 459 1 12
HELIX 25 25 SER B 13 LYS B 18 5 6
HELIX 26 26 SER B 42 LEU B 49 1 8
HELIX 27 27 ASN B 85 LEU B 92 1 8
HELIX 28 28 ASP B 120 VAL B 123 5 4
HELIX 29 29 ASN B 129 TYR B 134 1 6
HELIX 30 30 TYR B 134 LEU B 140 1 7
HELIX 31 31 LYS B 190 ASN B 199 1 10
HELIX 32 32 GLY B 202 ILE B 206 5 5
HELIX 33 33 CYS B 209 VAL B 220 1 12
HELIX 34 34 VAL B 220 HIS B 226 1 7
HELIX 35 35 HIS B 226 GLY B 234 1 9
HELIX 36 36 GLY B 250 THR B 262 1 13
HELIX 37 37 GLY B 271 SER B 276 1 6
HELIX 38 38 SER B 282 ASN B 296 1 15
HELIX 39 39 GLU B 305 ALA B 310 1 6
HELIX 40 40 GLY B 318 LEU B 335 1 18
HELIX 41 41 LYS B 336 ALA B 339 5 4
HELIX 42 42 ARG B 349 ILE B 353 5 5
HELIX 43 43 ASP B 354 ARG B 359 5 6
HELIX 44 44 ASP B 373 THR B 385 1 13
HELIX 45 45 ASP B 395 THR B 403 1 9
HELIX 46 46 VAL B 407 LYS B 426 1 20
HELIX 47 47 ASP B 438 LEU B 445 1 8
HELIX 48 48 THR B 448 SER B 459 1 12
HELIX 49 49 SER C 13 LYS C 18 5 6
HELIX 50 50 SER C 42 LEU C 49 1 8
HELIX 51 51 ASN C 85 LEU C 92 1 8
HELIX 52 52 ASP C 120 VAL C 123 5 4
HELIX 53 53 ASN C 129 TYR C 134 1 6
HELIX 54 54 TYR C 134 LEU C 140 1 7
HELIX 55 55 LYS C 190 ASN C 199 1 10
HELIX 56 56 GLY C 202 ILE C 206 5 5
HELIX 57 57 CYS C 209 VAL C 220 1 12
HELIX 58 58 VAL C 220 HIS C 226 1 7
HELIX 59 59 HIS C 226 GLY C 234 1 9
HELIX 60 60 GLY C 250 THR C 262 1 13
HELIX 61 61 GLY C 271 SER C 276 1 6
HELIX 62 62 GLY C 280 ASN C 296 1 17
HELIX 63 63 LEU C 306 ILE C 309 5 4
HELIX 64 64 GLY C 318 LEU C 335 1 18
HELIX 65 65 LYS C 336 ALA C 339 5 4
HELIX 66 66 ARG C 349 ILE C 353 5 5
HELIX 67 67 ASP C 354 ARG C 359 5 6
HELIX 68 68 ASP C 373 THR C 385 1 13
HELIX 69 69 ASP C 395 THR C 403 1 9
HELIX 70 70 VAL C 407 LYS C 426 1 20
HELIX 71 71 ASP C 438 LEU C 445 1 8
HELIX 72 72 THR C 448 SER C 459 1 12
HELIX 73 73 SER D 13 LYS D 18 5 6
HELIX 74 74 SER D 42 LEU D 49 1 8
HELIX 75 75 ASN D 85 ARG D 93 1 9
HELIX 76 76 ASP D 120 VAL D 123 5 4
HELIX 77 77 ASN D 129 TYR D 134 1 6
HELIX 78 78 TYR D 134 LEU D 140 1 7
HELIX 79 79 LYS D 190 ASN D 199 1 10
HELIX 80 80 GLY D 202 ILE D 206 5 5
HELIX 81 81 CYS D 209 VAL D 220 1 12
HELIX 82 82 VAL D 220 HIS D 226 1 7
HELIX 83 83 PRO D 227 GLY D 234 1 8
HELIX 84 84 GLY D 250 THR D 262 1 13
HELIX 85 85 GLY D 271 SER D 276 1 6
HELIX 86 86 GLY D 280 ASN D 296 1 17
HELIX 87 87 GLU D 305 ALA D 310 1 6
HELIX 88 88 GLY D 318 LEU D 335 1 18
HELIX 89 89 LYS D 336 ALA D 339 5 4
HELIX 90 90 ARG D 349 ILE D 353 5 5
HELIX 91 91 ASP D 354 ARG D 359 5 6
HELIX 92 92 ASP D 373 THR D 385 1 13
HELIX 93 93 ASP D 395 GLU D 402 1 8
HELIX 94 94 VAL D 407 LYS D 426 1 20
HELIX 95 95 ASP D 438 SER D 444 1 7
HELIX 96 96 THR D 448 SER D 459 1 12
HELIX 97 97 SER E 13 LYS E 18 5 6
HELIX 98 98 SER E 42 LEU E 49 1 8
HELIX 99 99 ASN E 85 LEU E 92 1 8
HELIX 100 100 ASP E 120 VAL E 123 5 4
HELIX 101 101 ASN E 129 TYR E 134 1 6
HELIX 102 102 TYR E 134 LEU E 140 1 7
HELIX 103 103 LYS E 190 ASN E 199 1 10
HELIX 104 104 GLY E 202 ILE E 206 5 5
HELIX 105 105 CYS E 209 VAL E 220 1 12
HELIX 106 106 VAL E 220 HIS E 226 1 7
HELIX 107 107 PRO E 227 GLY E 234 1 8
HELIX 108 108 GLY E 250 THR E 262 1 13
HELIX 109 109 GLY E 271 SER E 276 1 6
HELIX 110 110 SER E 282 ASN E 296 1 15
HELIX 111 111 GLU E 305 ILE E 309 5 5
HELIX 112 112 GLY E 318 LEU E 335 1 18
HELIX 113 113 LYS E 336 ALA E 339 5 4
HELIX 114 114 ARG E 349 ILE E 353 5 5
HELIX 115 115 ASP E 354 ARG E 359 5 6
HELIX 116 116 ASP E 373 THR E 385 1 13
HELIX 117 117 ASP E 395 THR E 403 1 9
HELIX 118 118 VAL E 407 LYS E 426 1 20
HELIX 119 119 ASP E 438 LEU E 445 1 8
HELIX 120 120 THR E 448 SER E 459 1 12
HELIX 121 121 SER F 13 LYS F 18 5 6
HELIX 122 122 SER F 42 GLN F 50 1 9
HELIX 123 123 ASN F 85 LEU F 92 1 8
HELIX 124 124 ASP F 120 VAL F 123 5 4
HELIX 125 125 ASN F 129 TYR F 134 1 6
HELIX 126 126 TYR F 134 LEU F 140 1 7
HELIX 127 127 LYS F 190 ASN F 199 1 10
HELIX 128 128 GLY F 202 ILE F 206 5 5
HELIX 129 129 CYS F 209 VAL F 220 1 12
HELIX 130 130 VAL F 220 HIS F 226 1 7
HELIX 131 131 HIS F 226 GLY F 234 1 9
HELIX 132 132 GLY F 250 THR F 262 1 13
HELIX 133 133 GLY F 271 SER F 276 1 6
HELIX 134 134 GLY F 280 ASN F 296 1 17
HELIX 135 135 GLU F 305 ALA F 310 1 6
HELIX 136 136 GLY F 318 LEU F 335 1 18
HELIX 137 137 LYS F 336 ALA F 339 5 4
HELIX 138 138 ARG F 349 ILE F 353 5 5
HELIX 139 139 ASP F 354 ARG F 359 5 6
HELIX 140 140 ASP F 373 THR F 385 1 13
HELIX 141 141 ASP F 395 THR F 403 1 9
HELIX 142 142 VAL F 407 LYS F 426 1 20
HELIX 143 143 ASP F 438 SER F 444 1 7
HELIX 144 144 THR F 448 SER F 459 1 12
SHEET 1 A 7 ARG A 25 ASP A 29 0
SHEET 2 A 7 LYS A 81 ARG A 83 1 O ILE A 82 N ASP A 29
SHEET 3 A 7 VAL A 38 LEU A 41 -1 N SER A 40 O ARG A 83
SHEET 4 A 7 GLU A 66 SER A 73 1 O ILE A 70 N VAL A 39
SHEET 5 A 7 THR A 56 LYS A 60 -1 N VAL A 57 O CYS A 69
SHEET 6 A 7 VAL A 99 PRO A 104 -1 O GLN A 103 N LEU A 58
SHEET 7 A 7 ARG A 25 ASP A 29 -1 N LEU A 26 O ILE A 100
SHEET 1 B 5 ARG A 144 ARG A 147 0
SHEET 2 B 5 TYR A 173 HIS A 183 -1 O VAL A 176 N ARG A 144
SHEET 3 B 5 TYR A 110 PRO A 118 1 N ILE A 114 O HIS A 183
SHEET 4 B 5 ARG A 159 GLU A 167 -1 O LYS A 164 N LEU A 117
SHEET 5 B 5 ILE A 151 GLY A 156 -1 N PHE A 152 O PHE A 163
SHEET 1 C 5 PHE A 265 ASN A 270 0
SHEET 2 C 5 ALA A 299 ASP A 304 1 O PHE A 302 N ILE A 269
SHEET 3 C 5 VAL A 341 THR A 347 1 O MET A 344 N ILE A 301
SHEET 4 C 5 GLY A 240 TYR A 244 1 N LEU A 243 O ALA A 345
SHEET 5 C 5 ARG A 365 ASP A 368 1 O ARG A 365 N LEU A 242
SHEET 1 D 7 ARG B 25 ASP B 29 0
SHEET 2 D 7 LYS B 81 ARG B 83 1 O ILE B 82 N ASP B 29
SHEET 3 D 7 VAL B 38 LEU B 41 -1 N SER B 40 O ARG B 83
SHEET 4 D 7 GLU B 66 SER B 73 1 O ILE B 70 N VAL B 39
SHEET 5 D 7 THR B 56 LYS B 60 -1 N VAL B 57 O CYS B 69
SHEET 6 D 7 VAL B 99 PRO B 104 -1 O GLN B 103 N LEU B 58
SHEET 7 D 7 ARG B 25 ASP B 29 -1 N LEU B 26 O ILE B 100
SHEET 1 E 5 ARG B 144 ARG B 147 0
SHEET 2 E 5 TYR B 173 HIS B 183 -1 O VAL B 176 N ARG B 144
SHEET 3 E 5 TYR B 110 PRO B 118 1 N GLY B 111 O ILE B 175
SHEET 4 E 5 ARG B 159 GLU B 167 -1 O LYS B 164 N LEU B 117
SHEET 5 E 5 ILE B 151 GLY B 156 -1 N VAL B 154 O VAL B 161
SHEET 1 F 5 PHE B 265 ASN B 270 0
SHEET 2 F 5 ALA B 299 ASP B 304 1 O PHE B 302 N PHE B 267
SHEET 3 F 5 VAL B 341 THR B 347 1 O MET B 344 N ILE B 301
SHEET 4 F 5 GLY B 240 TYR B 244 1 N LEU B 243 O ALA B 345
SHEET 5 F 5 ARG B 365 ASP B 368 1 O ARG B 365 N LEU B 242
SHEET 1 G 7 ARG C 25 ASP C 29 0
SHEET 2 G 7 LYS C 81 ARG C 83 1 O ILE C 82 N ASP C 29
SHEET 3 G 7 VAL C 38 LEU C 41 -1 N SER C 40 O ARG C 83
SHEET 4 G 7 GLU C 66 SER C 73 1 O ILE C 70 N VAL C 39
SHEET 5 G 7 THR C 56 LYS C 60 -1 N VAL C 57 O CYS C 69
SHEET 6 G 7 VAL C 99 PRO C 104 -1 O GLN C 103 N LEU C 58
SHEET 7 G 7 ARG C 25 ASP C 29 -1 N LEU C 26 O ILE C 100
SHEET 1 H 5 ARG C 144 ARG C 147 0
SHEET 2 H 5 TYR C 173 HIS C 183 -1 O VAL C 176 N ARG C 144
SHEET 3 H 5 TYR C 110 PRO C 118 1 N ILE C 114 O HIS C 183
SHEET 4 H 5 ARG C 159 THR C 168 -1 O LYS C 164 N LEU C 117
SHEET 5 H 5 ILE C 151 GLY C 156 -1 N PHE C 152 O PHE C 163
SHEET 1 I 5 PHE C 265 ASN C 270 0
SHEET 2 I 5 ALA C 299 ASP C 304 1 O ILE C 300 N PHE C 267
SHEET 3 I 5 VAL C 341 ALA C 346 1 O MET C 344 N ILE C 301
SHEET 4 I 5 GLY C 240 TYR C 244 1 N LEU C 243 O ALA C 345
SHEET 5 I 5 ARG C 365 ASP C 368 1 O VAL C 367 N LEU C 242
SHEET 1 J 7 ARG D 25 ASP D 29 0
SHEET 2 J 7 LYS D 81 ARG D 83 1 O ILE D 82 N ASP D 29
SHEET 3 J 7 VAL D 38 LEU D 41 -1 N SER D 40 O ARG D 83
SHEET 4 J 7 GLU D 66 SER D 73 1 O ILE D 70 N VAL D 39
SHEET 5 J 7 THR D 56 LYS D 60 -1 N VAL D 57 O CYS D 69
SHEET 6 J 7 VAL D 99 PRO D 104 -1 O GLN D 103 N LEU D 58
SHEET 7 J 7 ARG D 25 ASP D 29 -1 N LEU D 26 O ILE D 100
SHEET 1 K 5 ARG D 144 ARG D 147 0
SHEET 2 K 5 TYR D 173 HIS D 183 -1 O VAL D 176 N ARG D 144
SHEET 3 K 5 TYR D 110 PRO D 118 1 N ILE D 114 O HIS D 183
SHEET 4 K 5 ARG D 159 GLU D 167 -1 O LYS D 164 N LEU D 117
SHEET 5 K 5 ILE D 151 GLY D 156 -1 N PHE D 152 O PHE D 163
SHEET 1 L 5 PHE D 265 ASN D 270 0
SHEET 2 L 5 ALA D 299 ASP D 304 1 O ILE D 300 N PHE D 265
SHEET 3 L 5 VAL D 341 THR D 347 1 O MET D 344 N ILE D 301
SHEET 4 L 5 GLY D 240 TYR D 244 1 N LEU D 243 O ALA D 345
SHEET 5 L 5 ARG D 365 ASP D 368 1 O VAL D 367 N LEU D 242
SHEET 1 M 7 ARG E 25 ASP E 29 0
SHEET 2 M 7 LYS E 81 ARG E 83 1 O ILE E 82 N ASP E 29
SHEET 3 M 7 VAL E 38 LEU E 41 -1 N SER E 40 O ARG E 83
SHEET 4 M 7 GLU E 66 SER E 73 1 O ILE E 70 N VAL E 39
SHEET 5 M 7 THR E 56 LYS E 60 -1 N VAL E 57 O CYS E 69
SHEET 6 M 7 VAL E 99 PRO E 104 -1 O GLN E 103 N LEU E 58
SHEET 7 M 7 ARG E 25 ASP E 29 -1 N LEU E 26 O ILE E 100
SHEET 1 N 5 ARG E 144 ARG E 147 0
SHEET 2 N 5 TYR E 173 HIS E 183 -1 O VAL E 176 N ARG E 144
SHEET 3 N 5 TYR E 110 PRO E 118 1 N ILE E 114 O VAL E 181
SHEET 4 N 5 ARG E 159 GLU E 167 -1 O LYS E 164 N LEU E 117
SHEET 5 N 5 ILE E 151 GLY E 156 -1 N VAL E 154 O VAL E 161
SHEET 1 O 5 PHE E 265 ASN E 270 0
SHEET 2 O 5 ALA E 299 ASP E 304 1 O PHE E 302 N PHE E 267
SHEET 3 O 5 VAL E 341 THR E 347 1 O MET E 344 N ILE E 301
SHEET 4 O 5 GLY E 240 TYR E 244 1 N LEU E 243 O ALA E 345
SHEET 5 O 5 ARG E 365 ASP E 368 1 O VAL E 367 N LEU E 242
SHEET 1 P 7 ARG F 25 ASP F 29 0
SHEET 2 P 7 LYS F 81 ARG F 83 1 O ILE F 82 N ASP F 29
SHEET 3 P 7 VAL F 38 LEU F 41 -1 N SER F 40 O ARG F 83
SHEET 4 P 7 GLU F 66 SER F 73 1 O ILE F 70 N VAL F 39
SHEET 5 P 7 THR F 56 LYS F 60 -1 N VAL F 57 O CYS F 69
SHEET 6 P 7 VAL F 99 PRO F 104 -1 O GLN F 103 N LEU F 58
SHEET 7 P 7 ARG F 25 ASP F 29 -1 N LEU F 26 O ILE F 100
SHEET 1 Q 4 ILE F 151 GLY F 156 0
SHEET 2 Q 4 ARG F 159 GLU F 167 -1 O PHE F 163 N PHE F 152
SHEET 3 Q 4 ARG F 113 PRO F 118 -1 N LEU F 117 O LYS F 164
SHEET 4 Q 4 VAL F 181 HIS F 183 1 O VAL F 181 N ILE F 114
SHEET 1 R 2 ARG F 144 ARG F 147 0
SHEET 2 R 2 TYR F 173 VAL F 176 -1 O VAL F 176 N ARG F 144
SHEET 1 S 5 PHE F 265 ASN F 270 0
SHEET 2 S 5 ALA F 299 ASP F 304 1 O PHE F 302 N PHE F 267
SHEET 3 S 5 VAL F 341 THR F 347 1 O MET F 344 N ILE F 301
SHEET 4 S 5 GLY F 240 TYR F 244 1 N LEU F 243 O ALA F 345
SHEET 5 S 5 ARG F 365 ASP F 368 1 O VAL F 367 N LEU F 242
LINK OG1 THR A 252 MG MG A 801 1555 1555 2.20
LINK O2G AGS A 800 MG MG A 801 1555 1555 1.81
LINK O1B AGS A 800 MG MG A 801 1555 1555 1.86
LINK MG MG A 801 O HOH A 802 1555 1555 1.95
LINK MG MG A 801 O HOH A 803 1555 1555 2.16
LINK MG MG A 801 O HOH A 804 1555 1555 1.92
LINK OG1 THR B 252 MG MG B 801 1555 1555 2.28
LINK O2G AGS B 800 MG MG B 801 1555 1555 1.77
LINK O1B AGS B 800 MG MG B 801 1555 1555 2.03
LINK MG MG B 801 O HOH B 802 1555 1555 2.01
LINK MG MG B 801 O HOH B 803 1555 1555 2.11
LINK MG MG B 801 O HOH B 804 1555 1555 2.04
LINK OG1 THR C 252 MG MG C 801 1555 1555 2.14
LINK O1B AGS C 800 MG MG C 801 1555 1555 2.23
LINK MG MG C 801 O HOH C 802 1555 1555 2.13
LINK MG MG C 801 O HOH C 803 1555 1555 2.56
LINK MG MG C 801 O HOH C 804 1555 1555 2.09
LINK OG1 THR D 252 MG MG D 801 1555 1555 2.23
LINK O1B AGS D 800 MG MG D 801 1555 1555 1.91
LINK MG MG D 801 O HOH D 803 1555 1555 2.06
LINK MG MG D 801 O HOH D 804 1555 1555 2.00
LINK OG1 THR E 252 MG MG E 801 1555 1555 2.19
LINK O2G AGS E 800 MG MG E 801 1555 1555 1.76
LINK O1B AGS E 800 MG MG E 801 1555 1555 1.93
LINK MG MG E 801 O HOH E 802 1555 1555 2.14
LINK MG MG E 801 O HOH E 803 1555 1555 2.06
LINK MG MG E 801 O HOH E 804 1555 1555 2.02
LINK OG1 THR F 252 MG MG F 801 1555 1555 2.17
LINK O1B AGS F 800 MG MG F 801 1555 1555 1.89
LINK MG MG F 801 O HOH F 802 1555 1555 2.47
LINK MG MG F 801 O HOH F 803 1555 1555 2.32
LINK MG MG F 801 O HOH F 804 1555 1555 1.99
SITE 1 AC1 21 ASP A 205 ILE A 206 GLY A 207 PRO A 247
SITE 2 AC1 21 GLY A 248 THR A 249 GLY A 250 LYS A 251
SITE 3 AC1 21 THR A 252 LEU A 253 ASN A 348 ILE A 380
SITE 4 AC1 21 HIS A 384 GLY A 408 ALA A 409 MG A 801
SITE 5 AC1 21 HOH A 802 HOH A 803 HOH A 804 ARG B 359
SITE 6 AC1 21 PHE B 360
SITE 1 AC2 5 THR A 252 AGS A 800 HOH A 802 HOH A 803
SITE 2 AC2 5 HOH A 804
SITE 1 AC3 21 ASP B 205 ILE B 206 GLY B 207 PRO B 247
SITE 2 AC3 21 GLY B 248 THR B 249 GLY B 250 LYS B 251
SITE 3 AC3 21 THR B 252 LEU B 253 ASN B 348 ILE B 380
SITE 4 AC3 21 HIS B 384 GLY B 408 ALA B 409 MG B 801
SITE 5 AC3 21 HOH B 802 HOH B 803 HOH B 804 ARG C 359
SITE 6 AC3 21 PHE C 360
SITE 1 AC4 5 THR B 252 AGS B 800 HOH B 802 HOH B 803
SITE 2 AC4 5 HOH B 804
SITE 1 AC5 20 ASP C 205 ILE C 206 GLY C 207 PRO C 247
SITE 2 AC5 20 GLY C 248 THR C 249 GLY C 250 LYS C 251
SITE 3 AC5 20 THR C 252 LEU C 253 ASN C 348 ILE C 380
SITE 4 AC5 20 HIS C 384 GLY C 408 ALA C 409 MG C 801
SITE 5 AC5 20 HOH C 802 HOH C 804 ARG D 359 PHE D 360
SITE 1 AC6 5 THR C 252 AGS C 800 HOH C 802 HOH C 803
SITE 2 AC6 5 HOH C 804
SITE 1 AC7 20 ASP D 205 ILE D 206 GLY D 207 PRO D 247
SITE 2 AC7 20 GLY D 248 THR D 249 GLY D 250 LYS D 251
SITE 3 AC7 20 THR D 252 LEU D 253 ASN D 348 ILE D 380
SITE 4 AC7 20 HIS D 384 GLY D 408 ALA D 409 MG D 801
SITE 5 AC7 20 HOH D 803 HOH D 804 ARG E 359 PHE E 360
SITE 1 AC8 4 THR D 252 AGS D 800 HOH D 803 HOH D 804
SITE 1 AC9 21 ASP E 205 ILE E 206 GLY E 207 PRO E 247
SITE 2 AC9 21 GLY E 248 THR E 249 GLY E 250 LYS E 251
SITE 3 AC9 21 THR E 252 LEU E 253 ASN E 348 ILE E 380
SITE 4 AC9 21 HIS E 384 GLY E 408 ALA E 409 MG E 801
SITE 5 AC9 21 HOH E 802 HOH E 803 HOH E 804 ARG F 359
SITE 6 AC9 21 PHE F 360
SITE 1 BC1 5 THR E 252 AGS E 800 HOH E 802 HOH E 803
SITE 2 BC1 5 HOH E 804
SITE 1 BC2 20 ARG A 359 PHE A 360 ASP F 205 ILE F 206
SITE 2 BC2 20 GLY F 207 PRO F 247 GLY F 248 THR F 249
SITE 3 BC2 20 GLY F 250 LYS F 251 THR F 252 LEU F 253
SITE 4 BC2 20 ASN F 348 ILE F 380 HIS F 384 GLY F 408
SITE 5 BC2 20 ALA F 409 MG F 801 HOH F 802 HOH F 804
SITE 1 BC3 5 THR F 252 AGS F 800 HOH F 802 HOH F 803
SITE 2 BC3 5 HOH F 804
CRYST1 90.892 102.645 107.182 97.52 90.63 91.45 P 1 6
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 0.011002 0.000278 0.000159 0.00000
SCALE2 0.000000 0.009745 0.001290 0.00000
SCALE3 0.000000 0.000000 0.009412 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
