HEADER TRANSFERASE 20-JAN-05 1YM7
TITLE G PROTEIN-COUPLED RECEPTOR KINASE 2 (GRK2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-ADRENERGIC RECEPTOR KINASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: BETA-ARK-1, G- PROTEIN COUPLED RECEPTOR KINASE 2;
COMPND 5 EC: 2.7.1.126;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: ADRBK1, GRK2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS G PROTEIN, KINASE, GPCR, GRK2, BETA-ARK1, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.T.LODOWSKI,J.F.BARNHILL,R.M.PYSKADLO,R.GHIRLANDO,R.STERNE-MARR,
AUTHOR 2 J.J.G.TESMER
REVDAT 5 23-AUG-23 1YM7 1 REMARK
REVDAT 4 20-OCT-21 1YM7 1 SEQADV
REVDAT 3 13-JUL-11 1YM7 1 VERSN
REVDAT 2 24-FEB-09 1YM7 1 VERSN
REVDAT 1 05-JUL-05 1YM7 0
JRNL AUTH D.T.LODOWSKI,J.F.BARNHILL,R.M.PYSKADLO,R.GHIRLANDO,
JRNL AUTH 2 R.STERNE-MARR,J.J.G.TESMER
JRNL TITL THE ROLE OF GBETAGAMMA AND DOMAIN INTERFACES IN THE
JRNL TITL 2 ACTIVATION OF G PROTEIN-COUPLED RECEPTOR KINASE 2
JRNL REF BIOCHEMISTRY V. 44 6958 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15865441
JRNL DOI 10.1021/BI050119Q
REMARK 2
REMARK 2 RESOLUTION. 4.50 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) : 4.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22700
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1197
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) : 4.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1580
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.4230
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.4810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19846
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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) : 40.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.45000
REMARK 3 B22 (A**2) : -2.33000
REMARK 3 B33 (A**2) : 0.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.90000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 1.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 1.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 218.079
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20365 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27358 ; 1.881 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2419 ; 8.329 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1008 ;39.208 ;23.730
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3879 ;24.176 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 152 ;16.854 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2882 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15328 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 8477 ; 0.294 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 12726 ; 0.329 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 763 ; 0.210 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 46 ; 0.360 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 12643 ; 0.000 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19491 ; 0.000 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8993 ; 0.000 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7867 ; 0.000 ; 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 : 6
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 29 A 184 1
REMARK 3 2 B 29 B 184 1
REMARK 3 3 C 29 C 184 1
REMARK 3 4 D 29 D 184 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1316 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1316 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1316 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1316 ; .06 ; .05
REMARK 3 TIGHT THERMAL 1 A (A**2): 1316 ; .00 ; .50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1316 ; .00 ; .50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1316 ; .00 ; .50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1316 ; .00 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 5 A 185 A 475 1
REMARK 3 6 B 185 B 475 1
REMARK 3 7 C 185 C 475 1
REMARK 3 8 D 185 D 475 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 2321 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 B (A): 2321 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 C (A): 2321 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 D (A): 2321 ; .06 ; .05
REMARK 3 TIGHT THERMAL 2 A (A**2): 2321 ; .00 ; .50
REMARK 3 TIGHT THERMAL 2 B (A**2): 2321 ; .00 ; .50
REMARK 3 TIGHT THERMAL 2 C (A**2): 2321 ; .00 ; .50
REMARK 3 TIGHT THERMAL 2 D (A**2): 2321 ; .00 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 9 A 494 A 512 1
REMARK 3 10 B 494 B 512 1
REMARK 3 11 C 494 C 512 1
REMARK 3 12 D 494 D 512 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 B (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 C (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 D (A): 158 ; .06 ; .05
REMARK 3 TIGHT THERMAL 3 A (A**2): 158 ; .00 ; .50
REMARK 3 TIGHT THERMAL 3 B (A**2): 158 ; .00 ; .50
REMARK 3 TIGHT THERMAL 3 C (A**2): 158 ; .00 ; .50
REMARK 3 TIGHT THERMAL 3 D (A**2): 158 ; .00 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 16
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 13 A 513 A 537 1
REMARK 3 14 B 513 B 537 1
REMARK 3 15 C 513 C 537 1
REMARK 3 16 D 513 D 537 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 209 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 B (A): 209 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 C (A): 209 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 D (A): 209 ; .06 ; .05
REMARK 3 TIGHT THERMAL 4 A (A**2): 209 ; .00 ; .50
REMARK 3 TIGHT THERMAL 4 B (A**2): 209 ; .00 ; .50
REMARK 3 TIGHT THERMAL 4 C (A**2): 209 ; .00 ; .50
REMARK 3 TIGHT THERMAL 4 D (A**2): 209 ; .00 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 18
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 17 A 538 A 555 1
REMARK 3 18 B 538 B 555 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 149 ; .07 ; .05
REMARK 3 TIGHT THERMAL 5 A (A**2): 149 ; .00 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 22
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 19 A 556 A 656 1
REMARK 3 20 B 556 B 656 1
REMARK 3 21 C 556 C 656 1
REMARK 3 22 D 556 D 656 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 A (A): 822 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 B (A): 822 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 6 C (A): 822 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 6 D (A): 822 ; .05 ; .05
REMARK 3 TIGHT THERMAL 6 A (A**2): 822 ; .00 ; .50
REMARK 3 TIGHT THERMAL 6 B (A**2): 822 ; .00 ; .50
REMARK 3 TIGHT THERMAL 6 C (A**2): 822 ; .00 ; .50
REMARK 3 TIGHT THERMAL 6 D (A**2): 822 ; .00 ; .50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 185 A 513
REMARK 3 ORIGIN FOR THE GROUP (A): 83.0030 -48.0280 15.5270
REMARK 3 T TENSOR
REMARK 3 T11: -.6921 T22: -.2750
REMARK 3 T33: -.6217 T12: -.1406
REMARK 3 T13: -.5256 T23: -.1457
REMARK 3 L TENSOR
REMARK 3 L11: 6.1018 L22: 8.6158
REMARK 3 L33: 5.5113 L12: -1.8488
REMARK 3 L13: .1124 L23: 2.1886
REMARK 3 S TENSOR
REMARK 3 S11: -.2562 S12: .1963 S13: -.8706
REMARK 3 S21: .1936 S22: .3608 S23: .7418
REMARK 3 S31: .4945 S32: -.5679 S33: -.1046
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 : B 185 B 513
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4820 16.0660 15.2800
REMARK 3 T TENSOR
REMARK 3 T11: -1.1342 T22: -.6552
REMARK 3 T33: -.7887 T12: .0653
REMARK 3 T13: -.0755 T23: .2137
REMARK 3 L TENSOR
REMARK 3 L11: 6.2796 L22: 9.6781
REMARK 3 L33: 6.4703 L12: -3.1751
REMARK 3 L13: -1.2945 L23: .1138
REMARK 3 S TENSOR
REMARK 3 S11: -.1829 S12: .6360 S13: 1.0591
REMARK 3 S21: .0861 S22: .5639 S23: -.1503
REMARK 3 S31: -.7826 S32: .1669 S33: -.3810
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 : C 185 C 513
REMARK 3 ORIGIN FOR THE GROUP (A): 146.4600 -73.4440 76.5930
REMARK 3 T TENSOR
REMARK 3 T11: -1.1185 T22: -.1370
REMARK 3 T33: -.5216 T12: .0283
REMARK 3 T13: -.3167 T23: .1235
REMARK 3 L TENSOR
REMARK 3 L11: 4.7244 L22: 7.1287
REMARK 3 L33: 15.7825 L12: -1.3973
REMARK 3 L13: -1.9037 L23: 5.1039
REMARK 3 S TENSOR
REMARK 3 S11: -.4504 S12: -.0690 S13: -.2355
REMARK 3 S21: .4753 S22: -.6787 S23: -.8193
REMARK 3 S31: 1.5216 S32: .3754 S33: 1.1291
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 : D 185 D 513
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4210 27.5540 63.6830
REMARK 3 T TENSOR
REMARK 3 T11: .3910 T22: -.1758
REMARK 3 T33: .5086 T12: .1217
REMARK 3 T13: .2234 T23: -.0432
REMARK 3 L TENSOR
REMARK 3 L11: 5.5463 L22: 3.9838
REMARK 3 L33: 7.9426 L12: .5467
REMARK 3 L13: .0995 L23: -3.4398
REMARK 3 S TENSOR
REMARK 3 S11: .1305 S12: 1.0574 S13: .5500
REMARK 3 S21: -1.4078 S22: -.3198 S23: .5988
REMARK 3 S31: -.4385 S32: -.3973 S33: .1893
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 : A 29 A 184
REMARK 3 RESIDUE RANGE : A 514 A 538
REMARK 3 ORIGIN FOR THE GROUP (A): 95.0360 -26.4760 40.8500
REMARK 3 T TENSOR
REMARK 3 T11: -.6166 T22: -.4556
REMARK 3 T33: -.6995 T12: .2581
REMARK 3 T13: -.5017 T23: -.1605
REMARK 3 L TENSOR
REMARK 3 L11: 6.9346 L22: 8.3575
REMARK 3 L33: 6.8616 L12: -5.8127
REMARK 3 L13: 5.0730 L23: -4.3134
REMARK 3 S TENSOR
REMARK 3 S11: -.2029 S12: -.3767 S13: .0757
REMARK 3 S21: .3614 S22: .2289 S23: -.4877
REMARK 3 S31: -.9037 S32: .6920 S33: -.0261
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 29 B 184
REMARK 3 RESIDUE RANGE : B 514 B 538
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3560 -7.6140 39.0920
REMARK 3 T TENSOR
REMARK 3 T11: -.7490 T22: -.8941
REMARK 3 T33: -.4072 T12: .0493
REMARK 3 T13: .3005 T23: .1382
REMARK 3 L TENSOR
REMARK 3 L11: 11.4313 L22: 5.3928
REMARK 3 L33: 7.6644 L12: -2.2184
REMARK 3 L13: -6.6324 L23: 1.4657
REMARK 3 S TENSOR
REMARK 3 S11: .2932 S12: -.5253 S13: .1749
REMARK 3 S21: .1658 S22: -.1330 S23: 1.1625
REMARK 3 S31: 1.0466 S32: -.3773 S33: -.1603
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 29 C 184
REMARK 3 RESIDUE RANGE : C 514 C 538
REMARK 3 ORIGIN FOR THE GROUP (A): 122.6060 -46.2110 79.3910
REMARK 3 T TENSOR
REMARK 3 T11: -.9010 T22: .2284
REMARK 3 T33: -.3213 T12: .0609
REMARK 3 T13: -.6326 T23: -.1982
REMARK 3 L TENSOR
REMARK 3 L11: 2.1379 L22: 3.3642
REMARK 3 L33: 15.7591 L12: -1.2061
REMARK 3 L13: 5.4951 L23: -1.0056
REMARK 3 S TENSOR
REMARK 3 S11: -.1645 S12: -.1123 S13: .5162
REMARK 3 S21: .2159 S22: -.1202 S23: .5037
REMARK 3 S31: -.7747 S32: -.8115 S33: .2847
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 : D 29 D 184
REMARK 3 RESIDUE RANGE : D 514 D 538
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6760 5.4880 73.4150
REMARK 3 T TENSOR
REMARK 3 T11: -.7867 T22: -.1130
REMARK 3 T33: .6977 T12: -.1061
REMARK 3 T13: .5008 T23: -.2289
REMARK 3 L TENSOR
REMARK 3 L11: 7.0425 L22: 3.8072
REMARK 3 L33: 9.4956 L12: -2.8065
REMARK 3 L13: -7.8684 L23: 1.7593
REMARK 3 S TENSOR
REMARK 3 S11: -.0205 S12: -.7267 S13: .2348
REMARK 3 S21: .5410 S22: .3274 S23: -1.0095
REMARK 3 S31: -.0439 S32: .6048 S33: -.3069
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 : A 539 A 656
REMARK 3 ORIGIN FOR THE GROUP (A): 68.8890 -2.4860 33.9250
REMARK 3 T TENSOR
REMARK 3 T11: .1564 T22: -.3888
REMARK 3 T33: .3964 T12: .6710
REMARK 3 T13: -.4052 T23: .1486
REMARK 3 L TENSOR
REMARK 3 L11: 10.0297 L22: 8.6306
REMARK 3 L33: 9.1103 L12: 1.9493
REMARK 3 L13: -.8673 L23: 2.0878
REMARK 3 S TENSOR
REMARK 3 S11: .2553 S12: .2584 S13: 1.9445
REMARK 3 S21: .0192 S22: -.3113 S23: .8581
REMARK 3 S31: -2.3707 S32: .0481 S33: .0560
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 539 B 656
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6440 -29.2930 33.2090
REMARK 3 T TENSOR
REMARK 3 T11: .3121 T22: -.3027
REMARK 3 T33: .5233 T12: .9789
REMARK 3 T13: -.0180 T23: .2747
REMARK 3 L TENSOR
REMARK 3 L11: 10.5091 L22: 6.3915
REMARK 3 L33: 3.7962 L12: 2.9548
REMARK 3 L13: 3.8725 L23: 3.5969
REMARK 3 S TENSOR
REMARK 3 S11: .8580 S12: .1825 S13: -2.5115
REMARK 3 S21: .5056 S22: -.3952 S23: -1.2336
REMARK 3 S31: 2.0443 S32: .2390 S33: -.4629
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 539 C 656
REMARK 3 ORIGIN FOR THE GROUP (A): 136.5030 -38.5870 111.9500
REMARK 3 T TENSOR
REMARK 3 T11: .2384 T22: .1827
REMARK 3 T33: -.3455 T12: .0026
REMARK 3 T13: -.6382 T23: -.4738
REMARK 3 L TENSOR
REMARK 3 L11: 13.5811 L22: 6.2166
REMARK 3 L33: 8.2433 L12: 1.0967
REMARK 3 L13: -2.3418 L23: -2.9190
REMARK 3 S TENSOR
REMARK 3 S11: .1087 S12: -1.5028 S13: 1.1718
REMARK 3 S21: .9144 S22: .4754 S23: .6271
REMARK 3 S31: -1.1859 S32: -.0304 S33: -.5841
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 539 D 656
REMARK 3 ORIGIN FOR THE GROUP (A): -36.7020 -6.4310 101.7920
REMARK 3 T TENSOR
REMARK 3 T11: .7830 T22: .5741
REMARK 3 T33: .8032 T12: .0135
REMARK 3 T13: .4953 T23: .3042
REMARK 3 L TENSOR
REMARK 3 L11: 6.8992 L22: .4434
REMARK 3 L33: 5.3782 L12: 1.1920
REMARK 3 L13: -1.9905 L23: -.5305
REMARK 3 S TENSOR
REMARK 3 S11: .4061 S12: -1.3891 S13: -.7439
REMARK 3 S21: 1.5941 S22: -.1810 S23: -.3091
REMARK 3 S31: .7576 S32: -.1101 S33: -.2251
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS WERE ADDED IN THE RIDING
REMARK 3 POSITIONS. TLS REFINEMENT UTILIZED
REMARK 4
REMARK 4 1YM7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031678.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
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 : 100 MICRON COLLIMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24246
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.420
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.35
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.460
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1OMW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, PHOSPHOSERINE, SODIUM CHLORIDE,
REMARK 280 GLYCEROL, PEG 8000, UREA, DITHIOTHREITOL, PH 7.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ASP A 3
REMARK 465 LEU A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 VAL A 7
REMARK 465 LEU A 8
REMARK 465 ALA A 9
REMARK 465 ASP A 10
REMARK 465 VAL A 11
REMARK 465 SER A 12
REMARK 465 TYR A 13
REMARK 465 LEU A 14
REMARK 465 MET A 15
REMARK 465 ALA A 16
REMARK 465 MET A 17
REMARK 465 GLU A 18
REMARK 465 LYS A 19
REMARK 465 SER A 20
REMARK 465 LYS A 21
REMARK 465 ALA A 22
REMARK 465 THR A 23
REMARK 465 PRO A 24
REMARK 465 ALA A 25
REMARK 465 ALA A 26
REMARK 465 ARG A 27
REMARK 465 ALA A 28
REMARK 465 GLU A 476
REMARK 465 VAL A 477
REMARK 465 ASN A 478
REMARK 465 ALA A 479
REMARK 465 ALA A 480
REMARK 465 ASP A 481
REMARK 465 ALA A 482
REMARK 465 PHE A 483
REMARK 465 ASP A 484
REMARK 465 ILE A 485
REMARK 465 GLY A 486
REMARK 465 SER A 487
REMARK 465 PHE A 488
REMARK 465 ASP A 489
REMARK 465 GLU A 490
REMARK 465 GLU A 491
REMARK 465 ASP A 492
REMARK 465 PRO A 571
REMARK 465 PHE A 572
REMARK 465 LEU A 573
REMARK 465 LEU A 657
REMARK 465 VAL A 658
REMARK 465 GLN A 659
REMARK 465 ARG A 660
REMARK 465 VAL A 661
REMARK 465 PRO A 662
REMARK 465 LYS A 663
REMARK 465 MET A 664
REMARK 465 LYS A 665
REMARK 465 ASN A 666
REMARK 465 LYS A 667
REMARK 465 PRO A 668
REMARK 465 ARG A 669
REMARK 465 ALA A 670
REMARK 465 PRO A 671
REMARK 465 VAL A 672
REMARK 465 VAL A 673
REMARK 465 GLU A 674
REMARK 465 LEU A 675
REMARK 465 SER A 676
REMARK 465 LYS A 677
REMARK 465 VAL A 678
REMARK 465 PRO A 679
REMARK 465 LEU A 680
REMARK 465 ILE A 681
REMARK 465 GLN A 682
REMARK 465 ARG A 683
REMARK 465 GLY A 684
REMARK 465 SER A 685
REMARK 465 ALA A 686
REMARK 465 ASN A 687
REMARK 465 GLY A 688
REMARK 465 LEU A 689
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 4
REMARK 465 GLU B 5
REMARK 465 ALA B 6
REMARK 465 VAL B 7
REMARK 465 LEU B 8
REMARK 465 ALA B 9
REMARK 465 ASP B 10
REMARK 465 VAL B 11
REMARK 465 SER B 12
REMARK 465 TYR B 13
REMARK 465 LEU B 14
REMARK 465 MET B 15
REMARK 465 ALA B 16
REMARK 465 MET B 17
REMARK 465 GLU B 18
REMARK 465 LYS B 19
REMARK 465 SER B 20
REMARK 465 LYS B 21
REMARK 465 ALA B 22
REMARK 465 THR B 23
REMARK 465 PRO B 24
REMARK 465 ALA B 25
REMARK 465 ALA B 26
REMARK 465 ARG B 27
REMARK 465 ALA B 28
REMARK 465 GLU B 476
REMARK 465 VAL B 477
REMARK 465 ASN B 478
REMARK 465 ALA B 479
REMARK 465 ALA B 480
REMARK 465 ASP B 481
REMARK 465 ALA B 482
REMARK 465 PHE B 483
REMARK 465 ASP B 484
REMARK 465 ILE B 485
REMARK 465 GLY B 486
REMARK 465 SER B 487
REMARK 465 PHE B 488
REMARK 465 ASP B 489
REMARK 465 GLU B 490
REMARK 465 GLU B 491
REMARK 465 ASP B 492
REMARK 465 PRO B 571
REMARK 465 PHE B 572
REMARK 465 LEU B 573
REMARK 465 LEU B 657
REMARK 465 VAL B 658
REMARK 465 GLN B 659
REMARK 465 ARG B 660
REMARK 465 VAL B 661
REMARK 465 PRO B 662
REMARK 465 LYS B 663
REMARK 465 MET B 664
REMARK 465 LYS B 665
REMARK 465 ASN B 666
REMARK 465 LYS B 667
REMARK 465 PRO B 668
REMARK 465 ARG B 669
REMARK 465 ALA B 670
REMARK 465 PRO B 671
REMARK 465 VAL B 672
REMARK 465 VAL B 673
REMARK 465 GLU B 674
REMARK 465 LEU B 675
REMARK 465 SER B 676
REMARK 465 LYS B 677
REMARK 465 VAL B 678
REMARK 465 PRO B 679
REMARK 465 LEU B 680
REMARK 465 ILE B 681
REMARK 465 GLN B 682
REMARK 465 ARG B 683
REMARK 465 GLY B 684
REMARK 465 SER B 685
REMARK 465 ALA B 686
REMARK 465 ASN B 687
REMARK 465 GLY B 688
REMARK 465 LEU B 689
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ASP C 3
REMARK 465 LEU C 4
REMARK 465 GLU C 5
REMARK 465 ALA C 6
REMARK 465 VAL C 7
REMARK 465 LEU C 8
REMARK 465 ALA C 9
REMARK 465 ASP C 10
REMARK 465 VAL C 11
REMARK 465 SER C 12
REMARK 465 TYR C 13
REMARK 465 LEU C 14
REMARK 465 MET C 15
REMARK 465 ALA C 16
REMARK 465 MET C 17
REMARK 465 GLU C 18
REMARK 465 LYS C 19
REMARK 465 SER C 20
REMARK 465 LYS C 21
REMARK 465 ALA C 22
REMARK 465 THR C 23
REMARK 465 PRO C 24
REMARK 465 ALA C 25
REMARK 465 ALA C 26
REMARK 465 ARG C 27
REMARK 465 ALA C 28
REMARK 465 GLU C 476
REMARK 465 VAL C 477
REMARK 465 ASN C 478
REMARK 465 ALA C 479
REMARK 465 ALA C 480
REMARK 465 ASP C 481
REMARK 465 ALA C 482
REMARK 465 PHE C 483
REMARK 465 ASP C 484
REMARK 465 ILE C 485
REMARK 465 GLY C 486
REMARK 465 SER C 487
REMARK 465 PHE C 488
REMARK 465 ASP C 489
REMARK 465 GLU C 490
REMARK 465 GLU C 491
REMARK 465 ASP C 492
REMARK 465 THR C 493
REMARK 465 PRO C 571
REMARK 465 PHE C 572
REMARK 465 LEU C 573
REMARK 465 LEU C 657
REMARK 465 VAL C 658
REMARK 465 GLN C 659
REMARK 465 ARG C 660
REMARK 465 VAL C 661
REMARK 465 PRO C 662
REMARK 465 LYS C 663
REMARK 465 MET C 664
REMARK 465 LYS C 665
REMARK 465 ASN C 666
REMARK 465 LYS C 667
REMARK 465 PRO C 668
REMARK 465 ARG C 669
REMARK 465 ALA C 670
REMARK 465 PRO C 671
REMARK 465 VAL C 672
REMARK 465 VAL C 673
REMARK 465 GLU C 674
REMARK 465 LEU C 675
REMARK 465 SER C 676
REMARK 465 LYS C 677
REMARK 465 VAL C 678
REMARK 465 PRO C 679
REMARK 465 LEU C 680
REMARK 465 ILE C 681
REMARK 465 GLN C 682
REMARK 465 ARG C 683
REMARK 465 GLY C 684
REMARK 465 SER C 685
REMARK 465 ALA C 686
REMARK 465 ASN C 687
REMARK 465 GLY C 688
REMARK 465 LEU C 689
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 ASP D 3
REMARK 465 LEU D 4
REMARK 465 GLU D 5
REMARK 465 ALA D 6
REMARK 465 VAL D 7
REMARK 465 LEU D 8
REMARK 465 ALA D 9
REMARK 465 ASP D 10
REMARK 465 VAL D 11
REMARK 465 SER D 12
REMARK 465 TYR D 13
REMARK 465 LEU D 14
REMARK 465 MET D 15
REMARK 465 ALA D 16
REMARK 465 MET D 17
REMARK 465 GLU D 18
REMARK 465 LYS D 19
REMARK 465 SER D 20
REMARK 465 LYS D 21
REMARK 465 ALA D 22
REMARK 465 THR D 23
REMARK 465 PRO D 24
REMARK 465 ALA D 25
REMARK 465 ALA D 26
REMARK 465 ARG D 27
REMARK 465 ALA D 28
REMARK 465 GLU D 476
REMARK 465 VAL D 477
REMARK 465 ASN D 478
REMARK 465 ALA D 479
REMARK 465 ALA D 480
REMARK 465 ASP D 481
REMARK 465 ALA D 482
REMARK 465 PHE D 483
REMARK 465 ASP D 484
REMARK 465 ILE D 485
REMARK 465 GLY D 486
REMARK 465 SER D 487
REMARK 465 PHE D 488
REMARK 465 ASP D 489
REMARK 465 GLU D 490
REMARK 465 GLU D 491
REMARK 465 ASP D 492
REMARK 465 LYS D 543
REMARK 465 ASN D 544
REMARK 465 LYS D 545
REMARK 465 GLN D 546
REMARK 465 LEU D 547
REMARK 465 GLY D 548
REMARK 465 HIS D 549
REMARK 465 GLU D 550
REMARK 465 GLU D 551
REMARK 465 PRO D 571
REMARK 465 PHE D 572
REMARK 465 LEU D 573
REMARK 465 LEU D 657
REMARK 465 VAL D 658
REMARK 465 GLN D 659
REMARK 465 ARG D 660
REMARK 465 VAL D 661
REMARK 465 PRO D 662
REMARK 465 LYS D 663
REMARK 465 MET D 664
REMARK 465 LYS D 665
REMARK 465 ASN D 666
REMARK 465 LYS D 667
REMARK 465 PRO D 668
REMARK 465 ARG D 669
REMARK 465 ALA D 670
REMARK 465 PRO D 671
REMARK 465 VAL D 672
REMARK 465 VAL D 673
REMARK 465 GLU D 674
REMARK 465 LEU D 675
REMARK 465 SER D 676
REMARK 465 LYS D 677
REMARK 465 VAL D 678
REMARK 465 PRO D 679
REMARK 465 LEU D 680
REMARK 465 ILE D 681
REMARK 465 GLN D 682
REMARK 465 ARG D 683
REMARK 465 GLY D 684
REMARK 465 SER D 685
REMARK 465 ALA D 686
REMARK 465 ASN D 687
REMARK 465 GLY D 688
REMARK 465 LEU D 689
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 LYS A 545 CE LYS A 545 NZ 0.158
REMARK 500 GLN A 546 CD GLN A 546 OE1 0.567
REMARK 500 GLN A 546 CD GLN A 546 NE2 0.180
REMARK 500 LYS B 543 CE LYS B 543 NZ -0.156
REMARK 500 GLN B 546 CD GLN B 546 OE1 0.304
REMARK 500 LEU B 547 C LEU B 547 O -0.160
REMARK 500 LEU B 547 C GLY B 548 N 0.175
REMARK 500 GLU B 550 CD GLU B 550 OE1 0.092
REMARK 500 GLU B 550 CD GLU B 550 OE2 0.221
REMARK 500 GLU B 551 CD GLU B 551 OE1 0.094
REMARK 500 GLU B 551 CD GLU B 551 OE2 0.103
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 30 -72.49 -48.12
REMARK 500 LYS A 31 153.18 -46.42
REMARK 500 ARG A 40 -83.11 -32.48
REMARK 500 LYS A 80 -70.62 -24.96
REMARK 500 GLU A 96 -70.93 -99.13
REMARK 500 ILE A 113 -67.85 -106.20
REMARK 500 MET A 114 -73.07 -52.78
REMARK 500 CYS A 120 22.19 41.13
REMARK 500 PRO A 123 58.67 -101.05
REMARK 500 GLN A 133 -70.80 -55.00
REMARK 500 HIS A 194 -91.88 -94.06
REMARK 500 THR A 213 -60.23 -107.91
REMARK 500 PRO A 264 -46.56 -17.62
REMARK 500 ASN A 275 -83.03 -92.69
REMARK 500 PHE A 312 39.23 73.52
REMARK 500 ARG A 316 -26.22 74.24
REMARK 500 LEU A 318 106.46 -57.86
REMARK 500 SER A 334 -66.29 -125.66
REMARK 500 LEU A 338 38.41 -92.13
REMARK 500 TYR A 356 71.56 -117.90
REMARK 500 ASP A 369 -131.95 -122.87
REMARK 500 GLN A 393 53.21 -93.84
REMARK 500 HIS A 394 72.41 60.71
REMARK 500 PRO A 414 177.46 -59.44
REMARK 500 LEU A 429 54.20 -96.04
REMARK 500 CYS A 439 -85.21 -110.38
REMARK 500 PRO A 451 -12.31 -39.57
REMARK 500 SER A 514 -75.18 -15.89
REMARK 500 THR A 524 -51.84 -125.40
REMARK 500 GLU A 551 84.63 -43.30
REMARK 500 ASP A 552 124.33 -37.90
REMARK 500 PRO A 585 9.22 -69.31
REMARK 500 ASN A 586 -11.32 -140.25
REMARK 500 PRO A 597 111.24 -33.47
REMARK 500 LYS B 30 -71.91 -51.80
REMARK 500 LYS B 31 155.59 -46.68
REMARK 500 ARG B 40 -77.37 -33.45
REMARK 500 LYS B 80 -70.09 -25.17
REMARK 500 GLU B 96 -70.06 -97.90
REMARK 500 ILE B 113 -65.28 -105.09
REMARK 500 MET B 114 -72.47 -55.74
REMARK 500 CYS B 120 18.68 42.20
REMARK 500 SER B 121 20.56 -79.35
REMARK 500 PRO B 123 58.56 -99.75
REMARK 500 ASN B 183 41.65 -108.27
REMARK 500 HIS B 194 -94.05 -94.52
REMARK 500 THR B 213 -63.59 -107.94
REMARK 500 PRO B 264 -47.38 -16.59
REMARK 500 ASN B 275 -82.63 -95.80
REMARK 500 PHE B 312 37.22 71.58
REMARK 500
REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 493 LYS A 494 -149.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU B 547 -11.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OMW RELATED DB: PDB
REMARK 900 STRUCTURE OF GRK2 IN COMPLEX WITH HETEROTRIMERIC G BETA GAMMA
REMARK 900 SUBUNITS
DBREF 1YM7 A 1 689 UNP P21146 ARBK1_BOVIN 1 689
DBREF 1YM7 B 1 689 UNP P21146 ARBK1_BOVIN 1 689
DBREF 1YM7 C 1 689 UNP P21146 ARBK1_BOVIN 1 689
DBREF 1YM7 D 1 689 UNP P21146 ARBK1_BOVIN 1 689
SEQADV 1YM7 ALA A 670 UNP P21146 SER 670 ENGINEERED MUTATION
SEQADV 1YM7 ALA B 670 UNP P21146 SER 670 ENGINEERED MUTATION
SEQADV 1YM7 ALA C 670 UNP P21146 SER 670 ENGINEERED MUTATION
SEQADV 1YM7 ALA D 670 UNP P21146 SER 670 ENGINEERED MUTATION
SEQRES 1 A 689 MET ALA ASP LEU GLU ALA VAL LEU ALA ASP VAL SER TYR
SEQRES 2 A 689 LEU MET ALA MET GLU LYS SER LYS ALA THR PRO ALA ALA
SEQRES 3 A 689 ARG ALA SER LYS LYS ILE LEU LEU PRO GLU PRO SER ILE
SEQRES 4 A 689 ARG SER VAL MET GLN LYS TYR LEU GLU ASP ARG GLY GLU
SEQRES 5 A 689 VAL THR PHE GLU LYS ILE PHE SER GLN LYS LEU GLY TYR
SEQRES 6 A 689 LEU LEU PHE ARG ASP PHE CYS LEU LYS HIS LEU GLU GLU
SEQRES 7 A 689 ALA LYS PRO LEU VAL GLU PHE TYR GLU GLU ILE LYS LYS
SEQRES 8 A 689 TYR GLU LYS LEU GLU THR GLU GLU GLU ARG LEU VAL CYS
SEQRES 9 A 689 SER ARG GLU ILE PHE ASP THR TYR ILE MET LYS GLU LEU
SEQRES 10 A 689 LEU ALA CYS SER HIS PRO PHE SER LYS SER ALA ILE GLU
SEQRES 11 A 689 HIS VAL GLN GLY HIS LEU VAL LYS LYS GLN VAL PRO PRO
SEQRES 12 A 689 ASP LEU PHE GLN PRO TYR ILE GLU GLU ILE CYS GLN ASN
SEQRES 13 A 689 LEU ARG GLY ASP VAL PHE GLN LYS PHE ILE GLU SER ASP
SEQRES 14 A 689 LYS PHE THR ARG PHE CYS GLN TRP LYS ASN VAL GLU LEU
SEQRES 15 A 689 ASN ILE HIS LEU THR MET ASN ASP PHE SER VAL HIS ARG
SEQRES 16 A 689 ILE ILE GLY ARG GLY GLY PHE GLY GLU VAL TYR GLY CYS
SEQRES 17 A 689 ARG LYS ALA ASP THR GLY LYS MET TYR ALA MET LYS CYS
SEQRES 18 A 689 LEU ASP LYS LYS ARG ILE LYS MET LYS GLN GLY GLU THR
SEQRES 19 A 689 LEU ALA LEU ASN GLU ARG ILE MET LEU SER LEU VAL SER
SEQRES 20 A 689 THR GLY ASP CYS PRO PHE ILE VAL CYS MET SER TYR ALA
SEQRES 21 A 689 PHE HIS THR PRO ASP LYS LEU SER PHE ILE LEU ASP LEU
SEQRES 22 A 689 MET ASN GLY GLY ASP LEU HIS TYR HIS LEU SER GLN HIS
SEQRES 23 A 689 GLY VAL PHE SER GLU ALA ASP MET ARG PHE TYR ALA ALA
SEQRES 24 A 689 GLU ILE ILE LEU GLY LEU GLU HIS MET HIS ASN ARG PHE
SEQRES 25 A 689 VAL VAL TYR ARG ASP LEU LYS PRO ALA ASN ILE LEU LEU
SEQRES 26 A 689 ASP GLU HIS GLY HIS VAL ARG ILE SER ASP LEU GLY LEU
SEQRES 27 A 689 ALA CYS ASP PHE SER LYS LYS LYS PRO HIS ALA SER VAL
SEQRES 28 A 689 GLY THR HIS GLY TYR MET ALA PRO GLU VAL LEU GLN LYS
SEQRES 29 A 689 GLY VAL ALA TYR ASP SER SER ALA ASP TRP PHE SER LEU
SEQRES 30 A 689 GLY CYS MET LEU PHE LYS LEU LEU ARG GLY HIS SER PRO
SEQRES 31 A 689 PHE ARG GLN HIS LYS THR LYS ASP LYS HIS GLU ILE ASP
SEQRES 32 A 689 ARG MET THR LEU THR MET ALA VAL GLU LEU PRO ASP SER
SEQRES 33 A 689 PHE SER PRO GLU LEU ARG SER LEU LEU GLU GLY LEU LEU
SEQRES 34 A 689 GLN ARG ASP VAL ASN ARG ARG LEU GLY CYS LEU GLY ARG
SEQRES 35 A 689 GLY ALA GLN GLU VAL LYS GLU SER PRO PHE PHE ARG SER
SEQRES 36 A 689 LEU ASP TRP GLN MET VAL PHE LEU GLN LYS TYR PRO PRO
SEQRES 37 A 689 PRO LEU ILE PRO PRO ARG GLY GLU VAL ASN ALA ALA ASP
SEQRES 38 A 689 ALA PHE ASP ILE GLY SER PHE ASP GLU GLU ASP THR LYS
SEQRES 39 A 689 GLY ILE LYS LEU LEU ASP SER ASP GLN GLU LEU TYR ARG
SEQRES 40 A 689 ASN PHE PRO LEU THR ILE SER GLU ARG TRP GLN GLN GLU
SEQRES 41 A 689 VAL ALA GLU THR VAL PHE ASP THR ILE ASN ALA GLU THR
SEQRES 42 A 689 ASP ARG LEU GLU ALA ARG LYS LYS THR LYS ASN LYS GLN
SEQRES 43 A 689 LEU GLY HIS GLU GLU ASP TYR ALA LEU GLY LYS ASP CYS
SEQRES 44 A 689 ILE MET HIS GLY TYR MET SER LYS MET GLY ASN PRO PHE
SEQRES 45 A 689 LEU THR GLN TRP GLN ARG ARG TYR PHE TYR LEU PHE PRO
SEQRES 46 A 689 ASN ARG LEU GLU TRP ARG GLY GLU GLY GLU ALA PRO GLN
SEQRES 47 A 689 SER LEU LEU THR MET GLU GLU ILE GLN SER VAL GLU GLU
SEQRES 48 A 689 THR GLN ILE LYS GLU ARG LYS CYS LEU LEU LEU LYS ILE
SEQRES 49 A 689 ARG GLY GLY LYS GLN PHE VAL LEU GLN CYS ASP SER ASP
SEQRES 50 A 689 PRO GLU LEU VAL GLN TRP LYS LYS GLU LEU ARG ASP ALA
SEQRES 51 A 689 TYR ARG GLU ALA GLN GLN LEU VAL GLN ARG VAL PRO LYS
SEQRES 52 A 689 MET LYS ASN LYS PRO ARG ALA PRO VAL VAL GLU LEU SER
SEQRES 53 A 689 LYS VAL PRO LEU ILE GLN ARG GLY SER ALA ASN GLY LEU
SEQRES 1 B 689 MET ALA ASP LEU GLU ALA VAL LEU ALA ASP VAL SER TYR
SEQRES 2 B 689 LEU MET ALA MET GLU LYS SER LYS ALA THR PRO ALA ALA
SEQRES 3 B 689 ARG ALA SER LYS LYS ILE LEU LEU PRO GLU PRO SER ILE
SEQRES 4 B 689 ARG SER VAL MET GLN LYS TYR LEU GLU ASP ARG GLY GLU
SEQRES 5 B 689 VAL THR PHE GLU LYS ILE PHE SER GLN LYS LEU GLY TYR
SEQRES 6 B 689 LEU LEU PHE ARG ASP PHE CYS LEU LYS HIS LEU GLU GLU
SEQRES 7 B 689 ALA LYS PRO LEU VAL GLU PHE TYR GLU GLU ILE LYS LYS
SEQRES 8 B 689 TYR GLU LYS LEU GLU THR GLU GLU GLU ARG LEU VAL CYS
SEQRES 9 B 689 SER ARG GLU ILE PHE ASP THR TYR ILE MET LYS GLU LEU
SEQRES 10 B 689 LEU ALA CYS SER HIS PRO PHE SER LYS SER ALA ILE GLU
SEQRES 11 B 689 HIS VAL GLN GLY HIS LEU VAL LYS LYS GLN VAL PRO PRO
SEQRES 12 B 689 ASP LEU PHE GLN PRO TYR ILE GLU GLU ILE CYS GLN ASN
SEQRES 13 B 689 LEU ARG GLY ASP VAL PHE GLN LYS PHE ILE GLU SER ASP
SEQRES 14 B 689 LYS PHE THR ARG PHE CYS GLN TRP LYS ASN VAL GLU LEU
SEQRES 15 B 689 ASN ILE HIS LEU THR MET ASN ASP PHE SER VAL HIS ARG
SEQRES 16 B 689 ILE ILE GLY ARG GLY GLY PHE GLY GLU VAL TYR GLY CYS
SEQRES 17 B 689 ARG LYS ALA ASP THR GLY LYS MET TYR ALA MET LYS CYS
SEQRES 18 B 689 LEU ASP LYS LYS ARG ILE LYS MET LYS GLN GLY GLU THR
SEQRES 19 B 689 LEU ALA LEU ASN GLU ARG ILE MET LEU SER LEU VAL SER
SEQRES 20 B 689 THR GLY ASP CYS PRO PHE ILE VAL CYS MET SER TYR ALA
SEQRES 21 B 689 PHE HIS THR PRO ASP LYS LEU SER PHE ILE LEU ASP LEU
SEQRES 22 B 689 MET ASN GLY GLY ASP LEU HIS TYR HIS LEU SER GLN HIS
SEQRES 23 B 689 GLY VAL PHE SER GLU ALA ASP MET ARG PHE TYR ALA ALA
SEQRES 24 B 689 GLU ILE ILE LEU GLY LEU GLU HIS MET HIS ASN ARG PHE
SEQRES 25 B 689 VAL VAL TYR ARG ASP LEU LYS PRO ALA ASN ILE LEU LEU
SEQRES 26 B 689 ASP GLU HIS GLY HIS VAL ARG ILE SER ASP LEU GLY LEU
SEQRES 27 B 689 ALA CYS ASP PHE SER LYS LYS LYS PRO HIS ALA SER VAL
SEQRES 28 B 689 GLY THR HIS GLY TYR MET ALA PRO GLU VAL LEU GLN LYS
SEQRES 29 B 689 GLY VAL ALA TYR ASP SER SER ALA ASP TRP PHE SER LEU
SEQRES 30 B 689 GLY CYS MET LEU PHE LYS LEU LEU ARG GLY HIS SER PRO
SEQRES 31 B 689 PHE ARG GLN HIS LYS THR LYS ASP LYS HIS GLU ILE ASP
SEQRES 32 B 689 ARG MET THR LEU THR MET ALA VAL GLU LEU PRO ASP SER
SEQRES 33 B 689 PHE SER PRO GLU LEU ARG SER LEU LEU GLU GLY LEU LEU
SEQRES 34 B 689 GLN ARG ASP VAL ASN ARG ARG LEU GLY CYS LEU GLY ARG
SEQRES 35 B 689 GLY ALA GLN GLU VAL LYS GLU SER PRO PHE PHE ARG SER
SEQRES 36 B 689 LEU ASP TRP GLN MET VAL PHE LEU GLN LYS TYR PRO PRO
SEQRES 37 B 689 PRO LEU ILE PRO PRO ARG GLY GLU VAL ASN ALA ALA ASP
SEQRES 38 B 689 ALA PHE ASP ILE GLY SER PHE ASP GLU GLU ASP THR LYS
SEQRES 39 B 689 GLY ILE LYS LEU LEU ASP SER ASP GLN GLU LEU TYR ARG
SEQRES 40 B 689 ASN PHE PRO LEU THR ILE SER GLU ARG TRP GLN GLN GLU
SEQRES 41 B 689 VAL ALA GLU THR VAL PHE ASP THR ILE ASN ALA GLU THR
SEQRES 42 B 689 ASP ARG LEU GLU ALA ARG LYS LYS THR LYS ASN LYS GLN
SEQRES 43 B 689 LEU GLY HIS GLU GLU ASP TYR ALA LEU GLY LYS ASP CYS
SEQRES 44 B 689 ILE MET HIS GLY TYR MET SER LYS MET GLY ASN PRO PHE
SEQRES 45 B 689 LEU THR GLN TRP GLN ARG ARG TYR PHE TYR LEU PHE PRO
SEQRES 46 B 689 ASN ARG LEU GLU TRP ARG GLY GLU GLY GLU ALA PRO GLN
SEQRES 47 B 689 SER LEU LEU THR MET GLU GLU ILE GLN SER VAL GLU GLU
SEQRES 48 B 689 THR GLN ILE LYS GLU ARG LYS CYS LEU LEU LEU LYS ILE
SEQRES 49 B 689 ARG GLY GLY LYS GLN PHE VAL LEU GLN CYS ASP SER ASP
SEQRES 50 B 689 PRO GLU LEU VAL GLN TRP LYS LYS GLU LEU ARG ASP ALA
SEQRES 51 B 689 TYR ARG GLU ALA GLN GLN LEU VAL GLN ARG VAL PRO LYS
SEQRES 52 B 689 MET LYS ASN LYS PRO ARG ALA PRO VAL VAL GLU LEU SER
SEQRES 53 B 689 LYS VAL PRO LEU ILE GLN ARG GLY SER ALA ASN GLY LEU
SEQRES 1 C 689 MET ALA ASP LEU GLU ALA VAL LEU ALA ASP VAL SER TYR
SEQRES 2 C 689 LEU MET ALA MET GLU LYS SER LYS ALA THR PRO ALA ALA
SEQRES 3 C 689 ARG ALA SER LYS LYS ILE LEU LEU PRO GLU PRO SER ILE
SEQRES 4 C 689 ARG SER VAL MET GLN LYS TYR LEU GLU ASP ARG GLY GLU
SEQRES 5 C 689 VAL THR PHE GLU LYS ILE PHE SER GLN LYS LEU GLY TYR
SEQRES 6 C 689 LEU LEU PHE ARG ASP PHE CYS LEU LYS HIS LEU GLU GLU
SEQRES 7 C 689 ALA LYS PRO LEU VAL GLU PHE TYR GLU GLU ILE LYS LYS
SEQRES 8 C 689 TYR GLU LYS LEU GLU THR GLU GLU GLU ARG LEU VAL CYS
SEQRES 9 C 689 SER ARG GLU ILE PHE ASP THR TYR ILE MET LYS GLU LEU
SEQRES 10 C 689 LEU ALA CYS SER HIS PRO PHE SER LYS SER ALA ILE GLU
SEQRES 11 C 689 HIS VAL GLN GLY HIS LEU VAL LYS LYS GLN VAL PRO PRO
SEQRES 12 C 689 ASP LEU PHE GLN PRO TYR ILE GLU GLU ILE CYS GLN ASN
SEQRES 13 C 689 LEU ARG GLY ASP VAL PHE GLN LYS PHE ILE GLU SER ASP
SEQRES 14 C 689 LYS PHE THR ARG PHE CYS GLN TRP LYS ASN VAL GLU LEU
SEQRES 15 C 689 ASN ILE HIS LEU THR MET ASN ASP PHE SER VAL HIS ARG
SEQRES 16 C 689 ILE ILE GLY ARG GLY GLY PHE GLY GLU VAL TYR GLY CYS
SEQRES 17 C 689 ARG LYS ALA ASP THR GLY LYS MET TYR ALA MET LYS CYS
SEQRES 18 C 689 LEU ASP LYS LYS ARG ILE LYS MET LYS GLN GLY GLU THR
SEQRES 19 C 689 LEU ALA LEU ASN GLU ARG ILE MET LEU SER LEU VAL SER
SEQRES 20 C 689 THR GLY ASP CYS PRO PHE ILE VAL CYS MET SER TYR ALA
SEQRES 21 C 689 PHE HIS THR PRO ASP LYS LEU SER PHE ILE LEU ASP LEU
SEQRES 22 C 689 MET ASN GLY GLY ASP LEU HIS TYR HIS LEU SER GLN HIS
SEQRES 23 C 689 GLY VAL PHE SER GLU ALA ASP MET ARG PHE TYR ALA ALA
SEQRES 24 C 689 GLU ILE ILE LEU GLY LEU GLU HIS MET HIS ASN ARG PHE
SEQRES 25 C 689 VAL VAL TYR ARG ASP LEU LYS PRO ALA ASN ILE LEU LEU
SEQRES 26 C 689 ASP GLU HIS GLY HIS VAL ARG ILE SER ASP LEU GLY LEU
SEQRES 27 C 689 ALA CYS ASP PHE SER LYS LYS LYS PRO HIS ALA SER VAL
SEQRES 28 C 689 GLY THR HIS GLY TYR MET ALA PRO GLU VAL LEU GLN LYS
SEQRES 29 C 689 GLY VAL ALA TYR ASP SER SER ALA ASP TRP PHE SER LEU
SEQRES 30 C 689 GLY CYS MET LEU PHE LYS LEU LEU ARG GLY HIS SER PRO
SEQRES 31 C 689 PHE ARG GLN HIS LYS THR LYS ASP LYS HIS GLU ILE ASP
SEQRES 32 C 689 ARG MET THR LEU THR MET ALA VAL GLU LEU PRO ASP SER
SEQRES 33 C 689 PHE SER PRO GLU LEU ARG SER LEU LEU GLU GLY LEU LEU
SEQRES 34 C 689 GLN ARG ASP VAL ASN ARG ARG LEU GLY CYS LEU GLY ARG
SEQRES 35 C 689 GLY ALA GLN GLU VAL LYS GLU SER PRO PHE PHE ARG SER
SEQRES 36 C 689 LEU ASP TRP GLN MET VAL PHE LEU GLN LYS TYR PRO PRO
SEQRES 37 C 689 PRO LEU ILE PRO PRO ARG GLY GLU VAL ASN ALA ALA ASP
SEQRES 38 C 689 ALA PHE ASP ILE GLY SER PHE ASP GLU GLU ASP THR LYS
SEQRES 39 C 689 GLY ILE LYS LEU LEU ASP SER ASP GLN GLU LEU TYR ARG
SEQRES 40 C 689 ASN PHE PRO LEU THR ILE SER GLU ARG TRP GLN GLN GLU
SEQRES 41 C 689 VAL ALA GLU THR VAL PHE ASP THR ILE ASN ALA GLU THR
SEQRES 42 C 689 ASP ARG LEU GLU ALA ARG LYS LYS THR LYS ASN LYS GLN
SEQRES 43 C 689 LEU GLY HIS GLU GLU ASP TYR ALA LEU GLY LYS ASP CYS
SEQRES 44 C 689 ILE MET HIS GLY TYR MET SER LYS MET GLY ASN PRO PHE
SEQRES 45 C 689 LEU THR GLN TRP GLN ARG ARG TYR PHE TYR LEU PHE PRO
SEQRES 46 C 689 ASN ARG LEU GLU TRP ARG GLY GLU GLY GLU ALA PRO GLN
SEQRES 47 C 689 SER LEU LEU THR MET GLU GLU ILE GLN SER VAL GLU GLU
SEQRES 48 C 689 THR GLN ILE LYS GLU ARG LYS CYS LEU LEU LEU LYS ILE
SEQRES 49 C 689 ARG GLY GLY LYS GLN PHE VAL LEU GLN CYS ASP SER ASP
SEQRES 50 C 689 PRO GLU LEU VAL GLN TRP LYS LYS GLU LEU ARG ASP ALA
SEQRES 51 C 689 TYR ARG GLU ALA GLN GLN LEU VAL GLN ARG VAL PRO LYS
SEQRES 52 C 689 MET LYS ASN LYS PRO ARG ALA PRO VAL VAL GLU LEU SER
SEQRES 53 C 689 LYS VAL PRO LEU ILE GLN ARG GLY SER ALA ASN GLY LEU
SEQRES 1 D 689 MET ALA ASP LEU GLU ALA VAL LEU ALA ASP VAL SER TYR
SEQRES 2 D 689 LEU MET ALA MET GLU LYS SER LYS ALA THR PRO ALA ALA
SEQRES 3 D 689 ARG ALA SER LYS LYS ILE LEU LEU PRO GLU PRO SER ILE
SEQRES 4 D 689 ARG SER VAL MET GLN LYS TYR LEU GLU ASP ARG GLY GLU
SEQRES 5 D 689 VAL THR PHE GLU LYS ILE PHE SER GLN LYS LEU GLY TYR
SEQRES 6 D 689 LEU LEU PHE ARG ASP PHE CYS LEU LYS HIS LEU GLU GLU
SEQRES 7 D 689 ALA LYS PRO LEU VAL GLU PHE TYR GLU GLU ILE LYS LYS
SEQRES 8 D 689 TYR GLU LYS LEU GLU THR GLU GLU GLU ARG LEU VAL CYS
SEQRES 9 D 689 SER ARG GLU ILE PHE ASP THR TYR ILE MET LYS GLU LEU
SEQRES 10 D 689 LEU ALA CYS SER HIS PRO PHE SER LYS SER ALA ILE GLU
SEQRES 11 D 689 HIS VAL GLN GLY HIS LEU VAL LYS LYS GLN VAL PRO PRO
SEQRES 12 D 689 ASP LEU PHE GLN PRO TYR ILE GLU GLU ILE CYS GLN ASN
SEQRES 13 D 689 LEU ARG GLY ASP VAL PHE GLN LYS PHE ILE GLU SER ASP
SEQRES 14 D 689 LYS PHE THR ARG PHE CYS GLN TRP LYS ASN VAL GLU LEU
SEQRES 15 D 689 ASN ILE HIS LEU THR MET ASN ASP PHE SER VAL HIS ARG
SEQRES 16 D 689 ILE ILE GLY ARG GLY GLY PHE GLY GLU VAL TYR GLY CYS
SEQRES 17 D 689 ARG LYS ALA ASP THR GLY LYS MET TYR ALA MET LYS CYS
SEQRES 18 D 689 LEU ASP LYS LYS ARG ILE LYS MET LYS GLN GLY GLU THR
SEQRES 19 D 689 LEU ALA LEU ASN GLU ARG ILE MET LEU SER LEU VAL SER
SEQRES 20 D 689 THR GLY ASP CYS PRO PHE ILE VAL CYS MET SER TYR ALA
SEQRES 21 D 689 PHE HIS THR PRO ASP LYS LEU SER PHE ILE LEU ASP LEU
SEQRES 22 D 689 MET ASN GLY GLY ASP LEU HIS TYR HIS LEU SER GLN HIS
SEQRES 23 D 689 GLY VAL PHE SER GLU ALA ASP MET ARG PHE TYR ALA ALA
SEQRES 24 D 689 GLU ILE ILE LEU GLY LEU GLU HIS MET HIS ASN ARG PHE
SEQRES 25 D 689 VAL VAL TYR ARG ASP LEU LYS PRO ALA ASN ILE LEU LEU
SEQRES 26 D 689 ASP GLU HIS GLY HIS VAL ARG ILE SER ASP LEU GLY LEU
SEQRES 27 D 689 ALA CYS ASP PHE SER LYS LYS LYS PRO HIS ALA SER VAL
SEQRES 28 D 689 GLY THR HIS GLY TYR MET ALA PRO GLU VAL LEU GLN LYS
SEQRES 29 D 689 GLY VAL ALA TYR ASP SER SER ALA ASP TRP PHE SER LEU
SEQRES 30 D 689 GLY CYS MET LEU PHE LYS LEU LEU ARG GLY HIS SER PRO
SEQRES 31 D 689 PHE ARG GLN HIS LYS THR LYS ASP LYS HIS GLU ILE ASP
SEQRES 32 D 689 ARG MET THR LEU THR MET ALA VAL GLU LEU PRO ASP SER
SEQRES 33 D 689 PHE SER PRO GLU LEU ARG SER LEU LEU GLU GLY LEU LEU
SEQRES 34 D 689 GLN ARG ASP VAL ASN ARG ARG LEU GLY CYS LEU GLY ARG
SEQRES 35 D 689 GLY ALA GLN GLU VAL LYS GLU SER PRO PHE PHE ARG SER
SEQRES 36 D 689 LEU ASP TRP GLN MET VAL PHE LEU GLN LYS TYR PRO PRO
SEQRES 37 D 689 PRO LEU ILE PRO PRO ARG GLY GLU VAL ASN ALA ALA ASP
SEQRES 38 D 689 ALA PHE ASP ILE GLY SER PHE ASP GLU GLU ASP THR LYS
SEQRES 39 D 689 GLY ILE LYS LEU LEU ASP SER ASP GLN GLU LEU TYR ARG
SEQRES 40 D 689 ASN PHE PRO LEU THR ILE SER GLU ARG TRP GLN GLN GLU
SEQRES 41 D 689 VAL ALA GLU THR VAL PHE ASP THR ILE ASN ALA GLU THR
SEQRES 42 D 689 ASP ARG LEU GLU ALA ARG LYS LYS THR LYS ASN LYS GLN
SEQRES 43 D 689 LEU GLY HIS GLU GLU ASP TYR ALA LEU GLY LYS ASP CYS
SEQRES 44 D 689 ILE MET HIS GLY TYR MET SER LYS MET GLY ASN PRO PHE
SEQRES 45 D 689 LEU THR GLN TRP GLN ARG ARG TYR PHE TYR LEU PHE PRO
SEQRES 46 D 689 ASN ARG LEU GLU TRP ARG GLY GLU GLY GLU ALA PRO GLN
SEQRES 47 D 689 SER LEU LEU THR MET GLU GLU ILE GLN SER VAL GLU GLU
SEQRES 48 D 689 THR GLN ILE LYS GLU ARG LYS CYS LEU LEU LEU LYS ILE
SEQRES 49 D 689 ARG GLY GLY LYS GLN PHE VAL LEU GLN CYS ASP SER ASP
SEQRES 50 D 689 PRO GLU LEU VAL GLN TRP LYS LYS GLU LEU ARG ASP ALA
SEQRES 51 D 689 TYR ARG GLU ALA GLN GLN LEU VAL GLN ARG VAL PRO LYS
SEQRES 52 D 689 MET LYS ASN LYS PRO ARG ALA PRO VAL VAL GLU LEU SER
SEQRES 53 D 689 LYS VAL PRO LEU ILE GLN ARG GLY SER ALA ASN GLY LEU
HELIX 1 1 GLU A 36 SER A 38 5 3
HELIX 2 2 ILE A 39 ARG A 50 1 12
HELIX 3 3 THR A 54 GLN A 61 1 8
HELIX 4 4 GLN A 61 HIS A 75 1 15
HELIX 5 5 GLU A 78 LYS A 94 1 17
HELIX 6 6 THR A 97 ILE A 113 1 17
HELIX 7 7 ILE A 113 ALA A 119 1 7
HELIX 8 8 SER A 125 VAL A 137 1 13
HELIX 9 9 PHE A 146 GLY A 159 1 14
HELIX 10 10 GLY A 159 GLU A 167 1 9
HELIX 11 11 SER A 168 ASN A 183 1 16
HELIX 12 12 THR A 187 ASN A 189 5 3
HELIX 13 13 LYS A 224 LYS A 230 1 7
HELIX 14 14 GLY A 232 SER A 247 1 16
HELIX 15 15 ASP A 278 GLY A 287 1 10
HELIX 16 16 SER A 290 ARG A 311 1 22
HELIX 17 17 LYS A 319 ALA A 321 5 3
HELIX 18 18 ALA A 358 GLN A 363 1 6
HELIX 19 19 SER A 370 GLY A 387 1 18
HELIX 20 20 LYS A 399 MET A 409 1 11
HELIX 21 21 SER A 418 LEU A 429 1 12
HELIX 22 22 GLY A 443 SER A 450 1 8
HELIX 23 23 PRO A 451 ARG A 454 5 4
HELIX 24 24 ASP A 457 LEU A 463 1 7
HELIX 25 25 ASP A 502 TYR A 506 5 5
HELIX 26 26 ILE A 513 VAL A 525 1 13
HELIX 27 27 VAL A 525 ARG A 539 1 15
HELIX 28 28 LYS A 541 GLN A 546 1 6
HELIX 29 29 SER A 636 GLN A 655 1 20
HELIX 30 30 GLU B 36 SER B 38 5 3
HELIX 31 31 ILE B 39 ARG B 50 1 12
HELIX 32 32 THR B 54 GLN B 61 1 8
HELIX 33 33 GLN B 61 HIS B 75 1 15
HELIX 34 34 GLU B 78 LYS B 94 1 17
HELIX 35 35 THR B 97 ILE B 113 1 17
HELIX 36 36 ILE B 113 ALA B 119 1 7
HELIX 37 37 SER B 125 VAL B 137 1 13
HELIX 38 38 PHE B 146 GLY B 159 1 14
HELIX 39 39 GLY B 159 GLU B 167 1 9
HELIX 40 40 SER B 168 ASN B 183 1 16
HELIX 41 41 THR B 187 ASN B 189 5 3
HELIX 42 42 LYS B 224 LYS B 230 1 7
HELIX 43 43 GLY B 232 SER B 247 1 16
HELIX 44 44 ASP B 278 GLY B 287 1 10
HELIX 45 45 SER B 290 ARG B 311 1 22
HELIX 46 46 LYS B 319 ALA B 321 5 3
HELIX 47 47 ALA B 358 GLN B 363 1 6
HELIX 48 48 SER B 370 GLY B 387 1 18
HELIX 49 49 LYS B 399 MET B 409 1 11
HELIX 50 50 SER B 418 LEU B 429 1 12
HELIX 51 51 GLY B 443 SER B 450 1 8
HELIX 52 52 PRO B 451 ARG B 454 5 4
HELIX 53 53 ASP B 457 LEU B 463 1 7
HELIX 54 54 LEU B 499 GLU B 504 1 6
HELIX 55 55 ILE B 513 VAL B 525 1 13
HELIX 56 56 VAL B 525 LYS B 543 1 19
HELIX 57 57 SER B 636 GLN B 655 1 20
HELIX 58 58 GLU C 36 SER C 38 5 3
HELIX 59 59 ILE C 39 ARG C 50 1 12
HELIX 60 60 THR C 54 GLN C 61 1 8
HELIX 61 61 GLN C 61 HIS C 75 1 15
HELIX 62 62 GLU C 78 LYS C 94 1 17
HELIX 63 63 THR C 97 ILE C 113 1 17
HELIX 64 64 ILE C 113 ALA C 119 1 7
HELIX 65 65 SER C 125 VAL C 137 1 13
HELIX 66 66 PHE C 146 GLY C 159 1 14
HELIX 67 67 GLY C 159 GLU C 167 1 9
HELIX 68 68 SER C 168 ASN C 183 1 16
HELIX 69 69 THR C 187 ASN C 189 5 3
HELIX 70 70 LYS C 224 GLN C 231 1 8
HELIX 71 71 GLY C 232 SER C 247 1 16
HELIX 72 72 ASP C 278 GLY C 287 1 10
HELIX 73 73 SER C 290 ARG C 311 1 22
HELIX 74 74 LYS C 319 ALA C 321 5 3
HELIX 75 75 ALA C 358 GLN C 363 1 6
HELIX 76 76 SER C 370 GLY C 387 1 18
HELIX 77 77 LYS C 399 MET C 409 1 11
HELIX 78 78 SER C 418 LEU C 429 1 12
HELIX 79 79 GLY C 443 SER C 450 1 8
HELIX 80 80 PRO C 451 ARG C 454 5 4
HELIX 81 81 ASP C 457 LEU C 463 1 7
HELIX 82 82 LEU C 499 GLU C 504 1 6
HELIX 83 83 ILE C 513 VAL C 525 1 13
HELIX 84 84 VAL C 525 LYS C 541 1 17
HELIX 85 85 SER C 636 GLN C 655 1 20
HELIX 86 86 GLU D 36 SER D 38 5 3
HELIX 87 87 ILE D 39 ARG D 50 1 12
HELIX 88 88 THR D 54 GLN D 61 1 8
HELIX 89 89 GLN D 61 HIS D 75 1 15
HELIX 90 90 GLU D 78 LYS D 94 1 17
HELIX 91 91 THR D 97 ILE D 113 1 17
HELIX 92 92 ILE D 113 ALA D 119 1 7
HELIX 93 93 SER D 125 VAL D 137 1 13
HELIX 94 94 PHE D 146 GLY D 159 1 14
HELIX 95 95 GLY D 159 GLU D 167 1 9
HELIX 96 96 SER D 168 ASN D 183 1 16
HELIX 97 97 THR D 187 ASN D 189 5 3
HELIX 98 98 LYS D 224 GLN D 231 1 8
HELIX 99 99 GLY D 232 SER D 247 1 16
HELIX 100 100 ASP D 278 GLY D 287 1 10
HELIX 101 101 SER D 290 ARG D 311 1 22
HELIX 102 102 LYS D 319 ALA D 321 5 3
HELIX 103 103 ALA D 358 GLN D 363 1 6
HELIX 104 104 SER D 370 GLY D 387 1 18
HELIX 105 105 LYS D 399 MET D 409 1 11
HELIX 106 106 SER D 418 LEU D 429 1 12
HELIX 107 107 GLY D 443 SER D 450 1 8
HELIX 108 108 PRO D 451 ARG D 454 5 4
HELIX 109 109 ASP D 457 LEU D 463 1 7
HELIX 110 110 ASP D 502 TYR D 506 5 5
HELIX 111 111 ILE D 513 VAL D 525 1 13
HELIX 112 112 VAL D 525 ARG D 539 1 15
HELIX 113 113 SER D 636 GLN D 655 1 20
SHEET 1 A 6 PHE A 191 ILE A 196 0
SHEET 2 A 6 VAL A 205 LYS A 210 -1 O GLY A 207 N HIS A 194
SHEET 3 A 6 MET A 216 ASP A 223 -1 O MET A 219 N TYR A 206
SHEET 4 A 6 LYS A 266 ASP A 272 -1 O LEU A 271 N ALA A 218
SHEET 5 A 6 MET A 257 THR A 263 -1 N SER A 258 O ILE A 270
SHEET 6 A 6 LEU A 511 THR A 512 -1 O LEU A 511 N ALA A 260
SHEET 1 B 2 VAL A 313 VAL A 314 0
SHEET 2 B 2 CYS A 340 ASP A 341 -1 O CYS A 340 N VAL A 314
SHEET 1 C 2 ILE A 323 LEU A 325 0
SHEET 2 C 2 VAL A 331 ILE A 333 -1 O ARG A 332 N LEU A 324
SHEET 1 D 7 SER A 599 LEU A 600 0
SHEET 2 D 7 ARG A 587 ARG A 591 -1 N TRP A 590 O SER A 599
SHEET 3 D 7 GLN A 575 PHE A 584 -1 N TYR A 582 O GLU A 589
SHEET 4 D 7 TYR A 564 GLY A 569 -1 N MET A 565 O ARG A 579
SHEET 5 D 7 GLN A 629 GLN A 633 -1 O GLN A 633 N SER A 566
SHEET 6 D 7 CYS A 619 LYS A 623 -1 N LEU A 622 O PHE A 630
SHEET 7 D 7 SER A 608 THR A 612 -1 N GLU A 610 O LEU A 621
SHEET 1 E 6 PHE B 191 ARG B 199 0
SHEET 2 E 6 GLU B 204 LYS B 210 -1 O VAL B 205 N ILE B 197
SHEET 3 E 6 MET B 216 ASP B 223 -1 O TYR B 217 N CYS B 208
SHEET 4 E 6 LYS B 266 ASP B 272 -1 O LEU B 267 N LEU B 222
SHEET 5 E 6 MET B 257 THR B 263 -1 N SER B 258 O ILE B 270
SHEET 6 E 6 LEU B 511 THR B 512 -1 O LEU B 511 N ALA B 260
SHEET 1 F 2 VAL B 313 VAL B 314 0
SHEET 2 F 2 CYS B 340 ASP B 341 -1 O CYS B 340 N VAL B 314
SHEET 1 G 2 ILE B 323 LEU B 325 0
SHEET 2 G 2 VAL B 331 ILE B 333 -1 O ARG B 332 N LEU B 324
SHEET 1 H 4 MET B 561 GLY B 569 0
SHEET 2 H 4 GLN B 575 PHE B 584 -1 O LEU B 583 N MET B 561
SHEET 3 H 4 ARG B 587 ARG B 591 -1 O GLU B 589 N TYR B 582
SHEET 4 H 4 SER B 599 LEU B 600 -1 O SER B 599 N TRP B 590
SHEET 1 I 3 ILE B 606 THR B 612 0
SHEET 2 I 3 CYS B 619 ILE B 624 -1 O LEU B 621 N GLU B 610
SHEET 3 I 3 GLN B 629 LEU B 632 -1 O PHE B 630 N LEU B 622
SHEET 1 J 6 PHE C 191 ARG C 199 0
SHEET 2 J 6 GLU C 204 LYS C 210 -1 O VAL C 205 N ILE C 197
SHEET 3 J 6 MET C 216 ASP C 223 -1 O MET C 219 N TYR C 206
SHEET 4 J 6 LYS C 266 ASP C 272 -1 O LEU C 267 N LEU C 222
SHEET 5 J 6 MET C 257 THR C 263 -1 N SER C 258 O ILE C 270
SHEET 6 J 6 LEU C 511 THR C 512 -1 O LEU C 511 N ALA C 260
SHEET 1 K 2 VAL C 313 VAL C 314 0
SHEET 2 K 2 CYS C 340 ASP C 341 -1 O CYS C 340 N VAL C 314
SHEET 1 L 2 ILE C 323 LEU C 325 0
SHEET 2 L 2 VAL C 331 ILE C 333 -1 O ARG C 332 N LEU C 324
SHEET 1 M 4 MET C 561 GLY C 569 0
SHEET 2 M 4 GLN C 575 PHE C 584 -1 O ARG C 579 N MET C 565
SHEET 3 M 4 ARG C 587 ARG C 591 -1 O GLU C 589 N TYR C 582
SHEET 4 M 4 SER C 599 LEU C 600 -1 O SER C 599 N TRP C 590
SHEET 1 N 3 ILE C 606 THR C 612 0
SHEET 2 N 3 CYS C 619 ILE C 624 -1 O LEU C 621 N GLU C 610
SHEET 3 N 3 GLN C 629 LEU C 632 -1 O PHE C 630 N LEU C 622
SHEET 1 O 6 PHE D 191 ARG D 199 0
SHEET 2 O 6 GLU D 204 LYS D 210 -1 O VAL D 205 N ILE D 197
SHEET 3 O 6 MET D 216 ASP D 223 -1 O TYR D 217 N CYS D 208
SHEET 4 O 6 LYS D 266 ASP D 272 -1 O LEU D 271 N ALA D 218
SHEET 5 O 6 MET D 257 THR D 263 -1 N SER D 258 O ILE D 270
SHEET 6 O 6 LEU D 511 THR D 512 -1 O LEU D 511 N ALA D 260
SHEET 1 P 2 VAL D 313 VAL D 314 0
SHEET 2 P 2 CYS D 340 ASP D 341 -1 O CYS D 340 N VAL D 314
SHEET 1 Q 2 ILE D 323 LEU D 325 0
SHEET 2 Q 2 VAL D 331 ILE D 333 -1 O ARG D 332 N LEU D 324
SHEET 1 R 4 MET D 561 GLY D 569 0
SHEET 2 R 4 GLN D 575 PHE D 584 -1 O LEU D 583 N MET D 561
SHEET 3 R 4 ARG D 587 ARG D 591 -1 O GLU D 589 N TYR D 582
SHEET 4 R 4 SER D 599 LEU D 600 -1 O SER D 599 N TRP D 590
SHEET 1 S 3 SER D 608 THR D 612 0
SHEET 2 S 3 CYS D 619 LYS D 623 -1 O LEU D 621 N GLU D 610
SHEET 3 S 3 GLN D 629 LEU D 632 -1 O PHE D 630 N LEU D 622
CRYST1 115.162 82.156 218.795 90.00 95.57 90.00 P 1 2 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 0.008683 0.000000 0.000847 0.00000
SCALE2 0.000000 0.012172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004592 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
