HEADER TRANSFERASE 07-JAN-11 2Y4P
TITLE DIMERIC STRUCTURE OF DAPK-1 CATALYTIC DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEATH-ASSOCIATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1-285;
COMPND 5 SYNONYM: DAP KINASE 1;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PETM14
KEYWDS CALMODULIN-BINDING, SERINE/THREONINE-PROTEIN KINASE, NUCLEOTIDE-
KEYWDS 2 BINDING, APOPTOSIS, TRANSFERASE, ATP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR I.DE DIEGO,F.LEHMANN,M.WILMANNS
REVDAT 2 20-DEC-23 2Y4P 1 REMARK
REVDAT 1 18-JAN-12 2Y4P 0
JRNL AUTH I.DE DIEGO,J.KUPER,F.LEHMANN,M.WILMANNS
JRNL TITL A JOURNEY THROUGH THE DAP KINASE ARCHITECTURE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 117.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 39240
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) : 0.255
REMARK 3 R VALUE (WORKING SET) : 0.252
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2087
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) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2879
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.3280
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7171
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.48000
REMARK 3 B22 (A**2) : 2.01000
REMARK 3 B33 (A**2) : 1.79000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.83000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.590
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.367
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.302
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.574
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.895
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.840
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7313 ; 0.036 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9891 ; 1.787 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 878 ; 5.790 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 348 ;38.020 ;24.971
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1305 ;24.401 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;25.869 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1127 ; 0.180 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5441 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4448 ; 0.257 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7192 ; 0.350 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2865 ; 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): 2699 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 275 3
REMARK 3 1 C 1 C 275 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 995 ; 0.31 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 995 ; 0.31 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 1007 ; 0.52 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 1007 ; 0.52 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 995 ; 0.00 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 995 ; 0.00 ; 0.50
REMARK 3 LOOSE THERMAL 1 A (A**2): 1007 ; 0.00 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 1007 ; 0.00 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 275 3
REMARK 3 1 D 1 D 275 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 712 ; 0.27 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 712 ; 0.27 ; 0.05
REMARK 3 LOOSE POSITIONAL 2 B (A): 714 ; 0.48 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 D (A): 714 ; 0.48 ; 5.00
REMARK 3 TIGHT THERMAL 2 B (A**2): 712 ; 0.00 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 712 ; 0.00 ; 0.50
REMARK 3 LOOSE THERMAL 2 B (A**2): 714 ; 0.00 ; 10.00
REMARK 3 LOOSE THERMAL 2 D (A**2): 714 ; 0.00 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
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 4 A 39
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9285 30.2538 117.0913
REMARK 3 T TENSOR
REMARK 3 T11: 0.1736 T22: 0.1152
REMARK 3 T33: 0.4175 T12: -0.0524
REMARK 3 T13: 0.0390 T23: 0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 9.1382 L22: 8.6652
REMARK 3 L33: 11.5133 L12: -2.4065
REMARK 3 L13: -2.4910 L23: -2.7538
REMARK 3 S TENSOR
REMARK 3 S11: 0.3043 S12: 0.5471 S13: -0.0995
REMARK 3 S21: -0.2389 S22: 0.0324 S23: 0.4710
REMARK 3 S31: 0.2612 S32: -0.3394 S33: -0.3366
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 40 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0531 45.4145 109.6006
REMARK 3 T TENSOR
REMARK 3 T11: 0.0642 T22: 0.1151
REMARK 3 T33: 0.1250 T12: 0.0251
REMARK 3 T13: 0.0630 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 2.7020 L22: 4.9864
REMARK 3 L33: 2.0510 L12: 0.2304
REMARK 3 L13: -0.0676 L23: -1.4104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0336 S12: -0.0449 S13: -0.2197
REMARK 3 S21: -0.0299 S22: -0.0389 S23: 0.1137
REMARK 3 S31: 0.0351 S32: -0.0146 S33: 0.0053
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 159 A 193
REMARK 3 ORIGIN FOR THE GROUP (A): 49.8603 50.1860 109.9050
REMARK 3 T TENSOR
REMARK 3 T11: 0.1930 T22: 0.3603
REMARK 3 T33: 0.3673 T12: -0.0549
REMARK 3 T13: 0.0161 T23: 0.1673
REMARK 3 L TENSOR
REMARK 3 L11: 26.5120 L22: 0.5449
REMARK 3 L33: 0.2987 L12: 3.7951
REMARK 3 L13: -2.8080 L23: -0.4033
REMARK 3 S TENSOR
REMARK 3 S11: 0.1716 S12: -0.7643 S13: 0.3113
REMARK 3 S21: 0.0383 S22: -0.1404 S23: 0.0364
REMARK 3 S31: -0.0257 S32: 0.1011 S33: -0.0312
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 194 A 275
REMARK 3 ORIGIN FOR THE GROUP (A): 33.9824 57.9350 94.8389
REMARK 3 T TENSOR
REMARK 3 T11: 0.0563 T22: 0.0638
REMARK 3 T33: 0.0866 T12: -0.0319
REMARK 3 T13: 0.0216 T23: 0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 4.9231 L22: 3.4208
REMARK 3 L33: 3.9341 L12: -1.0738
REMARK 3 L13: -0.7916 L23: -0.5780
REMARK 3 S TENSOR
REMARK 3 S11: 0.0943 S12: 0.3387 S13: 0.1793
REMARK 3 S21: -0.1014 S22: -0.0821 S23: -0.0997
REMARK 3 S31: -0.3252 S32: 0.1542 S33: -0.0122
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 : B 57 B 102
REMARK 3 ORIGIN FOR THE GROUP (A): 64.3807 41.4461 125.3093
REMARK 3 T TENSOR
REMARK 3 T11: 0.5645 T22: 0.5255
REMARK 3 T33: 0.4683 T12: -0.1299
REMARK 3 T13: 0.0064 T23: 0.2849
REMARK 3 L TENSOR
REMARK 3 L11: 11.1024 L22: 0.6267
REMARK 3 L33: 2.4037 L12: 0.6498
REMARK 3 L13: -0.3889 L23: 1.0721
REMARK 3 S TENSOR
REMARK 3 S11: 0.4612 S12: -1.0689 S13: -0.5920
REMARK 3 S21: 0.3372 S22: -0.3587 S23: -0.0021
REMARK 3 S31: 0.2208 S32: -0.6224 S33: -0.1026
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 103 B 148
REMARK 3 ORIGIN FOR THE GROUP (A): 75.9629 42.3240 116.5100
REMARK 3 T TENSOR
REMARK 3 T11: 0.2021 T22: 0.1170
REMARK 3 T33: 0.3724 T12: -0.0326
REMARK 3 T13: -0.1087 T23: 0.1480
REMARK 3 L TENSOR
REMARK 3 L11: 11.7857 L22: 2.9393
REMARK 3 L33: 3.7384 L12: 2.4438
REMARK 3 L13: -1.2267 L23: 0.5389
REMARK 3 S TENSOR
REMARK 3 S11: 0.4071 S12: -0.4514 S13: -0.8499
REMARK 3 S21: 0.3705 S22: -0.0499 S23: -0.4559
REMARK 3 S31: -0.0672 S32: 0.2658 S33: -0.3572
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 155 B 192
REMARK 3 ORIGIN FOR THE GROUP (A): 55.6533 44.4211 110.6443
REMARK 3 T TENSOR
REMARK 3 T11: 0.2315 T22: 0.4858
REMARK 3 T33: 0.3414 T12: -0.0273
REMARK 3 T13: 0.0268 T23: 0.1292
REMARK 3 L TENSOR
REMARK 3 L11: 13.1229 L22: 0.2592
REMARK 3 L33: 6.4152 L12: 0.6704
REMARK 3 L13: 9.1108 L23: 0.3626
REMARK 3 S TENSOR
REMARK 3 S11: 0.7004 S12: 0.0641 S13: -0.6019
REMARK 3 S21: 0.0362 S22: -0.3602 S23: -0.0938
REMARK 3 S31: 0.5864 S32: 0.1924 S33: -0.3401
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 193 B 275
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3682 48.2219 103.6480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0532 T22: 0.1002
REMARK 3 T33: 0.1127 T12: 0.0072
REMARK 3 T13: -0.0421 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 10.0800 L22: 2.7105
REMARK 3 L33: 3.8089 L12: -0.1452
REMARK 3 L13: 0.0756 L23: -0.3334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0840 S12: 0.7001 S13: -0.5486
REMARK 3 S21: -0.1543 S22: -0.0012 S23: -0.1770
REMARK 3 S31: 0.1045 S32: -0.0174 S33: -0.0829
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 71
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9679 46.5827 49.9862
REMARK 3 T TENSOR
REMARK 3 T11: 0.2798 T22: 0.4387
REMARK 3 T33: 0.3252 T12: -0.0117
REMARK 3 T13: -0.0319 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 3.5496 L22: 4.2571
REMARK 3 L33: 2.4719 L12: 2.5976
REMARK 3 L13: 0.1654 L23: 0.9017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0357 S12: 0.2460 S13: -0.5472
REMARK 3 S21: -0.2542 S22: -0.0337 S23: -0.3477
REMARK 3 S31: 0.1509 S32: 0.2863 S33: -0.0020
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 : C 72 C 162
REMARK 3 ORIGIN FOR THE GROUP (A): 66.1322 57.2630 64.5434
REMARK 3 T TENSOR
REMARK 3 T11: 0.0687 T22: 0.2045
REMARK 3 T33: 0.1279 T12: -0.0448
REMARK 3 T13: 0.0043 T23: 0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 4.4026 L22: 2.8140
REMARK 3 L33: 3.1429 L12: -0.3027
REMARK 3 L13: 0.3125 L23: 1.1961
REMARK 3 S TENSOR
REMARK 3 S11: 0.0437 S12: -0.0527 S13: -0.1298
REMARK 3 S21: 0.0360 S22: 0.0911 S23: -0.3283
REMARK 3 S31: 0.1557 S32: 0.2860 S33: -0.1347
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 163 C 196
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3139 59.9641 64.5147
REMARK 3 T TENSOR
REMARK 3 T11: 0.1016 T22: 0.3840
REMARK 3 T33: 0.4421 T12: -0.0744
REMARK 3 T13: -0.0007 T23: 0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 20.4754 L22: 0.0667
REMARK 3 L33: 1.7140 L12: -0.9611
REMARK 3 L13: -5.7848 L23: 0.3128
REMARK 3 S TENSOR
REMARK 3 S11: 0.1144 S12: -0.0542 S13: 1.1863
REMARK 3 S21: -0.0326 S22: 0.0916 S23: -0.0007
REMARK 3 S31: -0.0735 S32: 0.1563 S33: -0.2059
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 197 C 275
REMARK 3 ORIGIN FOR THE GROUP (A): 55.1733 59.3681 81.2775
REMARK 3 T TENSOR
REMARK 3 T11: 0.0313 T22: 0.2444
REMARK 3 T33: 0.0630 T12: 0.0240
REMARK 3 T13: -0.0014 T23: -0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 6.8315 L22: 3.4351
REMARK 3 L33: 6.1544 L12: 1.2634
REMARK 3 L13: -1.0744 L23: -0.8386
REMARK 3 S TENSOR
REMARK 3 S11: 0.0157 S12: -0.6840 S13: 0.0023
REMARK 3 S21: 0.2931 S22: -0.1232 S23: 0.1070
REMARK 3 S31: -0.1231 S32: 0.1947 S33: 0.1075
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 : D 55 D 113
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3244 56.8496 46.1470
REMARK 3 T TENSOR
REMARK 3 T11: 0.5358 T22: 0.6107
REMARK 3 T33: 0.3389 T12: 0.1537
REMARK 3 T13: 0.1625 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 3.7109 L22: 4.3844
REMARK 3 L33: 4.7629 L12: 1.4574
REMARK 3 L13: -2.8319 L23: -2.2883
REMARK 3 S TENSOR
REMARK 3 S11: 0.4465 S12: 0.9544 S13: 0.5104
REMARK 3 S21: -0.9230 S22: -0.1473 S23: -0.3323
REMARK 3 S31: -0.4233 S32: -0.1115 S33: -0.2992
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 : D 114 D 149
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3135 52.7357 54.2194
REMARK 3 T TENSOR
REMARK 3 T11: 0.1256 T22: 0.1915
REMARK 3 T33: 0.1197 T12: -0.0178
REMARK 3 T13: 0.0100 T23: -0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 5.4018 L22: 4.9908
REMARK 3 L33: 5.1004 L12: -0.8435
REMARK 3 L13: 0.7431 L23: 0.1338
REMARK 3 S TENSOR
REMARK 3 S11: 0.1631 S12: 0.2047 S13: -0.0184
REMARK 3 S21: -0.3275 S22: -0.0323 S23: 0.3919
REMARK 3 S31: -0.0411 S32: -0.3266 S33: -0.1308
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 : D 150 D 192
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7691 53.8343 58.9334
REMARK 3 T TENSOR
REMARK 3 T11: 0.1986 T22: 0.2745
REMARK 3 T33: 0.1835 T12: -0.0104
REMARK 3 T13: 0.0678 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 7.1594 L22: 0.9622
REMARK 3 L33: 7.5276 L12: -0.0914
REMARK 3 L13: 6.5803 L23: -0.4461
REMARK 3 S TENSOR
REMARK 3 S11: 0.3641 S12: -0.0539 S13: -0.3376
REMARK 3 S21: -0.2669 S22: -0.0212 S23: 0.0585
REMARK 3 S31: 0.3872 S32: -0.1876 S33: -0.3430
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 193 D 276
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3697 55.6413 69.0508
REMARK 3 T TENSOR
REMARK 3 T11: 0.0443 T22: 0.0894
REMARK 3 T33: 0.0481 T12: -0.0110
REMARK 3 T13: -0.0208 T23: 0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 6.4347 L22: 2.5343
REMARK 3 L33: 4.1123 L12: 0.0202
REMARK 3 L13: -0.1492 L23: 0.1694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.2716 S13: -0.0677
REMARK 3 S21: 0.1880 S22: -0.0292 S23: 0.0147
REMARK 3 S31: 0.2145 S32: -0.2277 S33: 0.0326
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES WITH TLS ADDED. THE FOLLOWING RESIDUE RANGES
REMARK 3 ARE DISORDERED AND EXCLUDED FROM MODEL: CHAIN A RESIDUES 1-3, 23,
REMARK 3 48-57, 170-179, 276-285. CHAIN B RESIDUES 1-56, 78-97, 149-154,
REMARK 3 170-180, 276-285. CHAIN C RESIDUES 1, 170-179, 243, 277-285.
REMARK 3 CHAIN D RESIDUES 1-55, 83-92, 107-112, 170-180, 277-285.
REMARK 4
REMARK 4 2Y4P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1290046689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : SI(111) CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41340
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 62.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: PDB ENTRY 2W4J
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.0, 0.1 M MGCL2, 15%
REMARK 280 (W/V) PEG 4000, 0.5 MM AMPPCP, 0.5 MM PMSF.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.85000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR A 2
REMARK 465 VAL A 3
REMARK 465 GLN A 23
REMARK 465 ARG A 48
REMARK 465 THR A 49
REMARK 465 LYS A 50
REMARK 465 SER A 51
REMARK 465 SER A 52
REMARK 465 ARG A 53
REMARK 465 ARG A 54
REMARK 465 GLY A 55
REMARK 465 VAL A 56
REMARK 465 SER A 57
REMARK 465 PHE A 170
REMARK 465 GLY A 171
REMARK 465 ASN A 172
REMARK 465 GLU A 173
REMARK 465 PHE A 174
REMARK 465 LYS A 175
REMARK 465 ASN A 176
REMARK 465 ILE A 177
REMARK 465 PHE A 178
REMARK 465 GLY A 179
REMARK 465 LYS A 276
REMARK 465 PRO A 277
REMARK 465 LYS A 278
REMARK 465 ASP A 279
REMARK 465 THR A 280
REMARK 465 GLN A 281
REMARK 465 GLN A 282
REMARK 465 ALA A 283
REMARK 465 LEU A 284
REMARK 465 SER A 285
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 VAL B 3
REMARK 465 PHE B 4
REMARK 465 ARG B 5
REMARK 465 GLN B 6
REMARK 465 GLU B 7
REMARK 465 ASN B 8
REMARK 465 VAL B 9
REMARK 465 ASP B 10
REMARK 465 ASP B 11
REMARK 465 TYR B 12
REMARK 465 TYR B 13
REMARK 465 ASP B 14
REMARK 465 THR B 15
REMARK 465 GLY B 16
REMARK 465 GLU B 17
REMARK 465 GLU B 18
REMARK 465 LEU B 19
REMARK 465 GLY B 20
REMARK 465 SER B 21
REMARK 465 GLY B 22
REMARK 465 GLN B 23
REMARK 465 PHE B 24
REMARK 465 ALA B 25
REMARK 465 VAL B 26
REMARK 465 VAL B 27
REMARK 465 LYS B 28
REMARK 465 LYS B 29
REMARK 465 CYS B 30
REMARK 465 ARG B 31
REMARK 465 GLU B 32
REMARK 465 LYS B 33
REMARK 465 SER B 34
REMARK 465 THR B 35
REMARK 465 GLY B 36
REMARK 465 LEU B 37
REMARK 465 GLN B 38
REMARK 465 TYR B 39
REMARK 465 ALA B 40
REMARK 465 ALA B 41
REMARK 465 LYS B 42
REMARK 465 PHE B 43
REMARK 465 ILE B 44
REMARK 465 LYS B 45
REMARK 465 LYS B 46
REMARK 465 ARG B 47
REMARK 465 ARG B 48
REMARK 465 THR B 49
REMARK 465 LYS B 50
REMARK 465 SER B 51
REMARK 465 SER B 52
REMARK 465 ARG B 53
REMARK 465 ARG B 54
REMARK 465 GLY B 55
REMARK 465 VAL B 56
REMARK 465 HIS B 80
REMARK 465 GLU B 81
REMARK 465 VAL B 82
REMARK 465 TYR B 83
REMARK 465 GLU B 84
REMARK 465 ASN B 85
REMARK 465 LYS B 86
REMARK 465 THR B 87
REMARK 465 ASP B 88
REMARK 465 VAL B 89
REMARK 465 ILE B 90
REMARK 465 LEU B 91
REMARK 465 ILE B 92
REMARK 465 LEU B 93
REMARK 465 GLU B 94
REMARK 465 LEU B 95
REMARK 465 VAL B 96
REMARK 465 ALA B 97
REMARK 465 ASP B 149
REMARK 465 ARG B 150
REMARK 465 ASN B 151
REMARK 465 VAL B 152
REMARK 465 PRO B 153
REMARK 465 LYS B 154
REMARK 465 PHE B 170
REMARK 465 GLY B 171
REMARK 465 ASN B 172
REMARK 465 GLU B 173
REMARK 465 PHE B 174
REMARK 465 LYS B 175
REMARK 465 ASN B 176
REMARK 465 ILE B 177
REMARK 465 PHE B 178
REMARK 465 GLY B 179
REMARK 465 THR B 180
REMARK 465 LYS B 276
REMARK 465 PRO B 277
REMARK 465 LYS B 278
REMARK 465 ASP B 279
REMARK 465 THR B 280
REMARK 465 GLN B 281
REMARK 465 GLN B 282
REMARK 465 ALA B 283
REMARK 465 LEU B 284
REMARK 465 SER B 285
REMARK 465 MET C 1
REMARK 465 PHE C 170
REMARK 465 GLY C 171
REMARK 465 ASN C 172
REMARK 465 GLU C 173
REMARK 465 PHE C 174
REMARK 465 LYS C 175
REMARK 465 ASN C 176
REMARK 465 ILE C 177
REMARK 465 PHE C 178
REMARK 465 GLY C 179
REMARK 465 ASN C 243
REMARK 465 PRO C 277
REMARK 465 LYS C 278
REMARK 465 ASP C 279
REMARK 465 THR C 280
REMARK 465 GLN C 281
REMARK 465 GLN C 282
REMARK 465 ALA C 283
REMARK 465 LEU C 284
REMARK 465 SER C 285
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 VAL D 3
REMARK 465 PHE D 4
REMARK 465 ARG D 5
REMARK 465 GLN D 6
REMARK 465 GLU D 7
REMARK 465 ASN D 8
REMARK 465 VAL D 9
REMARK 465 ASP D 10
REMARK 465 ASP D 11
REMARK 465 TYR D 12
REMARK 465 TYR D 13
REMARK 465 ASP D 14
REMARK 465 THR D 15
REMARK 465 GLY D 16
REMARK 465 GLU D 17
REMARK 465 GLU D 18
REMARK 465 LEU D 19
REMARK 465 GLY D 20
REMARK 465 SER D 21
REMARK 465 GLY D 22
REMARK 465 GLN D 23
REMARK 465 PHE D 24
REMARK 465 ALA D 25
REMARK 465 VAL D 26
REMARK 465 VAL D 27
REMARK 465 LYS D 28
REMARK 465 LYS D 29
REMARK 465 CYS D 30
REMARK 465 ARG D 31
REMARK 465 GLU D 32
REMARK 465 LYS D 33
REMARK 465 SER D 34
REMARK 465 THR D 35
REMARK 465 GLY D 36
REMARK 465 LEU D 37
REMARK 465 GLN D 38
REMARK 465 TYR D 39
REMARK 465 ALA D 40
REMARK 465 ALA D 41
REMARK 465 LYS D 42
REMARK 465 PHE D 43
REMARK 465 ILE D 44
REMARK 465 LYS D 45
REMARK 465 LYS D 46
REMARK 465 ARG D 47
REMARK 465 ARG D 48
REMARK 465 THR D 49
REMARK 465 LYS D 50
REMARK 465 SER D 51
REMARK 465 SER D 52
REMARK 465 ARG D 53
REMARK 465 ARG D 54
REMARK 465 GLY D 55
REMARK 465 TYR D 83
REMARK 465 GLU D 84
REMARK 465 ASN D 85
REMARK 465 LYS D 86
REMARK 465 THR D 87
REMARK 465 ASP D 88
REMARK 465 VAL D 89
REMARK 465 ILE D 90
REMARK 465 LEU D 91
REMARK 465 ILE D 92
REMARK 465 GLU D 107
REMARK 465 LYS D 108
REMARK 465 GLU D 109
REMARK 465 SER D 110
REMARK 465 LEU D 111
REMARK 465 THR D 112
REMARK 465 PHE D 170
REMARK 465 GLY D 171
REMARK 465 ASN D 172
REMARK 465 GLU D 173
REMARK 465 PHE D 174
REMARK 465 LYS D 175
REMARK 465 ASN D 176
REMARK 465 ILE D 177
REMARK 465 PHE D 178
REMARK 465 GLY D 179
REMARK 465 THR D 180
REMARK 465 PRO D 277
REMARK 465 LYS D 278
REMARK 465 ASP D 279
REMARK 465 THR D 280
REMARK 465 GLN D 281
REMARK 465 GLN D 282
REMARK 465 ALA D 283
REMARK 465 LEU D 284
REMARK 465 SER D 285
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 4 N
REMARK 470 SER A 21 OG
REMARK 470 GLU A 59 CG CD OE1 OE2
REMARK 470 GLU A 109 CG CD OE1 OE2
REMARK 470 LYS A 222 CG CD CE NZ
REMARK 470 ARG B 58 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 59 CG CD OE1 OE2
REMARK 470 GLU B 109 CG CD OE1 OE2
REMARK 470 SER B 110 OG
REMARK 470 GLU C 18 CG CD OE1 OE2
REMARK 470 GLN C 23 CG CD OE1 NE2
REMARK 470 VAL C 89 CG1 CG2
REMARK 470 LYS C 261 CG CD CE NZ
REMARK 470 LYS C 276 CG CD CE NZ
REMARK 470 ARG D 58 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 82 CG1 CG2
REMARK 470 LEU D 95 CG CD1 CD2
REMARK 470 LYS D 154 CG CD CE NZ
REMARK 470 ARG D 156 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 2009 O HOH C 2010 0.15
REMARK 500 O LEU C 133 NZ LYS C 167 0.33
REMARK 500 C LEU C 133 NZ LYS C 167 0.94
REMARK 500 OE1 GLU C 32 OG1 THR C 35 1.16
REMARK 500 O LEU C 133 CE LYS C 167 1.28
REMARK 500 O ILE B 209 O SER B 212 1.43
REMARK 500 OE1 GLU B 70 NZ LYS B 167 1.49
REMARK 500 OH TYR C 13 OE1 GLU C 81 1.56
REMARK 500 OE2 GLU D 70 NZ LYS D 167 1.61
REMARK 500 O TYR D 129 OG SER D 132 1.62
REMARK 500 O ILE D 209 O SER D 212 1.65
REMARK 500 N THR B 112 OE2 GLU B 115 1.67
REMARK 500 OH TYR A 13 OE1 GLU A 81 1.70
REMARK 500 OE1 GLU B 113 OG SER B 245 1.71
REMARK 500 O ARG D 58 O HOH D 2001 1.74
REMARK 500 C GLY C 22 O HOH C 2007 1.76
REMARK 500 N THR C 2 OE2 GLU C 62 1.79
REMARK 500 O ILE A 209 O SER A 212 1.87
REMARK 500 N GLN C 134 NZ LYS C 167 1.87
REMARK 500 CD GLU B 70 NZ LYS B 167 1.88
REMARK 500 CG2 THR B 78 O HOH B 2004 1.92
REMARK 500 O GLU D 59 O HOH D 2001 1.93
REMARK 500 OE2 GLU B 70 NZ LYS B 167 1.93
REMARK 500 O ILE C 275 O HOH C 2058 1.96
REMARK 500 OE2 GLU A 64 O HOH A 2009 1.96
REMARK 500 CB GLU D 62 O HOH D 2001 1.97
REMARK 500 CD PRO D 181 O HOH D 2020 1.99
REMARK 500 N GLN C 23 O HOH C 2007 1.99
REMARK 500 OE1 GLU C 70 O HOH C 2017 2.00
REMARK 500 CG2 THR D 78 OE2 GLU D 94 2.03
REMARK 500 CB GLN D 223 O HOH D 2029 2.04
REMARK 500 OG1 THR D 221 OE1 GLU D 224 2.05
REMARK 500 NH1 ARG D 254 O HOH D 2039 2.05
REMARK 500 N GLU D 62 O HOH D 2001 2.12
REMARK 500 OE2 GLU A 187 O HOH A 2034 2.13
REMARK 500 CA GLY C 22 O HOH C 2007 2.13
REMARK 500 O ILE C 209 O SER C 212 2.14
REMARK 500 O ASP C 103 OE1 GLU C 107 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER C 51 O GLY D 219 2646 1.37
REMARK 500 O SER A 34 NE2 GLN A 271 2647 1.40
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 SER C 66 N SER C 66 CA -0.184
REMARK 500 VAL C 76 N VAL C 76 CA -0.169
REMARK 500 LEU C 91 CA LEU C 91 C -0.258
REMARK 500 ILE C 275 C LYS C 276 N -0.418
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU C 91 CA - C - O ANGL. DEV. = -25.0 DEGREES
REMARK 500 LEU C 91 CA - C - N ANGL. DEV. = 15.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 138 -0.99 76.73
REMARK 500 ASP A 161 74.81 62.98
REMARK 500 PHE A 162 30.34 -97.59
REMARK 500 ASP B 161 80.00 58.39
REMARK 500 TRP B 274 -8.87 -56.15
REMARK 500 PHE C 138 -1.43 81.59
REMARK 500 ASP C 139 34.62 -141.33
REMARK 500 ASP C 161 81.60 77.31
REMARK 500 SER C 212 -166.42 -127.51
REMARK 500 LEU C 256 59.32 -90.47
REMARK 500 PHE D 104 5.06 -63.81
REMARK 500 PHE D 138 -5.00 71.32
REMARK 500 ASN D 151 56.54 -96.89
REMARK 500 ASP D 161 73.54 53.89
REMARK 500 PHE D 162 30.58 -96.92
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 SER C 66 11.35
REMARK 500 VAL C 76 11.70
REMARK 500 ILE C 275 -10.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2001 DISTANCE = 6.84 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YAK RELATED DB: PDB
REMARK 900 STRUCTURE OF DEATH-ASSOCIATED PROTEIN KINASE 1 (DAPK1) IN COMPLEX
REMARK 900 WITH A RUTHENIUM OCTASPORINE LIGAND (OSV)
REMARK 900 RELATED ID: 1JKK RELATED DB: PDB
REMARK 900 2.4A X-RAY STRUCTURE OF TERNARY COMPLEX OF A CATALYTICDOMAIN OF
REMARK 900 DEATH-ASSOCIATED PROTEIN KINASE WITH ATPANALOGUE AND MG.
REMARK 900 RELATED ID: 1P4F RELATED DB: PDB
REMARK 900 DEATH ASSOCIATED PROTEIN KINASE CATALYTIC DOMAIN WITH
REMARK 900 BOUNDINHIBITOR FRAGMENT
REMARK 900 RELATED ID: 2Y0A RELATED DB: PDB
REMARK 900 STRUCTURE OF DAPK1 CONSTRUCT RESIDUES 1-304
REMARK 900 RELATED ID: 2W4J RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF A DAP-KINASE 2-277
REMARK 900 RELATED ID: 2X0G RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF A DAP-KINASE CALMODULIN COMPLEX
REMARK 900 RELATED ID: 2Y4V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CALMODULIN IN COMPLEX WITH A DAP KINASE-
REMARK 900 1 MUTANT (W305Y) PEPTIDE
REMARK 900 RELATED ID: 3ZXT RELATED DB: PDB
REMARK 900 DIMERIC STRUCTURE OF DAPK-1 CATALYTIC DOMAIN IN COMPLEX WITH AMPPCP-
REMARK 900 MG
REMARK 900 RELATED ID: 2W4K RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF A DAP-KINASE 2-302
REMARK 900 RELATED ID: 1JKT RELATED DB: PDB
REMARK 900 TETRAGONAL CRYSTAL FORM OF A CATALYTIC DOMAIN OF DEATH -ASSOCIATED
REMARK 900 PROTEIN KINASE
REMARK 900 RELATED ID: 1IG1 RELATED DB: PDB
REMARK 900 1.8A X-RAY STRUCTURE OF TERNARY COMPLEX OF A CATALYTICDOMAIN OF
REMARK 900 DEATH-ASSOCIATED PROTEIN KINASE WITH ATPANALOGUE AND MN.
REMARK 900 RELATED ID: 2XUU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A DAP-KINASE 1 MUTANT
REMARK 900 RELATED ID: 1JKS RELATED DB: PDB
REMARK 900 1.5A X-RAY STRUCTURE OF APO FORM OF A CATALYTIC DOMAIN OFDEATH-
REMARK 900 ASSOCIATED PROTEIN KINASE
REMARK 900 RELATED ID: 1JKL RELATED DB: PDB
REMARK 900 1.6A X-RAY STRUCTURE OF BINARY COMPLEX OF A CATALYTICDOMAIN OF
REMARK 900 DEATH-ASSOCIATED PROTEIN KINASE WITH ATP ANALOGUE
REMARK 900 RELATED ID: 2XZS RELATED DB: PDB
REMARK 900 DEATH ASSOCIATED PROTEIN KINASE 1 RESIDUES 1-312
DBREF 2Y4P A 1 285 UNP P53355 DAPK1_HUMAN 1 285
DBREF 2Y4P B 1 285 UNP P53355 DAPK1_HUMAN 1 285
DBREF 2Y4P C 1 285 UNP P53355 DAPK1_HUMAN 1 285
DBREF 2Y4P D 1 285 UNP P53355 DAPK1_HUMAN 1 285
SEQRES 1 A 285 MET THR VAL PHE ARG GLN GLU ASN VAL ASP ASP TYR TYR
SEQRES 2 A 285 ASP THR GLY GLU GLU LEU GLY SER GLY GLN PHE ALA VAL
SEQRES 3 A 285 VAL LYS LYS CYS ARG GLU LYS SER THR GLY LEU GLN TYR
SEQRES 4 A 285 ALA ALA LYS PHE ILE LYS LYS ARG ARG THR LYS SER SER
SEQRES 5 A 285 ARG ARG GLY VAL SER ARG GLU ASP ILE GLU ARG GLU VAL
SEQRES 6 A 285 SER ILE LEU LYS GLU ILE GLN HIS PRO ASN VAL ILE THR
SEQRES 7 A 285 LEU HIS GLU VAL TYR GLU ASN LYS THR ASP VAL ILE LEU
SEQRES 8 A 285 ILE LEU GLU LEU VAL ALA GLY GLY GLU LEU PHE ASP PHE
SEQRES 9 A 285 LEU ALA GLU LYS GLU SER LEU THR GLU GLU GLU ALA THR
SEQRES 10 A 285 GLU PHE LEU LYS GLN ILE LEU ASN GLY VAL TYR TYR LEU
SEQRES 11 A 285 HIS SER LEU GLN ILE ALA HIS PHE ASP LEU LYS PRO GLU
SEQRES 12 A 285 ASN ILE MET LEU LEU ASP ARG ASN VAL PRO LYS PRO ARG
SEQRES 13 A 285 ILE LYS ILE ILE ASP PHE GLY LEU ALA HIS LYS ILE ASP
SEQRES 14 A 285 PHE GLY ASN GLU PHE LYS ASN ILE PHE GLY THR PRO GLU
SEQRES 15 A 285 PHE VAL ALA PRO GLU ILE VAL ASN TYR GLU PRO LEU GLY
SEQRES 16 A 285 LEU GLU ALA ASP MET TRP SER ILE GLY VAL ILE THR TYR
SEQRES 17 A 285 ILE LEU LEU SER GLY ALA SER PRO PHE LEU GLY ASP THR
SEQRES 18 A 285 LYS GLN GLU THR LEU ALA ASN VAL SER ALA VAL ASN TYR
SEQRES 19 A 285 GLU PHE GLU ASP GLU TYR PHE SER ASN THR SER ALA LEU
SEQRES 20 A 285 ALA LYS ASP PHE ILE ARG ARG LEU LEU VAL LYS ASP PRO
SEQRES 21 A 285 LYS LYS ARG MET THR ILE GLN ASP SER LEU GLN HIS PRO
SEQRES 22 A 285 TRP ILE LYS PRO LYS ASP THR GLN GLN ALA LEU SER
SEQRES 1 B 285 MET THR VAL PHE ARG GLN GLU ASN VAL ASP ASP TYR TYR
SEQRES 2 B 285 ASP THR GLY GLU GLU LEU GLY SER GLY GLN PHE ALA VAL
SEQRES 3 B 285 VAL LYS LYS CYS ARG GLU LYS SER THR GLY LEU GLN TYR
SEQRES 4 B 285 ALA ALA LYS PHE ILE LYS LYS ARG ARG THR LYS SER SER
SEQRES 5 B 285 ARG ARG GLY VAL SER ARG GLU ASP ILE GLU ARG GLU VAL
SEQRES 6 B 285 SER ILE LEU LYS GLU ILE GLN HIS PRO ASN VAL ILE THR
SEQRES 7 B 285 LEU HIS GLU VAL TYR GLU ASN LYS THR ASP VAL ILE LEU
SEQRES 8 B 285 ILE LEU GLU LEU VAL ALA GLY GLY GLU LEU PHE ASP PHE
SEQRES 9 B 285 LEU ALA GLU LYS GLU SER LEU THR GLU GLU GLU ALA THR
SEQRES 10 B 285 GLU PHE LEU LYS GLN ILE LEU ASN GLY VAL TYR TYR LEU
SEQRES 11 B 285 HIS SER LEU GLN ILE ALA HIS PHE ASP LEU LYS PRO GLU
SEQRES 12 B 285 ASN ILE MET LEU LEU ASP ARG ASN VAL PRO LYS PRO ARG
SEQRES 13 B 285 ILE LYS ILE ILE ASP PHE GLY LEU ALA HIS LYS ILE ASP
SEQRES 14 B 285 PHE GLY ASN GLU PHE LYS ASN ILE PHE GLY THR PRO GLU
SEQRES 15 B 285 PHE VAL ALA PRO GLU ILE VAL ASN TYR GLU PRO LEU GLY
SEQRES 16 B 285 LEU GLU ALA ASP MET TRP SER ILE GLY VAL ILE THR TYR
SEQRES 17 B 285 ILE LEU LEU SER GLY ALA SER PRO PHE LEU GLY ASP THR
SEQRES 18 B 285 LYS GLN GLU THR LEU ALA ASN VAL SER ALA VAL ASN TYR
SEQRES 19 B 285 GLU PHE GLU ASP GLU TYR PHE SER ASN THR SER ALA LEU
SEQRES 20 B 285 ALA LYS ASP PHE ILE ARG ARG LEU LEU VAL LYS ASP PRO
SEQRES 21 B 285 LYS LYS ARG MET THR ILE GLN ASP SER LEU GLN HIS PRO
SEQRES 22 B 285 TRP ILE LYS PRO LYS ASP THR GLN GLN ALA LEU SER
SEQRES 1 C 285 MET THR VAL PHE ARG GLN GLU ASN VAL ASP ASP TYR TYR
SEQRES 2 C 285 ASP THR GLY GLU GLU LEU GLY SER GLY GLN PHE ALA VAL
SEQRES 3 C 285 VAL LYS LYS CYS ARG GLU LYS SER THR GLY LEU GLN TYR
SEQRES 4 C 285 ALA ALA LYS PHE ILE LYS LYS ARG ARG THR LYS SER SER
SEQRES 5 C 285 ARG ARG GLY VAL SER ARG GLU ASP ILE GLU ARG GLU VAL
SEQRES 6 C 285 SER ILE LEU LYS GLU ILE GLN HIS PRO ASN VAL ILE THR
SEQRES 7 C 285 LEU HIS GLU VAL TYR GLU ASN LYS THR ASP VAL ILE LEU
SEQRES 8 C 285 ILE LEU GLU LEU VAL ALA GLY GLY GLU LEU PHE ASP PHE
SEQRES 9 C 285 LEU ALA GLU LYS GLU SER LEU THR GLU GLU GLU ALA THR
SEQRES 10 C 285 GLU PHE LEU LYS GLN ILE LEU ASN GLY VAL TYR TYR LEU
SEQRES 11 C 285 HIS SER LEU GLN ILE ALA HIS PHE ASP LEU LYS PRO GLU
SEQRES 12 C 285 ASN ILE MET LEU LEU ASP ARG ASN VAL PRO LYS PRO ARG
SEQRES 13 C 285 ILE LYS ILE ILE ASP PHE GLY LEU ALA HIS LYS ILE ASP
SEQRES 14 C 285 PHE GLY ASN GLU PHE LYS ASN ILE PHE GLY THR PRO GLU
SEQRES 15 C 285 PHE VAL ALA PRO GLU ILE VAL ASN TYR GLU PRO LEU GLY
SEQRES 16 C 285 LEU GLU ALA ASP MET TRP SER ILE GLY VAL ILE THR TYR
SEQRES 17 C 285 ILE LEU LEU SER GLY ALA SER PRO PHE LEU GLY ASP THR
SEQRES 18 C 285 LYS GLN GLU THR LEU ALA ASN VAL SER ALA VAL ASN TYR
SEQRES 19 C 285 GLU PHE GLU ASP GLU TYR PHE SER ASN THR SER ALA LEU
SEQRES 20 C 285 ALA LYS ASP PHE ILE ARG ARG LEU LEU VAL LYS ASP PRO
SEQRES 21 C 285 LYS LYS ARG MET THR ILE GLN ASP SER LEU GLN HIS PRO
SEQRES 22 C 285 TRP ILE LYS PRO LYS ASP THR GLN GLN ALA LEU SER
SEQRES 1 D 285 MET THR VAL PHE ARG GLN GLU ASN VAL ASP ASP TYR TYR
SEQRES 2 D 285 ASP THR GLY GLU GLU LEU GLY SER GLY GLN PHE ALA VAL
SEQRES 3 D 285 VAL LYS LYS CYS ARG GLU LYS SER THR GLY LEU GLN TYR
SEQRES 4 D 285 ALA ALA LYS PHE ILE LYS LYS ARG ARG THR LYS SER SER
SEQRES 5 D 285 ARG ARG GLY VAL SER ARG GLU ASP ILE GLU ARG GLU VAL
SEQRES 6 D 285 SER ILE LEU LYS GLU ILE GLN HIS PRO ASN VAL ILE THR
SEQRES 7 D 285 LEU HIS GLU VAL TYR GLU ASN LYS THR ASP VAL ILE LEU
SEQRES 8 D 285 ILE LEU GLU LEU VAL ALA GLY GLY GLU LEU PHE ASP PHE
SEQRES 9 D 285 LEU ALA GLU LYS GLU SER LEU THR GLU GLU GLU ALA THR
SEQRES 10 D 285 GLU PHE LEU LYS GLN ILE LEU ASN GLY VAL TYR TYR LEU
SEQRES 11 D 285 HIS SER LEU GLN ILE ALA HIS PHE ASP LEU LYS PRO GLU
SEQRES 12 D 285 ASN ILE MET LEU LEU ASP ARG ASN VAL PRO LYS PRO ARG
SEQRES 13 D 285 ILE LYS ILE ILE ASP PHE GLY LEU ALA HIS LYS ILE ASP
SEQRES 14 D 285 PHE GLY ASN GLU PHE LYS ASN ILE PHE GLY THR PRO GLU
SEQRES 15 D 285 PHE VAL ALA PRO GLU ILE VAL ASN TYR GLU PRO LEU GLY
SEQRES 16 D 285 LEU GLU ALA ASP MET TRP SER ILE GLY VAL ILE THR TYR
SEQRES 17 D 285 ILE LEU LEU SER GLY ALA SER PRO PHE LEU GLY ASP THR
SEQRES 18 D 285 LYS GLN GLU THR LEU ALA ASN VAL SER ALA VAL ASN TYR
SEQRES 19 D 285 GLU PHE GLU ASP GLU TYR PHE SER ASN THR SER ALA LEU
SEQRES 20 D 285 ALA LYS ASP PHE ILE ARG ARG LEU LEU VAL LYS ASP PRO
SEQRES 21 D 285 LYS LYS ARG MET THR ILE GLN ASP SER LEU GLN HIS PRO
SEQRES 22 D 285 TRP ILE LYS PRO LYS ASP THR GLN GLN ALA LEU SER
FORMUL 5 HOH *175(H2 O)
HELIX 1 1 ASN A 8 ASP A 11 5 4
HELIX 2 2 ARG A 58 ILE A 71 1 14
HELIX 3 3 GLU A 100 GLU A 107 1 8
HELIX 4 4 THR A 112 LEU A 133 1 22
HELIX 5 5 LYS A 141 GLU A 143 5 3
HELIX 6 6 ASP A 161 ALA A 165 5 5
HELIX 7 7 ALA A 185 ASN A 190 1 6
HELIX 8 8 LEU A 196 LEU A 211 1 16
HELIX 9 9 THR A 221 VAL A 232 1 12
HELIX 10 10 GLU A 237 SER A 242 1 6
HELIX 11 11 SER A 245 ARG A 254 1 10
HELIX 12 12 ASP A 259 ARG A 263 5 5
HELIX 13 13 THR A 265 HIS A 272 1 8
HELIX 14 14 ARG B 58 ILE B 71 1 14
HELIX 15 15 GLU B 100 LEU B 105 1 6
HELIX 16 16 THR B 112 LEU B 133 1 22
HELIX 17 17 LYS B 141 GLU B 143 5 3
HELIX 18 18 ALA B 185 ASN B 190 1 6
HELIX 19 19 LEU B 196 LEU B 211 1 16
HELIX 20 20 THR B 221 VAL B 232 1 12
HELIX 21 21 GLU B 237 SER B 242 1 6
HELIX 22 22 SER B 245 LEU B 256 1 12
HELIX 23 23 THR B 265 LEU B 270 1 6
HELIX 24 24 ASN C 8 ASP C 11 5 4
HELIX 25 25 SER C 57 ILE C 71 1 15
HELIX 26 26 GLU C 100 ALA C 106 1 7
HELIX 27 27 THR C 112 LEU C 133 1 22
HELIX 28 28 LYS C 141 GLU C 143 5 3
HELIX 29 29 THR C 180 VAL C 184 5 5
HELIX 30 30 ALA C 185 ASN C 190 1 6
HELIX 31 31 LEU C 196 SER C 212 1 17
HELIX 32 32 THR C 221 VAL C 232 1 12
HELIX 33 33 GLU C 237 SER C 242 1 6
HELIX 34 34 SER C 245 LEU C 256 1 12
HELIX 35 35 ASP C 259 ARG C 263 5 5
HELIX 36 36 THR C 265 HIS C 272 1 8
HELIX 37 37 SER D 57 ILE D 71 1 15
HELIX 38 38 PHE D 102 ALA D 106 5 5
HELIX 39 39 GLU D 113 LEU D 133 1 21
HELIX 40 40 LYS D 141 GLU D 143 5 3
HELIX 41 41 ALA D 185 ASN D 190 1 6
HELIX 42 42 LEU D 196 SER D 212 1 17
HELIX 43 43 THR D 221 VAL D 232 1 12
HELIX 44 44 GLU D 237 SER D 242 1 6
HELIX 45 45 SER D 245 LEU D 256 1 12
HELIX 46 46 ASP D 259 ARG D 263 5 5
HELIX 47 47 THR D 265 GLN D 271 1 7
SHEET 1 AA 5 TYR A 13 SER A 21 0
SHEET 2 AA 5 ALA A 25 GLU A 32 -1 O VAL A 27 N LEU A 19
SHEET 3 AA 5 GLN A 38 LYS A 45 -1 O TYR A 39 N CYS A 30
SHEET 4 AA 5 ASP A 88 LEU A 93 -1 O VAL A 89 N ILE A 44
SHEET 5 AA 5 LEU A 79 GLU A 84 -1 N HIS A 80 O ILE A 92
SHEET 1 AB 2 ILE A 135 ALA A 136 0
SHEET 2 AB 2 HIS A 166 LYS A 167 -1 O HIS A 166 N ALA A 136
SHEET 1 AC 2 ILE A 145 LEU A 147 0
SHEET 2 AC 2 ILE A 157 ILE A 159 -1 O LYS A 158 N MET A 146
SHEET 1 BA 2 ILE B 135 ALA B 136 0
SHEET 2 BA 2 HIS B 166 LYS B 167 -1 O HIS B 166 N ALA B 136
SHEET 1 BB 2 ILE B 145 LEU B 147 0
SHEET 2 BB 2 ILE B 157 ILE B 159 -1 O LYS B 158 N MET B 146
SHEET 1 CA 5 TYR C 13 SER C 21 0
SHEET 2 CA 5 ALA C 25 GLU C 32 -1 O VAL C 27 N LEU C 19
SHEET 3 CA 5 GLN C 38 LYS C 45 -1 O TYR C 39 N CYS C 30
SHEET 4 CA 5 ASP C 88 GLU C 94 -1 O VAL C 89 N ILE C 44
SHEET 5 CA 5 LEU C 79 GLU C 84 -1 N HIS C 80 O ILE C 92
SHEET 1 CB 2 ILE C 135 ALA C 136 0
SHEET 2 CB 2 HIS C 166 LYS C 167 -1 O HIS C 166 N ALA C 136
SHEET 1 CC 2 ILE C 145 LEU C 147 0
SHEET 2 CC 2 ILE C 157 ILE C 159 -1 O LYS C 158 N MET C 146
SHEET 1 DA 2 ILE D 135 ALA D 136 0
SHEET 2 DA 2 HIS D 166 LYS D 167 -1 O HIS D 166 N ALA D 136
SHEET 1 DB 2 ILE D 145 LEU D 147 0
SHEET 2 DB 2 ILE D 157 ILE D 159 -1 O LYS D 158 N MET D 146
CRYST1 83.940 73.700 120.280 90.00 101.24 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011913 0.000000 0.002368 0.00000
SCALE2 0.000000 0.013569 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008477 0.00000
MTRIX1 1 -0.997100 -0.075970 -0.001111 93.57000 1
MTRIX2 1 -0.068370 0.890800 0.449100 -27.90000 1
MTRIX3 1 -0.033130 0.447900 -0.893500 142.10000 1
MTRIX1 2 0.821600 -0.049150 0.567900 -15.21000 1
MTRIX2 2 -0.381300 -0.788000 0.483500 74.53000 1
MTRIX3 2 0.423700 -0.613800 -0.666200 168.60000 1
MTRIX1 3 -0.830800 0.188900 -0.523500 140.30000 1
MTRIX2 3 0.313000 -0.619200 -0.720200 139.40000 1
MTRIX3 3 -0.460200 -0.762200 0.455300 118.50000 1
(ATOM LINES ARE NOT SHOWN.)
END
