HEADER MOTOR PROTEIN 13-JUL-15 5CJ4
TITLE CRYSTAL STRUCTURE OF AMINO ACIDS 1562-1622 OF MYH7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XRCC4-MYH7-(1562-1622) CHIMERA PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP Q13426 RESIDUES 2-144, UNP P12883 1562-1622;
COMPND 5 SYNONYM: X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 4,MYOSIN HEAVY
COMPND 6 CHAIN 7,MYOSIN HEAVY CHAIN SLOW ISOFORM,MYHC-SLOW,MYOSIN HEAVY CHAIN,
COMPND 7 CARDIAC MUSCLE BETA ISOFORM,MYHC-BETA;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: LYSINES WERE REDUCTIVELY ALKYLATED TO DIMETHYLLYSINE.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: XRCC4, MYH7, MYHCB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS MYOSIN, COILED-COIL, MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.E.KORKMAZ,K.C.TAYLOR,M.P.ANDREAS,G.AJAY,N.T.HEINZE,Q.CUI,I.RAYMENT
REVDAT 5 27-SEP-23 5CJ4 1 REMARK
REVDAT 4 27-NOV-19 5CJ4 1 REMARK
REVDAT 3 27-SEP-17 5CJ4 1 JRNL REMARK
REVDAT 2 27-JAN-16 5CJ4 1 JRNL
REVDAT 1 02-DEC-15 5CJ4 0
JRNL AUTH E.N.KORKMAZ,K.C.TAYLOR,M.P.ANDREAS,G.AJAY,N.T.HEINZE,Q.CUI,
JRNL AUTH 2 I.RAYMENT
JRNL TITL A COMPOSITE APPROACH TOWARDS A COMPLETE MODEL OF THE MYOSIN
JRNL TITL 2 ROD.
JRNL REF PROTEINS V. 84 172 2016
JRNL REFN ESSN 1097-0134
JRNL PMID 26573747
JRNL DOI 10.1002/PROT.24964
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 18959
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 948
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.9292 - 5.9302 0.98 2627 138 0.2330 0.2884
REMARK 3 2 5.9302 - 4.7082 0.98 2587 138 0.2390 0.2694
REMARK 3 3 4.7082 - 4.1133 0.99 2572 135 0.2162 0.2571
REMARK 3 4 4.1133 - 3.7374 0.99 2562 135 0.2493 0.2493
REMARK 3 5 3.7374 - 3.4696 0.99 2579 136 0.2533 0.2923
REMARK 3 6 3.4696 - 3.2651 0.99 2564 134 0.2854 0.3236
REMARK 3 7 3.2651 - 3.1016 0.98 2520 132 0.2844 0.3241
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 6433
REMARK 3 ANGLE : 0.741 8655
REMARK 3 CHIRALITY : 0.032 940
REMARK 3 PLANARITY : 0.003 1098
REMARK 3 DIHEDRAL : 14.586 2447
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 96.3493 -17.7439 110.6900
REMARK 3 T TENSOR
REMARK 3 T11: 0.4576 T22: 0.7233
REMARK 3 T33: 0.5358 T12: 0.0100
REMARK 3 T13: -0.0319 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 3.7725 L22: 1.8022
REMARK 3 L33: 5.2135 L12: -0.3135
REMARK 3 L13: -1.4293 L23: 1.9634
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: 0.3266 S13: -0.1993
REMARK 3 S21: -0.2331 S22: -0.1334 S23: -0.1818
REMARK 3 S31: -0.1459 S32: 0.9860 S33: 0.1484
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 1572 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.4668 -15.4385 118.3763
REMARK 3 T TENSOR
REMARK 3 T11: 0.4728 T22: 1.1474
REMARK 3 T33: 0.7814 T12: 0.0961
REMARK 3 T13: -0.1918 T23: -0.1729
REMARK 3 L TENSOR
REMARK 3 L11: 6.1656 L22: -0.2373
REMARK 3 L33: 1.9995 L12: 0.9032
REMARK 3 L13: 2.5315 L23: 0.1478
REMARK 3 S TENSOR
REMARK 3 S11: 0.2196 S12: 0.1903 S13: 1.4971
REMARK 3 S21: 0.0922 S22: -0.7578 S23: 0.5431
REMARK 3 S31: -0.2200 S32: -0.5045 S33: 0.3004
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1573 THROUGH 1614 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8274 -22.2149 89.8215
REMARK 3 T TENSOR
REMARK 3 T11: 0.6119 T22: 1.1418
REMARK 3 T33: 0.5605 T12: -0.0064
REMARK 3 T13: -0.0747 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 7.1687 L22: 2.9155
REMARK 3 L33: 5.2238 L12: 1.5899
REMARK 3 L13: 1.8752 L23: 1.1347
REMARK 3 S TENSOR
REMARK 3 S11: 0.6870 S12: -0.7172 S13: -0.9625
REMARK 3 S21: 0.3270 S22: -0.4434 S23: -0.0625
REMARK 3 S31: 1.1442 S32: -0.4960 S33: -0.0055
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 1570 )
REMARK 3 ORIGIN FOR THE GROUP (A): 72.4945 -22.9779 135.0062
REMARK 3 T TENSOR
REMARK 3 T11: 0.5017 T22: 0.6679
REMARK 3 T33: 0.6682 T12: -0.1742
REMARK 3 T13: 0.0189 T23: -0.1014
REMARK 3 L TENSOR
REMARK 3 L11: 3.1664 L22: 2.2649
REMARK 3 L33: 4.3758 L12: 0.2275
REMARK 3 L13: -1.3870 L23: -0.1007
REMARK 3 S TENSOR
REMARK 3 S11: 0.1073 S12: -0.4124 S13: -0.2665
REMARK 3 S21: 0.3050 S22: -0.3637 S23: 0.3182
REMARK 3 S31: 0.4629 S32: -0.5090 S33: 0.1009
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1571 THROUGH 1608 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.2548 -16.3078 84.7998
REMARK 3 T TENSOR
REMARK 3 T11: 0.5127 T22: 0.9210
REMARK 3 T33: 0.5638 T12: -0.0085
REMARK 3 T13: -0.0709 T23: 0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 5.9612 L22: 2.8773
REMARK 3 L33: 3.9635 L12: 0.2233
REMARK 3 L13: 2.2801 L23: 1.0200
REMARK 3 S TENSOR
REMARK 3 S11: -0.0862 S12: -0.0768 S13: 0.9717
REMARK 3 S21: -0.2932 S22: 0.1385 S23: 0.3022
REMARK 3 S31: 0.3542 S32: -0.1289 S33: -0.2545
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 104.6833 9.3777 61.5806
REMARK 3 T TENSOR
REMARK 3 T11: 0.5268 T22: 0.3972
REMARK 3 T33: 0.5013 T12: -0.0785
REMARK 3 T13: -0.0591 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 3.4613 L22: 2.1794
REMARK 3 L33: 4.4088 L12: -1.0392
REMARK 3 L13: -2.1534 L23: 0.9401
REMARK 3 S TENSOR
REMARK 3 S11: 0.0571 S12: 0.1375 S13: 0.2810
REMARK 3 S21: -0.3263 S22: 0.2343 S23: -0.0499
REMARK 3 S31: -0.3569 S32: 0.1152 S33: -0.2140
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 91 THROUGH 1572 )
REMARK 3 ORIGIN FOR THE GROUP (A): 93.8552 8.5553 65.7969
REMARK 3 T TENSOR
REMARK 3 T11: 0.6369 T22: 0.4094
REMARK 3 T33: 0.4590 T12: -0.0137
REMARK 3 T13: -0.0290 T23: 0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 1.0125 L22: 1.8349
REMARK 3 L33: 3.3339 L12: 0.7805
REMARK 3 L13: -0.8247 L23: 1.0753
REMARK 3 S TENSOR
REMARK 3 S11: 0.0967 S12: -0.1086 S13: 0.5138
REMARK 3 S21: -0.2549 S22: 0.1797 S23: -0.0516
REMARK 3 S31: -0.0198 S32: 0.1667 S33: -0.1358
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1573 THROUGH 1619 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8892 0.4652 38.7101
REMARK 3 T TENSOR
REMARK 3 T11: 0.7034 T22: 0.8348
REMARK 3 T33: 0.5066 T12: -0.1460
REMARK 3 T13: -0.0333 T23: 0.2184
REMARK 3 L TENSOR
REMARK 3 L11: 2.9248 L22: 2.2504
REMARK 3 L33: 1.6769 L12: 0.6810
REMARK 3 L13: -0.5805 L23: 2.4849
REMARK 3 S TENSOR
REMARK 3 S11: -0.1283 S12: 0.1506 S13: 0.8391
REMARK 3 S21: 0.0835 S22: -0.1980 S23: 0.2962
REMARK 3 S31: -0.0650 S32: 0.3049 S33: 0.1356
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 1572 )
REMARK 3 ORIGIN FOR THE GROUP (A): 82.8839 5.4487 86.0213
REMARK 3 T TENSOR
REMARK 3 T11: 0.6087 T22: 0.8020
REMARK 3 T33: 0.6989 T12: -0.0198
REMARK 3 T13: -0.0144 T23: 0.1002
REMARK 3 L TENSOR
REMARK 3 L11: 4.4914 L22: -0.0028
REMARK 3 L33: 3.5608 L12: -0.9013
REMARK 3 L13: -1.8286 L23: 0.2824
REMARK 3 S TENSOR
REMARK 3 S11: -0.2083 S12: -0.5317 S13: -0.0436
REMARK 3 S21: 0.0639 S22: 0.2302 S23: 0.3415
REMARK 3 S31: 0.1986 S32: -0.6775 S33: -0.0582
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1573 THROUGH 1612 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3619 4.7302 34.5294
REMARK 3 T TENSOR
REMARK 3 T11: 0.5269 T22: 0.7664
REMARK 3 T33: 0.5911 T12: -0.0653
REMARK 3 T13: -0.0344 T23: 0.1469
REMARK 3 L TENSOR
REMARK 3 L11: 8.9595 L22: 1.6466
REMARK 3 L33: 3.8406 L12: 0.8865
REMARK 3 L13: 2.4008 L23: 0.4956
REMARK 3 S TENSOR
REMARK 3 S11: 0.5878 S12: -0.2293 S13: 0.2795
REMARK 3 S21: 0.2863 S22: -0.3435 S23: 0.3716
REMARK 3 S31: 0.9068 S32: 0.1699 S33: -0.0474
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 3056
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 3056
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 3056
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211727.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-14
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 : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL MONOCHROMATOR.
REMARK 200 LN2 COOLED FIRST CRYSTAL,
REMARK 200 SAGITTAL FOCUSING 2ND CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19051
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.36600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.9_1692
REMARK 200 STARTING MODEL: 1IK9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% (W/V) PEG 4000, 500 MM NACL, 100
REMARK 280 MM TRIETHANOLAMINE PH 8.0., VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 28.64250
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: 4700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 5030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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 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 GLY A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 ALA A 78
REMARK 465 GLY A 79
REMARK 465 PRO A 80
REMARK 465 ALA A 81
REMARK 465 MLY A 1616
REMARK 465 MLY A 1617
REMARK 465 MET A 1618
REMARK 465 GLU A 1619
REMARK 465 GLY A 1620
REMARK 465 ASP A 1621
REMARK 465 LEU A 1622
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 PRO B 80
REMARK 465 ASN B 1609
REMARK 465 GLU B 1610
REMARK 465 ALA B 1611
REMARK 465 LEU B 1612
REMARK 465 ARG B 1613
REMARK 465 VAL B 1614
REMARK 465 MLY B 1615
REMARK 465 MLY B 1616
REMARK 465 MLY B 1617
REMARK 465 MET B 1618
REMARK 465 GLU B 1619
REMARK 465 GLY B 1620
REMARK 465 ASP B 1621
REMARK 465 LEU B 1622
REMARK 465 GLY C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 GLY C 77
REMARK 465 ALA C 78
REMARK 465 GLY C 79
REMARK 465 PRO C 80
REMARK 465 ALA C 81
REMARK 465 GLY C 1620
REMARK 465 ASP C 1621
REMARK 465 LEU C 1622
REMARK 465 GLY D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 GLY D 77
REMARK 465 ALA D 78
REMARK 465 GLY D 79
REMARK 465 PRO D 80
REMARK 465 ALA D 81
REMARK 465 ASP D 82
REMARK 465 ARG D 1613
REMARK 465 VAL D 1614
REMARK 465 MLY D 1615
REMARK 465 MLY D 1616
REMARK 465 MLY D 1617
REMARK 465 MET D 1618
REMARK 465 GLU D 1619
REMARK 465 GLY D 1620
REMARK 465 ASP D 1621
REMARK 465 LEU D 1622
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 OG SER C 89 OG SER C 92 2.05
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 OE1 GLU B 1578 NH1 ARG D 1606 2646 2.10
REMARK 500 O MET A 59 NH2 ARG A 1592 1655 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 25 -77.12 -78.81
REMARK 500 ASP A 38 -167.82 -107.35
REMARK 500 MLY A 102 55.87 38.19
REMARK 500 HIS B 40 -52.87 -121.26
REMARK 500 HIS C 40 -52.44 -121.61
REMARK 500 MLY D 26 -56.21 -125.17
REMARK 500 HIS D 40 -51.94 -122.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CHX RELATED DB: PDB
REMARK 900 RELATED ID: 5CJ0 RELATED DB: PDB
REMARK 900 RELATED ID: 5CJ1 RELATED DB: PDB
DBREF 5CJ4 A 2 144 UNP Q13426 XRCC4_HUMAN 2 144
DBREF 5CJ4 A 1562 1622 UNP P12883 MYH7_HUMAN 1562 1622
DBREF 5CJ4 B 2 144 UNP Q13426 XRCC4_HUMAN 2 144
DBREF 5CJ4 B 1562 1622 UNP P12883 MYH7_HUMAN 1562 1622
DBREF 5CJ4 C 2 144 UNP Q13426 XRCC4_HUMAN 2 144
DBREF 5CJ4 C 1562 1622 UNP P12883 MYH7_HUMAN 1562 1622
DBREF 5CJ4 D 2 144 UNP Q13426 XRCC4_HUMAN 2 144
DBREF 5CJ4 D 1562 1622 UNP P12883 MYH7_HUMAN 1562 1622
SEQADV 5CJ4 GLY A -2 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 GLY A -1 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 SER A 0 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 GLY A 1 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 THR A 134 UNP Q13426 ILE 134 ENGINEERED MUTATION
SEQADV 5CJ4 GLY B -2 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 GLY B -1 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 SER B 0 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 GLY B 1 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 THR B 134 UNP Q13426 ILE 134 ENGINEERED MUTATION
SEQADV 5CJ4 GLY C -2 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 GLY C -1 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 SER C 0 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 GLY C 1 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 THR C 134 UNP Q13426 ILE 134 ENGINEERED MUTATION
SEQADV 5CJ4 GLY D -2 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 GLY D -1 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 SER D 0 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 GLY D 1 UNP Q13426 EXPRESSION TAG
SEQADV 5CJ4 THR D 134 UNP Q13426 ILE 134 ENGINEERED MUTATION
SEQRES 1 A 208 GLY GLY SER GLY GLU ARG MLY ILE SER ARG ILE HIS LEU
SEQRES 2 A 208 VAL SER GLU PRO SER ILE THR HIS PHE LEU GLN VAL SER
SEQRES 3 A 208 TRP GLU MLY THR LEU GLU SER GLY PHE VAL ILE THR LEU
SEQRES 4 A 208 THR ASP GLY HIS SER ALA TRP THR GLY THR VAL SER GLU
SEQRES 5 A 208 SER GLU ILE SER GLN GLU ALA ASP ASP MET ALA MET GLU
SEQRES 6 A 208 MLY GLY MLY TYR VAL GLY GLU LEU ARG MLY ALA LEU LEU
SEQRES 7 A 208 SER GLY ALA GLY PRO ALA ASP VAL TYR THR PHE ASN PHE
SEQRES 8 A 208 SER MLY GLU SER CYS TYR PHE PHE PHE GLU MLY ASN LEU
SEQRES 9 A 208 MLY ASP VAL SER PHE ARG LEU GLY SER PHE ASN LEU GLU
SEQRES 10 A 208 MLY VAL GLU ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE
SEQRES 11 A 208 CYS TYR CYS LEU ASP THR THR ALA GLU ASN GLN ALA MLY
SEQRES 12 A 208 ASN GLU HIS LEU GLN LEU GLU PHE ASN GLN ILE MLY ALA
SEQRES 13 A 208 GLU ILE GLU ARG MLY LEU ALA GLU MLY ASP GLU GLU MET
SEQRES 14 A 208 GLU GLN ALA MLY ARG ASN HIS LEU ARG VAL VAL ASP SER
SEQRES 15 A 208 LEU GLN THR SER LEU ASP ALA GLU THR ARG SER ARG ASN
SEQRES 16 A 208 GLU ALA LEU ARG VAL MLY MLY MLY MET GLU GLY ASP LEU
SEQRES 1 B 208 GLY GLY SER GLY GLU ARG MLY ILE SER ARG ILE HIS LEU
SEQRES 2 B 208 VAL SER GLU PRO SER ILE THR HIS PHE LEU GLN VAL SER
SEQRES 3 B 208 TRP GLU MLY THR LEU GLU SER GLY PHE VAL ILE THR LEU
SEQRES 4 B 208 THR ASP GLY HIS SER ALA TRP THR GLY THR VAL SER GLU
SEQRES 5 B 208 SER GLU ILE SER GLN GLU ALA ASP ASP MET ALA MET GLU
SEQRES 6 B 208 MLY GLY MLY TYR VAL GLY GLU LEU ARG MLY ALA LEU LEU
SEQRES 7 B 208 SER GLY ALA GLY PRO ALA ASP VAL TYR THR PHE ASN PHE
SEQRES 8 B 208 SER MLY GLU SER CYS TYR PHE PHE PHE GLU MLY ASN LEU
SEQRES 9 B 208 MLY ASP VAL SER PHE ARG LEU GLY SER PHE ASN LEU GLU
SEQRES 10 B 208 MLY VAL GLU ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE
SEQRES 11 B 208 CYS TYR CYS LEU ASP THR THR ALA GLU ASN GLN ALA MLY
SEQRES 12 B 208 ASN GLU HIS LEU GLN LEU GLU PHE ASN GLN ILE MLY ALA
SEQRES 13 B 208 GLU ILE GLU ARG MLY LEU ALA GLU MLY ASP GLU GLU MET
SEQRES 14 B 208 GLU GLN ALA MLY ARG ASN HIS LEU ARG VAL VAL ASP SER
SEQRES 15 B 208 LEU GLN THR SER LEU ASP ALA GLU THR ARG SER ARG ASN
SEQRES 16 B 208 GLU ALA LEU ARG VAL MLY MLY MLY MET GLU GLY ASP LEU
SEQRES 1 C 208 GLY GLY SER GLY GLU ARG MLY ILE SER ARG ILE HIS LEU
SEQRES 2 C 208 VAL SER GLU PRO SER ILE THR HIS PHE LEU GLN VAL SER
SEQRES 3 C 208 TRP GLU MLY THR LEU GLU SER GLY PHE VAL ILE THR LEU
SEQRES 4 C 208 THR ASP GLY HIS SER ALA TRP THR GLY THR VAL SER GLU
SEQRES 5 C 208 SER GLU ILE SER GLN GLU ALA ASP ASP MET ALA MET GLU
SEQRES 6 C 208 MLY GLY MLY TYR VAL GLY GLU LEU ARG MLY ALA LEU LEU
SEQRES 7 C 208 SER GLY ALA GLY PRO ALA ASP VAL TYR THR PHE ASN PHE
SEQRES 8 C 208 SER MLY GLU SER CYS TYR PHE PHE PHE GLU MLY ASN LEU
SEQRES 9 C 208 MLY ASP VAL SER PHE ARG LEU GLY SER PHE ASN LEU GLU
SEQRES 10 C 208 MLY VAL GLU ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE
SEQRES 11 C 208 CYS TYR CYS LEU ASP THR THR ALA GLU ASN GLN ALA MLY
SEQRES 12 C 208 ASN GLU HIS LEU GLN LEU GLU PHE ASN GLN ILE MLY ALA
SEQRES 13 C 208 GLU ILE GLU ARG MLY LEU ALA GLU MLY ASP GLU GLU MET
SEQRES 14 C 208 GLU GLN ALA MLY ARG ASN HIS LEU ARG VAL VAL ASP SER
SEQRES 15 C 208 LEU GLN THR SER LEU ASP ALA GLU THR ARG SER ARG ASN
SEQRES 16 C 208 GLU ALA LEU ARG VAL MLY MLY MLY MET GLU GLY ASP LEU
SEQRES 1 D 208 GLY GLY SER GLY GLU ARG MLY ILE SER ARG ILE HIS LEU
SEQRES 2 D 208 VAL SER GLU PRO SER ILE THR HIS PHE LEU GLN VAL SER
SEQRES 3 D 208 TRP GLU MLY THR LEU GLU SER GLY PHE VAL ILE THR LEU
SEQRES 4 D 208 THR ASP GLY HIS SER ALA TRP THR GLY THR VAL SER GLU
SEQRES 5 D 208 SER GLU ILE SER GLN GLU ALA ASP ASP MET ALA MET GLU
SEQRES 6 D 208 MLY GLY MLY TYR VAL GLY GLU LEU ARG MLY ALA LEU LEU
SEQRES 7 D 208 SER GLY ALA GLY PRO ALA ASP VAL TYR THR PHE ASN PHE
SEQRES 8 D 208 SER MLY GLU SER CYS TYR PHE PHE PHE GLU MLY ASN LEU
SEQRES 9 D 208 MLY ASP VAL SER PHE ARG LEU GLY SER PHE ASN LEU GLU
SEQRES 10 D 208 MLY VAL GLU ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE
SEQRES 11 D 208 CYS TYR CYS LEU ASP THR THR ALA GLU ASN GLN ALA MLY
SEQRES 12 D 208 ASN GLU HIS LEU GLN LEU GLU PHE ASN GLN ILE MLY ALA
SEQRES 13 D 208 GLU ILE GLU ARG MLY LEU ALA GLU MLY ASP GLU GLU MET
SEQRES 14 D 208 GLU GLN ALA MLY ARG ASN HIS LEU ARG VAL VAL ASP SER
SEQRES 15 D 208 LEU GLN THR SER LEU ASP ALA GLU THR ARG SER ARG ASN
SEQRES 16 D 208 GLU ALA LEU ARG VAL MLY MLY MLY MET GLU GLY ASP LEU
MODRES 5CJ4 MLY A 4 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 26 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 63 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 65 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 72 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 90 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 99 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 102 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 115 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 140 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 1569 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 1575 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 1579 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 1587 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY A 1615 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 4 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 26 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 63 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 65 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 72 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 90 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 99 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 102 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 115 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 140 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 1569 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 1575 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 1579 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY B 1587 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 4 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 26 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 63 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 65 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 72 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 90 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 99 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 102 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 115 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 140 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 1569 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 1575 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 1579 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 1587 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 1615 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 1616 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY C 1617 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 4 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 26 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 63 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 65 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 72 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 90 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 99 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 102 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 115 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 140 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 1569 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 1575 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 1579 LYS MODIFIED RESIDUE
MODRES 5CJ4 MLY D 1587 LYS MODIFIED RESIDUE
HET MLY A 4 11
HET MLY A 26 11
HET MLY A 63 11
HET MLY A 65 11
HET MLY A 72 11
HET MLY A 90 11
HET MLY A 99 11
HET MLY A 102 11
HET MLY A 115 11
HET MLY A 140 11
HET MLY A1569 11
HET MLY A1575 11
HET MLY A1579 11
HET MLY A1587 11
HET MLY A1615 11
HET MLY B 4 11
HET MLY B 26 11
HET MLY B 63 11
HET MLY B 65 11
HET MLY B 72 11
HET MLY B 90 11
HET MLY B 99 11
HET MLY B 102 11
HET MLY B 115 11
HET MLY B 140 11
HET MLY B1569 11
HET MLY B1575 11
HET MLY B1579 11
HET MLY B1587 11
HET MLY C 4 11
HET MLY C 26 11
HET MLY C 63 11
HET MLY C 65 11
HET MLY C 72 11
HET MLY C 90 11
HET MLY C 99 11
HET MLY C 102 11
HET MLY C 115 11
HET MLY C 140 11
HET MLY C1569 11
HET MLY C1575 11
HET MLY C1579 11
HET MLY C1587 11
HET MLY C1615 11
HET MLY C1616 11
HET MLY C1617 11
HET MLY D 4 11
HET MLY D 26 11
HET MLY D 63 11
HET MLY D 65 11
HET MLY D 72 11
HET MLY D 90 11
HET MLY D 99 11
HET MLY D 102 11
HET MLY D 115 11
HET MLY D 140 11
HET MLY D1569 11
HET MLY D1575 11
HET MLY D1579 11
HET MLY D1587 11
HETNAM MLY N-DIMETHYL-LYSINE
FORMUL 1 MLY 60(C8 H18 N2 O2)
FORMUL 5 HOH *2(H2 O)
HELIX 1 AA1 THR A 27 SER A 30 5 4
HELIX 2 AA2 SER A 48 MET A 59 1 12
HELIX 3 AA3 GLU A 62 LEU A 75 1 14
HELIX 4 AA4 ASN A 118 MLY A 1615 1 81
HELIX 5 AA5 THR B 27 GLY B 31 5 5
HELIX 6 AA6 SER B 48 MET B 59 1 12
HELIX 7 AA7 GLU B 62 LEU B 75 1 14
HELIX 8 AA8 ASN B 118 ARG B 1608 1 74
HELIX 9 AA9 THR C 27 GLU C 29 5 3
HELIX 10 AB1 GLU C 49 MET C 59 1 11
HELIX 11 AB2 GLU C 62 LEU C 75 1 14
HELIX 12 AB3 ASN C 118 GLU C 1619 1 85
HELIX 13 AB4 THR D 27 GLU D 29 5 3
HELIX 14 AB5 GLU D 49 MET D 59 1 11
HELIX 15 AB6 GLU D 62 LEU D 75 1 14
HELIX 16 AB7 ASN D 118 ALA D 1611 1 77
SHEET 1 AA1 5 GLU A 2 ILE A 8 0
SHEET 2 AA1 5 HIS A 18 TRP A 24 -1 O LEU A 20 N SER A 6
SHEET 3 AA1 5 PHE A 32 THR A 37 -1 O VAL A 33 N SER A 23
SHEET 4 AA1 5 ALA A 42 VAL A 47 -1 O TRP A 43 N LEU A 36
SHEET 5 AA1 5 GLU A 114 MLY A 115 -1 O GLU A 114 N THR A 44
SHEET 1 AA2 3 TYR A 84 SER A 89 0
SHEET 2 AA2 3 TYR A 94 LEU A 101 -1 O GLU A 98 N THR A 85
SHEET 3 AA2 3 VAL A 104 ASN A 112 -1 O VAL A 104 N LEU A 101
SHEET 1 AA3 5 GLU B 2 ILE B 8 0
SHEET 2 AA3 5 HIS B 18 TRP B 24 -1 O LEU B 20 N SER B 6
SHEET 3 AA3 5 PHE B 32 THR B 37 -1 O VAL B 33 N SER B 23
SHEET 4 AA3 5 ALA B 42 VAL B 47 -1 O GLY B 45 N ILE B 34
SHEET 5 AA3 5 GLU B 114 MLY B 115 -1 O GLU B 114 N THR B 44
SHEET 1 AA4 3 TYR B 84 SER B 89 0
SHEET 2 AA4 3 TYR B 94 LEU B 101 -1 O GLU B 98 N THR B 85
SHEET 3 AA4 3 VAL B 104 ASN B 112 -1 O VAL B 104 N LEU B 101
SHEET 1 AA5 5 GLU C 2 HIS C 9 0
SHEET 2 AA5 5 THR C 17 TRP C 24 -1 O LEU C 20 N SER C 6
SHEET 3 AA5 5 GLY C 31 THR C 37 -1 O THR C 37 N PHE C 19
SHEET 4 AA5 5 ALA C 42 SER C 48 -1 O VAL C 47 N PHE C 32
SHEET 5 AA5 5 GLU C 114 MLY C 115 -1 O GLU C 114 N THR C 44
SHEET 1 AA6 3 TYR C 84 SER C 89 0
SHEET 2 AA6 3 TYR C 94 ASN C 100 -1 O GLU C 98 N THR C 85
SHEET 3 AA6 3 SER C 105 ASN C 112 -1 O PHE C 111 N PHE C 95
SHEET 1 AA7 5 GLU D 2 HIS D 9 0
SHEET 2 AA7 5 THR D 17 TRP D 24 -1 O LEU D 20 N SER D 6
SHEET 3 AA7 5 GLY D 31 THR D 37 -1 O VAL D 33 N SER D 23
SHEET 4 AA7 5 ALA D 42 SER D 48 -1 O TRP D 43 N LEU D 36
SHEET 5 AA7 5 GLU D 114 MLY D 115 -1 O GLU D 114 N THR D 44
SHEET 1 AA8 3 TYR D 84 SER D 89 0
SHEET 2 AA8 3 TYR D 94 LEU D 101 -1 O GLU D 98 N THR D 85
SHEET 3 AA8 3 VAL D 104 ASN D 112 -1 O PHE D 111 N PHE D 95
LINK C ARG A 3 N MLY A 4 1555 1555 1.33
LINK C MLY A 4 N ILE A 5 1555 1555 1.33
LINK C GLU A 25 N MLY A 26 1555 1555 1.33
LINK C MLY A 26 N THR A 27 1555 1555 1.33
LINK C GLU A 62 N MLY A 63 1555 1555 1.33
LINK C MLY A 63 N GLY A 64 1555 1555 1.33
LINK C GLY A 64 N MLY A 65 1555 1555 1.33
LINK C MLY A 65 N TYR A 66 1555 1555 1.33
LINK C ARG A 71 N MLY A 72 1555 1555 1.33
LINK C MLY A 72 N ALA A 73 1555 1555 1.33
LINK C SER A 89 N MLY A 90 1555 1555 1.33
LINK C MLY A 90 N GLU A 91 1555 1555 1.33
LINK C GLU A 98 N MLY A 99 1555 1555 1.33
LINK C MLY A 99 N ASN A 100 1555 1555 1.33
LINK C LEU A 101 N MLY A 102 1555 1555 1.33
LINK C MLY A 102 N ASP A 103 1555 1555 1.33
LINK C GLU A 114 N MLY A 115 1555 1555 1.33
LINK C MLY A 115 N VAL A 116 1555 1555 1.33
LINK C ALA A 139 N MLY A 140 1555 1555 1.33
LINK C MLY A 140 N ASN A 141 1555 1555 1.33
LINK C ILE A1568 N MLY A1569 1555 1555 1.33
LINK C MLY A1569 N ALA A1570 1555 1555 1.33
LINK C ARG A1574 N MLY A1575 1555 1555 1.33
LINK C MLY A1575 N LEU A1576 1555 1555 1.33
LINK C GLU A1578 N MLY A1579 1555 1555 1.33
LINK C MLY A1579 N ASP A1580 1555 1555 1.33
LINK C ALA A1586 N MLY A1587 1555 1555 1.33
LINK C MLY A1587 N ARG A1588 1555 1555 1.33
LINK C VAL A1614 N MLY A1615 1555 1555 1.33
LINK C ARG B 3 N MLY B 4 1555 1555 1.33
LINK C MLY B 4 N ILE B 5 1555 1555 1.33
LINK C GLU B 25 N MLY B 26 1555 1555 1.33
LINK C MLY B 26 N THR B 27 1555 1555 1.33
LINK C GLU B 62 N MLY B 63 1555 1555 1.33
LINK C MLY B 63 N GLY B 64 1555 1555 1.33
LINK C GLY B 64 N MLY B 65 1555 1555 1.33
LINK C MLY B 65 N TYR B 66 1555 1555 1.33
LINK C ARG B 71 N MLY B 72 1555 1555 1.33
LINK C MLY B 72 N ALA B 73 1555 1555 1.33
LINK C SER B 89 N MLY B 90 1555 1555 1.33
LINK C MLY B 90 N GLU B 91 1555 1555 1.33
LINK C GLU B 98 N MLY B 99 1555 1555 1.33
LINK C MLY B 99 N ASN B 100 1555 1555 1.33
LINK C LEU B 101 N MLY B 102 1555 1555 1.33
LINK C MLY B 102 N ASP B 103 1555 1555 1.34
LINK C GLU B 114 N MLY B 115 1555 1555 1.33
LINK C MLY B 115 N VAL B 116 1555 1555 1.33
LINK C ALA B 139 N MLY B 140 1555 1555 1.33
LINK C MLY B 140 N ASN B 141 1555 1555 1.33
LINK C ILE B1568 N MLY B1569 1555 1555 1.33
LINK C MLY B1569 N ALA B1570 1555 1555 1.33
LINK C ARG B1574 N MLY B1575 1555 1555 1.33
LINK C MLY B1575 N LEU B1576 1555 1555 1.33
LINK C GLU B1578 N MLY B1579 1555 1555 1.33
LINK C MLY B1579 N ASP B1580 1555 1555 1.33
LINK C ALA B1586 N MLY B1587 1555 1555 1.33
LINK C MLY B1587 N ARG B1588 1555 1555 1.33
LINK C ARG C 3 N MLY C 4 1555 1555 1.33
LINK C MLY C 4 N ILE C 5 1555 1555 1.33
LINK C GLU C 25 N MLY C 26 1555 1555 1.33
LINK C MLY C 26 N THR C 27 1555 1555 1.33
LINK C GLU C 62 N MLY C 63 1555 1555 1.33
LINK C MLY C 63 N GLY C 64 1555 1555 1.33
LINK C GLY C 64 N MLY C 65 1555 1555 1.33
LINK C MLY C 65 N TYR C 66 1555 1555 1.33
LINK C ARG C 71 N MLY C 72 1555 1555 1.33
LINK C MLY C 72 N ALA C 73 1555 1555 1.33
LINK C SER C 89 N MLY C 90 1555 1555 1.33
LINK C MLY C 90 N GLU C 91 1555 1555 1.33
LINK C GLU C 98 N MLY C 99 1555 1555 1.33
LINK C MLY C 99 N ASN C 100 1555 1555 1.33
LINK C LEU C 101 N MLY C 102 1555 1555 1.33
LINK C MLY C 102 N ASP C 103 1555 1555 1.33
LINK C GLU C 114 N MLY C 115 1555 1555 1.33
LINK C MLY C 115 N VAL C 116 1555 1555 1.33
LINK C ALA C 139 N MLY C 140 1555 1555 1.33
LINK C MLY C 140 N ASN C 141 1555 1555 1.33
LINK C ILE C1568 N MLY C1569 1555 1555 1.33
LINK C MLY C1569 N ALA C1570 1555 1555 1.33
LINK C ARG C1574 N MLY C1575 1555 1555 1.33
LINK C MLY C1575 N LEU C1576 1555 1555 1.33
LINK C GLU C1578 N MLY C1579 1555 1555 1.33
LINK C MLY C1579 N ASP C1580 1555 1555 1.33
LINK C ALA C1586 N MLY C1587 1555 1555 1.33
LINK C MLY C1587 N ARG C1588 1555 1555 1.33
LINK C VAL C1614 N MLY C1615 1555 1555 1.33
LINK C MLY C1615 N MLY C1616 1555 1555 1.33
LINK C MLY C1616 N MLY C1617 1555 1555 1.33
LINK C MLY C1617 N MET C1618 1555 1555 1.33
LINK C ARG D 3 N MLY D 4 1555 1555 1.33
LINK C MLY D 4 N ILE D 5 1555 1555 1.33
LINK C GLU D 25 N MLY D 26 1555 1555 1.33
LINK C MLY D 26 N THR D 27 1555 1555 1.33
LINK C GLU D 62 N MLY D 63 1555 1555 1.33
LINK C MLY D 63 N GLY D 64 1555 1555 1.33
LINK C GLY D 64 N MLY D 65 1555 1555 1.33
LINK C MLY D 65 N TYR D 66 1555 1555 1.33
LINK C ARG D 71 N MLY D 72 1555 1555 1.33
LINK C MLY D 72 N ALA D 73 1555 1555 1.33
LINK C SER D 89 N MLY D 90 1555 1555 1.33
LINK C MLY D 90 N GLU D 91 1555 1555 1.33
LINK C GLU D 98 N MLY D 99 1555 1555 1.33
LINK C MLY D 99 N ASN D 100 1555 1555 1.33
LINK C LEU D 101 N MLY D 102 1555 1555 1.33
LINK C MLY D 102 N ASP D 103 1555 1555 1.33
LINK C GLU D 114 N MLY D 115 1555 1555 1.33
LINK C MLY D 115 N VAL D 116 1555 1555 1.33
LINK C ALA D 139 N MLY D 140 1555 1555 1.33
LINK C MLY D 140 N ASN D 141 1555 1555 1.33
LINK C ILE D1568 N MLY D1569 1555 1555 1.33
LINK C MLY D1569 N ALA D1570 1555 1555 1.33
LINK C ARG D1574 N MLY D1575 1555 1555 1.33
LINK C MLY D1575 N LEU D1576 1555 1555 1.33
LINK C GLU D1578 N MLY D1579 1555 1555 1.33
LINK C MLY D1579 N ASP D1580 1555 1555 1.33
LINK C ALA D1586 N MLY D1587 1555 1555 1.33
LINK C MLY D1587 N ARG D1588 1555 1555 1.33
CRYST1 83.145 57.285 112.100 90.00 99.86 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 0.012027 0.000000 0.002090 0.00000
SCALE2 0.000000 0.017457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009054 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
