HEADER CELL CYCLE 12-MAY-14 4PJU
TITLE CRYSTAL STRUCTURE OF HUMAN STROMAL ANTIGEN 2 (SA2) IN COMPLEX WITH
TITLE 2 SISTER CHROMATID COHESION PROTEIN 1 (SCC1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COHESIN SUBUNIT SA-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 80-1060;
COMPND 5 SYNONYM: SCC3 HOMOLOG 2,STROMAL ANTIGEN 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DOUBLE-STRAND-BREAK REPAIR PROTEIN RAD21 HOMOLOG;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 281-420;
COMPND 11 SYNONYM: HHR21,NUCLEAR MATRIX PROTEIN 1,NXP-1,SCC1 HOMOLOG;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: STAG2, SA2;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HT;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: RAD21, HR21, KIAA0078, NXP1;
SOURCE 17 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HT
KEYWDS SISTER CHROMATID COHESION, COHESIN SUBUNITS, PROTEIN-PROTEIN
KEYWDS 2 INTERACTION, HEAT REPEAT, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HARA,Z.CHEN,D.R.TOMCHICK,H.YU
REVDAT 5 27-DEC-23 4PJU 1 REMARK
REVDAT 4 20-NOV-19 4PJU 1 SOURCE KEYWDS REMARK
REVDAT 3 15-OCT-14 4PJU 1 JRNL
REVDAT 2 17-SEP-14 4PJU 1 JRNL
REVDAT 1 27-AUG-14 4PJU 0
JRNL AUTH K.HARA,G.ZHENG,Q.QU,H.LIU,Z.OUYANG,Z.CHEN,D.R.TOMCHICK,H.YU
JRNL TITL STRUCTURE OF COHESIN SUBCOMPLEX PINPOINTS DIRECT
JRNL TITL 2 SHUGOSHIN-WAPL ANTAGONISM IN CENTROMERIC COHESION.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 21 864 2014
JRNL REFN ESSN 1545-9985
JRNL PMID 25173175
JRNL DOI 10.1038/NSMB.2880
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 30393
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1520
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 45.4528 - 6.7763 0.99 2782 146 0.2027 0.2156
REMARK 3 2 6.7763 - 5.3813 1.00 2674 141 0.2248 0.2602
REMARK 3 3 5.3813 - 4.7019 1.00 2639 139 0.1661 0.2194
REMARK 3 4 4.7019 - 4.2724 1.00 2644 139 0.1489 0.2177
REMARK 3 5 4.2724 - 3.9663 1.00 2599 137 0.1596 0.2266
REMARK 3 6 3.9663 - 3.7326 1.00 2596 137 0.1719 0.2059
REMARK 3 7 3.7326 - 3.5457 1.00 2607 137 0.1875 0.2405
REMARK 3 8 3.5457 - 3.3914 1.00 2594 136 0.2171 0.3112
REMARK 3 9 3.3914 - 3.2609 1.00 2574 136 0.2384 0.3198
REMARK 3 10 3.2609 - 3.1484 1.00 2591 137 0.2763 0.3098
REMARK 3 11 3.1484 - 3.0500 1.00 2573 135 0.2849 0.3528
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 92.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.50
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 : 0.007 8041
REMARK 3 ANGLE : 1.032 10831
REMARK 3 CHIRALITY : 0.054 1246
REMARK 3 PLANARITY : 0.004 1355
REMARK 3 DIHEDRAL : 15.854 3022
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 83 THROUGH 318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.4466 39.1042 -5.2162
REMARK 3 T TENSOR
REMARK 3 T11: 0.3201 T22: 0.3421
REMARK 3 T33: 0.4245 T12: -0.0069
REMARK 3 T13: -0.0113 T23: -0.0630
REMARK 3 L TENSOR
REMARK 3 L11: 1.9969 L22: 0.6283
REMARK 3 L33: 0.6395 L12: 0.8874
REMARK 3 L13: 0.4277 L23: 0.1496
REMARK 3 S TENSOR
REMARK 3 S11: -0.0874 S12: 0.2097 S13: 0.3766
REMARK 3 S21: 0.1016 S22: 0.0434 S23: -0.0513
REMARK 3 S31: 0.0465 S32: 0.0657 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 605 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0514 -6.9999 -6.7697
REMARK 3 T TENSOR
REMARK 3 T11: 0.4375 T22: 0.3672
REMARK 3 T33: 0.3070 T12: 0.1086
REMARK 3 T13: -0.0696 T23: -0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 0.9530 L22: 1.0660
REMARK 3 L33: -0.2675 L12: 0.1542
REMARK 3 L13: 0.4483 L23: 0.0271
REMARK 3 S TENSOR
REMARK 3 S11: 0.1311 S12: 0.1720 S13: -0.0663
REMARK 3 S21: 0.1945 S22: -0.0950 S23: -0.0231
REMARK 3 S31: 0.1360 S32: 0.1680 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 606 THROUGH 1049 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1362 -21.1746 -36.2674
REMARK 3 T TENSOR
REMARK 3 T11: 0.5850 T22: 0.7219
REMARK 3 T33: 0.4029 T12: 0.1038
REMARK 3 T13: -0.0699 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 1.3661 L22: 0.6116
REMARK 3 L33: 0.7082 L12: 0.1740
REMARK 3 L13: 0.4003 L23: 0.0312
REMARK 3 S TENSOR
REMARK 3 S11: 0.0181 S12: 0.3571 S13: -0.1136
REMARK 3 S21: -0.1218 S22: 0.2454 S23: 0.0000
REMARK 3 S31: 0.1050 S32: -0.1034 S33: 0.0193
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 321 THROUGH 347 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7662 23.1085 -4.2049
REMARK 3 T TENSOR
REMARK 3 T11: 0.4892 T22: 0.4888
REMARK 3 T33: 0.4497 T12: 0.0414
REMARK 3 T13: -0.0541 T23: 0.0493
REMARK 3 L TENSOR
REMARK 3 L11: 0.0786 L22: 0.0762
REMARK 3 L33: 0.0425 L12: -0.0804
REMARK 3 L13: 0.0222 L23: 0.0910
REMARK 3 S TENSOR
REMARK 3 S11: -0.2067 S12: 0.1440 S13: 0.1194
REMARK 3 S21: -0.1046 S22: 0.5170 S23: 0.0483
REMARK 3 S31: -0.0302 S32: 0.1597 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 348 THROUGH 357 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.4206 -7.1705 -9.4161
REMARK 3 T TENSOR
REMARK 3 T11: 0.5039 T22: 0.3817
REMARK 3 T33: 0.6789 T12: -0.1044
REMARK 3 T13: -0.0773 T23: -0.0757
REMARK 3 L TENSOR
REMARK 3 L11: -0.0084 L22: 0.0211
REMARK 3 L33: 0.0400 L12: 0.0175
REMARK 3 L13: -0.0518 L23: -0.0573
REMARK 3 S TENSOR
REMARK 3 S11: -0.0414 S12: 0.0833 S13: 0.0361
REMARK 3 S21: 0.0239 S22: -0.1142 S23: 0.0915
REMARK 3 S31: -0.2099 S32: 0.1477 S33: 0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 358 THROUGH 365 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0975 -17.0926 -20.2534
REMARK 3 T TENSOR
REMARK 3 T11: 0.8954 T22: 0.8721
REMARK 3 T33: 1.0215 T12: -0.0387
REMARK 3 T13: -0.2531 T23: -0.6902
REMARK 3 L TENSOR
REMARK 3 L11: -0.0009 L22: 0.0573
REMARK 3 L33: 0.0212 L12: 0.0028
REMARK 3 L13: -0.0044 L23: 0.0114
REMARK 3 S TENSOR
REMARK 3 S11: 0.1246 S12: 0.0056 S13: -0.0229
REMARK 3 S21: 0.0294 S22: -0.2292 S23: -0.4118
REMARK 3 S31: 0.0794 S32: 0.0838 S33: -0.0463
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 366 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0317 -19.7602 -36.8355
REMARK 3 T TENSOR
REMARK 3 T11: 0.7035 T22: 0.8507
REMARK 3 T33: 0.4973 T12: 0.2434
REMARK 3 T13: -0.0166 T23: -0.1007
REMARK 3 L TENSOR
REMARK 3 L11: 0.0244 L22: 0.0224
REMARK 3 L33: 0.0305 L12: 0.0387
REMARK 3 L13: -0.0079 L23: -0.0014
REMARK 3 S TENSOR
REMARK 3 S11: 0.1775 S12: -0.1704 S13: -0.0310
REMARK 3 S21: 0.2252 S22: -0.0440 S23: -0.4893
REMARK 3 S31: 0.2931 S32: 0.3599 S33: -0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PJU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201542.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.979
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30609
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 8.90
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.12 M MORPHEUS DIVALENTS MIX, 0.1 M
REMARK 280 MORPHEUS BUFFER SYSTEM 1, AND 27-30% (V/V) MORPHEUS EOD_P8K
REMARK 280 (MOLECULAR DIMENSIONS)., VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 39.30300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.89550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.37600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.89550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.30300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.37600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 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 GLU A 80
REMARK 465 ASN A 81
REMARK 465 MSE A 82
REMARK 465 LYS A 254
REMARK 465 MSE A 255
REMARK 465 ILE A 256
REMARK 465 GLY A 257
REMARK 465 LYS A 258
REMARK 465 ARG A 259
REMARK 465 ALA A 260
REMARK 465 ARG A 439
REMARK 465 ARG A 440
REMARK 465 ASP A 441
REMARK 465 PRO A 442
REMARK 465 GLU A 443
REMARK 465 GLU A 444
REMARK 465 ASP A 445
REMARK 465 GLY A 446
REMARK 465 MSE A 447
REMARK 465 MSE A 448
REMARK 465 LYS A 449
REMARK 465 ARG A 450
REMARK 465 ARG A 451
REMARK 465 GLY A 452
REMARK 465 ARG A 453
REMARK 465 GLN A 454
REMARK 465 GLY A 455
REMARK 465 PRO A 506
REMARK 465 LEU A 507
REMARK 465 SER A 508
REMARK 465 GLY A 509
REMARK 465 GLU A 510
REMARK 465 GLU A 511
REMARK 465 ALA A 512
REMARK 465 GLY A 544
REMARK 465 LYS A 545
REMARK 465 GLU A 675
REMARK 465 GLY A 676
REMARK 465 THR A 749
REMARK 465 GLU A 750
REMARK 465 SER A 751
REMARK 465 SER A 752
REMARK 465 GLY A 805
REMARK 465 GLY A 806
REMARK 465 ARG A 807
REMARK 465 GLN A 837
REMARK 465 ASP A 838
REMARK 465 ASP A 839
REMARK 465 ASP A 840
REMARK 465 ASN A 841
REMARK 465 ASN A 842
REMARK 465 SER A 843
REMARK 465 ALA A 844
REMARK 465 ASP A 845
REMARK 465 GLY A 846
REMARK 465 GLN A 847
REMARK 465 GLN A 848
REMARK 465 GLU A 849
REMARK 465 ASP A 850
REMARK 465 GLU A 851
REMARK 465 GLU A 933
REMARK 465 ASN A 934
REMARK 465 GLY A 935
REMARK 465 TYR A 936
REMARK 465 ASN A 937
REMARK 465 GLY A 960
REMARK 465 LEU A 961
REMARK 465 ASP A 962
REMARK 465 GLN A 963
REMARK 465 LEU A 964
REMARK 465 LYS A 965
REMARK 465 PRO A 987
REMARK 465 SER A 991
REMARK 465 HIS A 992
REMARK 465 ALA A 1050
REMARK 465 GLY A 1051
REMARK 465 GLY A 1052
REMARK 465 ASP A 1053
REMARK 465 ASP A 1054
REMARK 465 ASP A 1055
REMARK 465 THR A 1056
REMARK 465 MSE A 1057
REMARK 465 SER A 1058
REMARK 465 VAL A 1059
REMARK 465 ILE A 1060
REMARK 465 VAL B 281
REMARK 465 ASP B 282
REMARK 465 PRO B 283
REMARK 465 VAL B 284
REMARK 465 GLU B 285
REMARK 465 PRO B 286
REMARK 465 MSE B 287
REMARK 465 PRO B 288
REMARK 465 THR B 289
REMARK 465 MSE B 290
REMARK 465 THR B 291
REMARK 465 ASP B 292
REMARK 465 GLN B 293
REMARK 465 THR B 294
REMARK 465 THR B 295
REMARK 465 LEU B 296
REMARK 465 VAL B 297
REMARK 465 PRO B 298
REMARK 465 ASN B 299
REMARK 465 GLU B 300
REMARK 465 GLU B 301
REMARK 465 GLU B 302
REMARK 465 ALA B 303
REMARK 465 PHE B 304
REMARK 465 ALA B 305
REMARK 465 LEU B 306
REMARK 465 GLU B 307
REMARK 465 PRO B 308
REMARK 465 ILE B 309
REMARK 465 ASP B 310
REMARK 465 ILE B 311
REMARK 465 THR B 312
REMARK 465 VAL B 313
REMARK 465 LYS B 314
REMARK 465 GLU B 315
REMARK 465 THR B 316
REMARK 465 LYS B 317
REMARK 465 ALA B 318
REMARK 465 LYS B 319
REMARK 465 ARG B 320
REMARK 465 PRO B 395
REMARK 465 LEU B 396
REMARK 465 VAL B 397
REMARK 465 PRO B 398
REMARK 465 GLU B 399
REMARK 465 ASP B 400
REMARK 465 LEU B 401
REMARK 465 ARG B 402
REMARK 465 LYS B 403
REMARK 465 ARG B 404
REMARK 465 ARG B 405
REMARK 465 LYS B 406
REMARK 465 GLY B 407
REMARK 465 GLY B 408
REMARK 465 GLU B 409
REMARK 465 ALA B 410
REMARK 465 ASP B 411
REMARK 465 ASN B 412
REMARK 465 LEU B 413
REMARK 465 ASP B 414
REMARK 465 GLU B 415
REMARK 465 PHE B 416
REMARK 465 LEU B 417
REMARK 465 LYS B 418
REMARK 465 GLU B 419
REMARK 465 PHE B 420
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 HG SER A 1007 OG SER A 1047 1.46
REMARK 500 OD1 ASP A 111 HH TYR A 195 1.48
REMARK 500 HE2 HIS A 337 O HOH A 1117 1.50
REMARK 500 O ARG A 560 HG1 THR A 564 1.52
REMARK 500 OD1 ASN A 325 HG SER A 327 1.54
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 HIS A 108 -71.08 -59.28
REMARK 500 SER A 189 -81.41 -157.78
REMARK 500 VAL A 292 -63.04 -127.70
REMARK 500 SER A 401 135.69 -178.58
REMARK 500 GLU A 504 64.92 -105.67
REMARK 500 ALA A 533 -76.28 -70.52
REMARK 500 CYS A 535 55.27 -102.64
REMARK 500 CYS A 640 48.14 -83.07
REMARK 500 GLU A 642 47.47 -83.83
REMARK 500 LEU A 673 63.44 -112.30
REMARK 500 LEU A 703 17.56 50.81
REMARK 500 ASP A 707 93.00 -62.74
REMARK 500 HIS A 800 45.93 -71.00
REMARK 500 ASP A 911 98.20 -167.80
REMARK 500 ILE A 931 -8.69 -55.71
REMARK 500 ASP A 939 -1.96 -141.51
REMARK 500 LYS A1009 23.33 -78.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PJW RELATED DB: PDB
DBREF 4PJU A 80 1060 UNP Q8N3U4 STAG2_HUMAN 80 1060
DBREF 4PJU B 281 420 UNP O60216 RAD21_HUMAN 281 420
SEQRES 1 A 981 GLU ASN MSE MSE LEU PHE GLU VAL VAL LYS MSE GLY LYS
SEQRES 2 A 981 SER ALA MSE GLN SER VAL VAL ASP ASP TRP ILE GLU SER
SEQRES 3 A 981 TYR LYS HIS ASP ARG ASP ILE ALA LEU LEU ASP LEU ILE
SEQRES 4 A 981 ASN PHE PHE ILE GLN CYS SER GLY CYS LYS GLY VAL VAL
SEQRES 5 A 981 THR ALA GLU MSE PHE ARG HIS MSE GLN ASN SER GLU ILE
SEQRES 6 A 981 ILE ARG LYS MSE THR GLU GLU PHE ASP GLU ASP SER GLY
SEQRES 7 A 981 ASP TYR PRO LEU THR MSE ALA GLY PRO GLN TRP LYS LYS
SEQRES 8 A 981 PHE LYS SER SER PHE CYS GLU PHE ILE GLY VAL LEU VAL
SEQRES 9 A 981 ARG GLN CYS GLN TYR SER ILE ILE TYR ASP GLU TYR MSE
SEQRES 10 A 981 MSE ASP THR VAL ILE SER LEU LEU THR GLY LEU SER ASP
SEQRES 11 A 981 SER GLN VAL ARG ALA PHE ARG HIS THR SER THR LEU ALA
SEQRES 12 A 981 ALA MSE LYS LEU MSE THR ALA LEU VAL ASN VAL ALA LEU
SEQRES 13 A 981 ASN LEU SER ILE ASN MSE ASP ASN THR GLN ARG GLN TYR
SEQRES 14 A 981 GLU ALA GLU ARG ASN LYS MSE ILE GLY LYS ARG ALA ASN
SEQRES 15 A 981 GLU ARG LEU GLU LEU LEU LEU GLN LYS ARG LYS GLU LEU
SEQRES 16 A 981 GLN GLU ASN GLN ASP GLU ILE GLU ASN MSE MSE ASN ALA
SEQRES 17 A 981 ILE PHE LYS GLY VAL PHE VAL HIS ARG TYR ARG ASP ALA
SEQRES 18 A 981 ILE ALA GLU ILE ARG ALA ILE CYS ILE GLU GLU ILE GLY
SEQRES 19 A 981 ILE TRP MSE LYS MSE TYR SER ASP ALA PHE LEU ASN ASP
SEQRES 20 A 981 SER TYR LEU LYS TYR VAL GLY TRP THR MSE HIS ASP LYS
SEQRES 21 A 981 GLN GLY GLU VAL ARG LEU LYS CYS LEU THR ALA LEU GLN
SEQRES 22 A 981 GLY LEU TYR TYR ASN LYS GLU LEU ASN SER LYS LEU GLU
SEQRES 23 A 981 LEU PHE THR SER ARG PHE LYS ASP ARG ILE VAL SER MSE
SEQRES 24 A 981 THR LEU ASP LYS GLU TYR ASP VAL ALA VAL GLN ALA ILE
SEQRES 25 A 981 LYS LEU LEU THR LEU VAL LEU GLN SER SER GLU GLU VAL
SEQRES 26 A 981 LEU THR ALA GLU ASP CYS GLU ASN VAL TYR HIS LEU VAL
SEQRES 27 A 981 TYR SER ALA HIS ARG PRO VAL ALA VAL ALA ALA GLY GLU
SEQRES 28 A 981 PHE LEU TYR LYS LYS LEU PHE SER ARG ARG ASP PRO GLU
SEQRES 29 A 981 GLU ASP GLY MSE MSE LYS ARG ARG GLY ARG GLN GLY PRO
SEQRES 30 A 981 ASN ALA ASN LEU VAL LYS THR LEU VAL PHE PHE PHE LEU
SEQRES 31 A 981 GLU SER GLU LEU HIS GLU HIS ALA ALA TYR LEU VAL ASP
SEQRES 32 A 981 SER MSE TRP ASP CYS ALA THR GLU LEU LEU LYS ASP TRP
SEQRES 33 A 981 GLU CYS MSE ASN SER LEU LEU LEU GLU GLU PRO LEU SER
SEQRES 34 A 981 GLY GLU GLU ALA LEU THR ASP ARG GLN GLU SER ALA LEU
SEQRES 35 A 981 ILE GLU ILE MSE LEU CYS THR ILE ARG GLN ALA ALA GLU
SEQRES 36 A 981 CYS HIS PRO PRO VAL GLY ARG GLY THR GLY LYS ARG VAL
SEQRES 37 A 981 LEU THR ALA LYS GLU LYS LYS THR GLN LEU ASP ASP ARG
SEQRES 38 A 981 THR LYS ILE THR GLU LEU PHE ALA VAL ALA LEU PRO GLN
SEQRES 39 A 981 LEU LEU ALA LYS TYR SER VAL ASP ALA GLU LYS VAL THR
SEQRES 40 A 981 ASN LEU LEU GLN LEU PRO GLN TYR PHE ASP LEU GLU ILE
SEQRES 41 A 981 TYR THR THR GLY ARG LEU GLU LYS HIS LEU ASP ALA LEU
SEQRES 42 A 981 LEU ARG GLN ILE ARG ASN ILE VAL GLU LYS HIS THR ASP
SEQRES 43 A 981 THR ASP VAL LEU GLU ALA CYS SER LYS THR TYR HIS ALA
SEQRES 44 A 981 LEU CYS ASN GLU GLU PHE THR ILE PHE ASN ARG VAL ASP
SEQRES 45 A 981 ILE SER ARG SER GLN LEU ILE ASP GLU LEU ALA ASP LYS
SEQRES 46 A 981 PHE ASN ARG LEU LEU GLU ASP PHE LEU GLN GLU GLY GLU
SEQRES 47 A 981 GLU PRO ASP GLU ASP ASP ALA TYR GLN VAL LEU SER THR
SEQRES 48 A 981 LEU LYS ARG ILE THR ALA PHE HIS ASN ALA HIS ASP LEU
SEQRES 49 A 981 SER LYS TRP ASP LEU PHE ALA CYS ASN TYR LYS LEU LEU
SEQRES 50 A 981 LYS THR GLY ILE GLU ASN GLY ASP MSE PRO GLU GLN ILE
SEQRES 51 A 981 VAL ILE HIS ALA LEU GLN CYS THR HIS TYR VAL ILE LEU
SEQRES 52 A 981 TRP GLN LEU ALA LYS ILE THR GLU SER SER SER THR LYS
SEQRES 53 A 981 GLU ASP LEU LEU ARG LEU LYS LYS GLN MSE ARG VAL PHE
SEQRES 54 A 981 CYS GLN ILE CYS GLN HIS TYR LEU THR ASN VAL ASN THR
SEQRES 55 A 981 THR VAL LYS GLU GLN ALA PHE THR ILE LEU CYS ASP ILE
SEQRES 56 A 981 LEU MSE ILE PHE SER HIS GLN ILE MSE SER GLY GLY ARG
SEQRES 57 A 981 ASP MSE LEU GLU PRO LEU VAL TYR THR PRO ASP SER SER
SEQRES 58 A 981 LEU GLN SER GLU LEU LEU SER PHE ILE LEU ASP HIS VAL
SEQRES 59 A 981 PHE ILE GLU GLN ASP ASP ASP ASN ASN SER ALA ASP GLY
SEQRES 60 A 981 GLN GLN GLU ASP GLU ALA SER LYS ILE GLU ALA LEU HIS
SEQRES 61 A 981 LYS ARG ARG ASN LEU LEU ALA ALA PHE CYS LYS LEU ILE
SEQRES 62 A 981 VAL TYR THR VAL VAL GLU MSE ASN THR ALA ALA ASP ILE
SEQRES 63 A 981 PHE LYS GLN TYR MSE LYS TYR TYR ASN ASP TYR GLY ASP
SEQRES 64 A 981 ILE ILE LYS GLU THR MSE SER LYS THR ARG GLN ILE ASP
SEQRES 65 A 981 LYS ILE GLN CYS ALA LYS THR LEU ILE LEU SER LEU GLN
SEQRES 66 A 981 GLN LEU PHE ASN GLU MSE ILE GLN GLU ASN GLY TYR ASN
SEQRES 67 A 981 PHE ASP ARG SER SER SER THR PHE SER GLY ILE LYS GLU
SEQRES 68 A 981 LEU ALA ARG ARG PHE ALA LEU THR PHE GLY LEU ASP GLN
SEQRES 69 A 981 LEU LYS THR ARG GLU ALA ILE ALA MSE LEU HIS LYS ASP
SEQRES 70 A 981 GLY ILE GLU PHE ALA PHE LYS GLU PRO ASN PRO GLN GLY
SEQRES 71 A 981 GLU SER HIS PRO PRO LEU ASN LEU ALA PHE LEU ASP ILE
SEQRES 72 A 981 LEU SER GLU PHE SER SER LYS LEU LEU ARG GLN ASP LYS
SEQRES 73 A 981 ARG THR VAL TYR VAL TYR LEU GLU LYS PHE MSE THR PHE
SEQRES 74 A 981 GLN MSE SER LEU ARG ARG GLU ASP VAL TRP LEU PRO LEU
SEQRES 75 A 981 MSE SER TYR ARG ASN SER LEU LEU ALA GLY GLY ASP ASP
SEQRES 76 A 981 ASP THR MSE SER VAL ILE
SEQRES 1 B 140 VAL ASP PRO VAL GLU PRO MSE PRO THR MSE THR ASP GLN
SEQRES 2 B 140 THR THR LEU VAL PRO ASN GLU GLU GLU ALA PHE ALA LEU
SEQRES 3 B 140 GLU PRO ILE ASP ILE THR VAL LYS GLU THR LYS ALA LYS
SEQRES 4 B 140 ARG LYS ARG LYS LEU ILE VAL ASP SER VAL LYS GLU LEU
SEQRES 5 B 140 ASP SER LYS THR ILE ARG ALA GLN LEU SER ASP TYR SER
SEQRES 6 B 140 ASP ILE VAL THR THR LEU ASP LEU ALA PRO PRO THR LYS
SEQRES 7 B 140 LYS LEU MSE MSE TRP LYS GLU THR GLY GLY VAL GLU LYS
SEQRES 8 B 140 LEU PHE SER LEU PRO ALA GLN PRO LEU TRP ASN ASN ARG
SEQRES 9 B 140 LEU LEU LYS LEU PHE THR ARG CYS LEU THR PRO LEU VAL
SEQRES 10 B 140 PRO GLU ASP LEU ARG LYS ARG ARG LYS GLY GLY GLU ALA
SEQRES 11 B 140 ASP ASN LEU ASP GLU PHE LEU LYS GLU PHE
MODRES 4PJU MSE A 83 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 90 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 95 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 135 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 139 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 148 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 163 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 196 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 197 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 224 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 227 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 241 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 284 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 285 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 316 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 318 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 336 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 378 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 484 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 498 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 525 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 725 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 765 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 796 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 803 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 809 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 879 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 890 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 904 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 930 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 972 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 1026 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 1030 MET MODIFIED RESIDUE
MODRES 4PJU MSE A 1042 MET MODIFIED RESIDUE
MODRES 4PJU MSE B 361 MET MODIFIED RESIDUE
MODRES 4PJU MSE B 362 MET MODIFIED RESIDUE
HET MSE A 83 16
HET MSE A 90 17
HET MSE A 95 17
HET MSE A 135 17
HET MSE A 139 17
HET MSE A 148 17
HET MSE A 163 17
HET MSE A 196 17
HET MSE A 197 17
HET MSE A 224 17
HET MSE A 227 17
HET MSE A 241 17
HET MSE A 284 17
HET MSE A 285 17
HET MSE A 316 17
HET MSE A 318 17
HET MSE A 336 17
HET MSE A 378 17
HET MSE A 484 17
HET MSE A 498 17
HET MSE A 525 17
HET MSE A 725 17
HET MSE A 765 17
HET MSE A 796 17
HET MSE A 803 17
HET MSE A 809 17
HET MSE A 879 17
HET MSE A 890 17
HET MSE A 904 17
HET MSE A 930 17
HET MSE A 972 17
HET MSE A1026 17
HET MSE A1030 17
HET MSE A1042 17
HET MSE B 361 17
HET MSE B 362 17
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 36(C5 H11 N O2 SE)
FORMUL 3 HOH *22(H2 O)
HELIX 1 AA1 MSE A 83 GLY A 91 1 9
HELIX 2 AA2 ALA A 94 ASP A 109 1 16
HELIX 3 AA3 ASP A 109 CYS A 124 1 16
HELIX 4 AA4 THR A 132 MSE A 139 1 8
HELIX 5 AA5 GLN A 140 GLU A 151 1 12
HELIX 6 AA6 GLY A 165 CYS A 186 1 22
HELIX 7 AA7 SER A 189 ASP A 193 5 5
HELIX 8 AA8 TYR A 195 SER A 208 1 14
HELIX 9 AA9 VAL A 212 GLU A 251 1 40
HELIX 10 AB1 GLU A 262 VAL A 292 1 31
HELIX 11 AB2 VAL A 292 TYR A 297 1 6
HELIX 12 AB3 ILE A 301 TYR A 319 1 19
HELIX 13 AB4 TYR A 319 LEU A 324 1 6
HELIX 14 AB5 ASN A 325 MSE A 336 1 12
HELIX 15 AB6 GLN A 340 GLY A 353 1 14
HELIX 16 AB7 ASN A 361 PHE A 371 1 11
HELIX 17 AB8 PHE A 371 MSE A 378 1 8
HELIX 18 AB9 THR A 379 ASP A 381 5 3
HELIX 19 AC1 GLU A 383 SER A 401 1 19
HELIX 20 AC2 THR A 406 HIS A 415 1 10
HELIX 21 AC3 LEU A 416 SER A 419 5 4
HELIX 22 AC4 HIS A 421 PHE A 437 1 17
HELIX 23 AC5 ASN A 457 SER A 471 1 15
HELIX 24 AC6 ALA A 477 MSE A 484 1 8
HELIX 25 AC7 ALA A 488 LYS A 493 1 6
HELIX 26 AC8 ASP A 494 GLU A 504 1 11
HELIX 27 AC9 THR A 514 GLU A 534 1 21
HELIX 28 AD1 THR A 549 SER A 579 1 31
HELIX 29 AD2 ASP A 581 GLN A 590 1 10
HELIX 30 AD3 LEU A 591 PHE A 595 5 5
HELIX 31 AD4 LEU A 597 THR A 601 5 5
HELIX 32 AD5 LEU A 605 HIS A 623 1 19
HELIX 33 AD6 ASP A 625 CYS A 640 1 16
HELIX 34 AD7 ILE A 646 LEU A 673 1 28
HELIX 35 AD8 ASP A 680 HIS A 701 1 22
HELIX 36 AD9 LEU A 708 GLY A 723 1 16
HELIX 37 AE1 PRO A 726 LYS A 747 1 22
HELIX 38 AE2 GLU A 756 LEU A 776 1 21
HELIX 39 AE3 ASN A 780 PHE A 798 1 19
HELIX 40 AE4 LEU A 810 VAL A 814 5 5
HELIX 41 AE5 ASP A 818 VAL A 833 1 16
HELIX 42 AE6 LYS A 854 TYR A 874 1 21
HELIX 43 AE7 GLU A 878 THR A 881 5 4
HELIX 44 AE8 ALA A 882 LYS A 887 1 6
HELIX 45 AE9 TYR A 896 GLN A 909 1 14
HELIX 46 AF1 ASP A 911 ILE A 931 1 21
HELIX 47 AF2 SER A 942 LEU A 957 1 16
HELIX 48 AF3 ARG A 967 PHE A 982 1 16
HELIX 49 AF4 ALA A 998 SER A 1004 1 7
HELIX 50 AF5 GLU A 1005 SER A 1007 5 3
HELIX 51 AF6 LEU A 1011 GLU A 1023 1 13
HELIX 52 AF7 TRP A 1038 SER A 1047 1 10
HELIX 53 AF8 ASP B 333 ASP B 343 1 11
HELIX 54 AF9 TYR B 344 VAL B 348 5 5
HELIX 55 AG1 THR B 357 THR B 366 1 10
HELIX 56 AG2 GLY B 368 PHE B 373 1 6
HELIX 57 AG3 ASN B 382 ARG B 391 1 10
LINK C MSE A 83 N LEU A 84 1555 1555 1.33
LINK C LYS A 89 N MSE A 90 1555 1555 1.33
LINK C MSE A 90 N GLY A 91 1555 1555 1.33
LINK C ALA A 94 N MSE A 95 1555 1555 1.33
LINK C MSE A 95 N GLN A 96 1555 1555 1.33
LINK C GLU A 134 N MSE A 135 1555 1555 1.33
LINK C MSE A 135 N PHE A 136 1555 1555 1.33
LINK C HIS A 138 N MSE A 139 1555 1555 1.33
LINK C MSE A 139 N GLN A 140 1555 1555 1.33
LINK C LYS A 147 N MSE A 148 1555 1555 1.33
LINK C MSE A 148 N THR A 149 1555 1555 1.33
LINK C THR A 162 N MSE A 163 1555 1555 1.33
LINK C MSE A 163 N ALA A 164 1555 1555 1.33
LINK C TYR A 195 N MSE A 196 1555 1555 1.33
LINK C MSE A 196 N MSE A 197 1555 1555 1.33
LINK C MSE A 197 N ASP A 198 1555 1555 1.32
LINK C ALA A 223 N MSE A 224 1555 1555 1.32
LINK C MSE A 224 N LYS A 225 1555 1555 1.33
LINK C LEU A 226 N MSE A 227 1555 1555 1.32
LINK C MSE A 227 N THR A 228 1555 1555 1.32
LINK C ASN A 240 N MSE A 241 1555 1555 1.33
LINK C MSE A 241 N ASP A 242 1555 1555 1.33
LINK C ASN A 283 N MSE A 284 1555 1555 1.33
LINK C MSE A 284 N MSE A 285 1555 1555 1.32
LINK C MSE A 285 N ASN A 286 1555 1555 1.32
LINK C TRP A 315 N MSE A 316 1555 1555 1.33
LINK C MSE A 316 N LYS A 317 1555 1555 1.33
LINK C LYS A 317 N MSE A 318 1555 1555 1.33
LINK C MSE A 318 N TYR A 319 1555 1555 1.33
LINK C THR A 335 N MSE A 336 1555 1555 1.33
LINK C MSE A 336 N HIS A 337 1555 1555 1.33
LINK C SER A 377 N MSE A 378 1555 1555 1.33
LINK C MSE A 378 N THR A 379 1555 1555 1.33
LINK C SER A 483 N MSE A 484 1555 1555 1.33
LINK C MSE A 484 N TRP A 485 1555 1555 1.33
LINK C CYS A 497 N MSE A 498 1555 1555 1.33
LINK C MSE A 498 N ASN A 499 1555 1555 1.33
LINK C ILE A 524 N MSE A 525 1555 1555 1.33
LINK C MSE A 525 N LEU A 526 1555 1555 1.33
LINK C ASP A 724 N MSE A 725 1555 1555 1.33
LINK C MSE A 725 N PRO A 726 1555 1555 1.35
LINK C GLN A 764 N MSE A 765 1555 1555 1.33
LINK C MSE A 765 N ARG A 766 1555 1555 1.33
LINK C LEU A 795 N MSE A 796 1555 1555 1.33
LINK C MSE A 796 N ILE A 797 1555 1555 1.33
LINK C ILE A 802 N MSE A 803 1555 1555 1.34
LINK C MSE A 803 N SER A 804 1555 1555 1.33
LINK C ASP A 808 N MSE A 809 1555 1555 1.33
LINK C MSE A 809 N LEU A 810 1555 1555 1.33
LINK C GLU A 878 N MSE A 879 1555 1555 1.33
LINK C MSE A 879 N ASN A 880 1555 1555 1.33
LINK C TYR A 889 N MSE A 890 1555 1555 1.33
LINK C MSE A 890 N LYS A 891 1555 1555 1.33
LINK C THR A 903 N MSE A 904 1555 1555 1.33
LINK C MSE A 904 N SER A 905 1555 1555 1.33
LINK C GLU A 929 N MSE A 930 1555 1555 1.33
LINK C MSE A 930 N ILE A 931 1555 1555 1.33
LINK C ALA A 971 N MSE A 972 1555 1555 1.33
LINK C MSE A 972 N LEU A 973 1555 1555 1.33
LINK C PHE A1025 N MSE A1026 1555 1555 1.33
LINK C MSE A1026 N THR A1027 1555 1555 1.33
LINK C GLN A1029 N MSE A1030 1555 1555 1.33
LINK C MSE A1030 N SER A1031 1555 1555 1.33
LINK C LEU A1041 N MSE A1042 1555 1555 1.33
LINK C MSE A1042 N SER A1043 1555 1555 1.33
LINK C LEU B 360 N MSE B 361 1555 1555 1.33
LINK C MSE B 361 N MSE B 362 1555 1555 1.32
LINK C MSE B 362 N TRP B 363 1555 1555 1.33
CISPEP 1 TYR A 356 ASN A 357 0 -4.37
CISPEP 2 GLU A 359 LEU A 360 0 -1.68
CISPEP 3 GLU A 1035 ASP A 1036 0 -3.30
CRYST1 78.606 108.752 181.791 90.00 90.00 90.00 P 21 21 21 4
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 0.012722 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009195 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005501 0.00000
HETATM 1 N MSE A 83 44.866 46.194 -21.761 1.00128.38 N
ANISOU 1 N MSE A 83 14493 17526 16761 -1413 -520 1451 N
HETATM 2 CA MSE A 83 45.904 45.452 -22.471 1.00128.49 C
ANISOU 2 CA MSE A 83 14482 17775 16565 -1489 -444 1385 C
HETATM 3 C MSE A 83 46.440 44.304 -21.629 1.00121.83 C
ANISOU 3 C MSE A 83 13746 16894 15650 -1352 -335 1120 C
HETATM 4 O MSE A 83 46.917 43.311 -22.169 1.00121.47 O
ANISOU 4 O MSE A 83 13699 17032 15421 -1385 -249 1012 O
HETATM 5 CB MSE A 83 47.073 46.367 -22.845 1.00140.14 C
ANISOU 5 CB MSE A 83 15860 19307 18079 -1584 -505 1510 C
HETATM 6 CG MSE A 83 46.684 47.652 -23.556 1.00161.01 C
ANISOU 6 CG MSE A 83 18392 21952 20833 -1720 -638 1794 C
HETATM 7 SE MSE A 83 48.248 48.696 -24.082 1.00190.65 SE
ANISOU 7 SE MSE A 83 22024 25807 24608 -1861 -709 1950 SE
HETATM 8 CE MSE A 83 48.835 49.376 -22.340 1.00139.20 C
ANISOU 8 CE MSE A 83 15585 18941 18363 -1666 -742 1825 C
HETATM 9 HA MSE A 83 45.529 45.094 -23.291 1.00154.19 H
HETATM 10 HB2 MSE A 83 47.543 46.613 -22.033 1.00168.17 H
HETATM 11 HB3 MSE A 83 47.671 45.878 -23.431 1.00168.17 H
HETATM 12 HG2 MSE A 83 46.183 47.433 -24.357 1.00193.22 H
HETATM 13 HG3 MSE A 83 46.144 48.194 -22.961 1.00193.22 H
HETATM 14 HE1 MSE A 83 49.625 49.925 -22.466 1.00167.04 H
HETATM 15 HE2 MSE A 83 48.121 49.907 -21.953 1.00167.04 H
HETATM 16 HE3 MSE A 83 49.041 48.626 -21.762 1.00167.04 H
(ATOM LINES ARE NOT SHOWN.)
END