HEADER CELL CYCLE 20-SEP-18 6MJE
TITLE STRUCTURE OF CANDIDA GLABRATA CSM1: S. CEREVISIAE DSN1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOPOLIN COMPLEX SUBUNIT CSM1;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: UNP RESIDUES 69-181;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DSN1P;
COMPND 8 CHAIN: B, D, F, H;
COMPND 9 FRAGMENT: UNP RESIDUES 71-110;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA GLABRATA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 5478;
SOURCE 5 GENE: AO440_000897, AO440_004693;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 10 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 11 ORGANISM_TAXID: 4932;
SOURCE 12 GENE: DSN1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MONOPOLIN, KINETOCHORE, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SINGH,K.D.CORBETT
REVDAT 5 11-OCT-23 6MJE 1 REMARK
REVDAT 4 01-JAN-20 6MJE 1 REMARK
REVDAT 3 13-NOV-19 6MJE 1 JRNL
REVDAT 2 22-MAY-19 6MJE 1 JRNL
REVDAT 1 07-NOV-18 6MJE 0
JRNL AUTH R.PLOWMAN,N.SINGH,E.C.TROMER,A.PAYAN,E.DURO,C.SPANOS,
JRNL AUTH 2 J.RAPPSILBER,B.SNEL,G.J.P.L.KOPS,K.D.CORBETT,A.L.MARSTON
JRNL TITL THE MOLECULAR BASIS OF MONOPOLIN RECRUITMENT TO THE
JRNL TITL 2 KINETOCHORE.
JRNL REF CHROMOSOMA V. 128 331 2019
JRNL REFN ISSN 1432-0886
JRNL PMID 31037469
JRNL DOI 10.1007/S00412-019-00700-0
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 25661
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1277
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 43.3578 - 5.1864 0.99 2892 135 0.2151 0.2770
REMARK 3 2 5.1864 - 4.1176 1.00 2833 174 0.1838 0.2135
REMARK 3 3 4.1176 - 3.5974 0.99 2880 136 0.2336 0.2819
REMARK 3 4 3.5974 - 3.2686 0.99 2849 132 0.2363 0.3540
REMARK 3 5 3.2686 - 3.0344 0.97 2817 138 0.2739 0.3514
REMARK 3 6 3.0344 - 2.8555 0.97 2763 156 0.3415 0.4137
REMARK 3 7 2.8555 - 2.7125 0.93 2648 162 0.3493 0.4122
REMARK 3 8 2.7125 - 2.5945 0.89 2527 129 0.3902 0.4780
REMARK 3 9 2.5945 - 2.4946 0.75 2175 115 0.3970 0.4882
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 4641
REMARK 3 ANGLE : 0.891 6234
REMARK 3 CHIRALITY : 0.047 690
REMARK 3 PLANARITY : 0.005 791
REMARK 3 DIHEDRAL : 15.924 2800
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1476 -24.6765 4.3510
REMARK 3 T TENSOR
REMARK 3 T11: 0.6159 T22: 0.5882
REMARK 3 T33: 0.5472 T12: 0.0032
REMARK 3 T13: -0.0029 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.1558 L22: 2.6140
REMARK 3 L33: 0.4058 L12: -0.3193
REMARK 3 L13: -0.1494 L23: 0.9115
REMARK 3 S TENSOR
REMARK 3 S11: -0.0612 S12: 0.0025 S13: 0.0117
REMARK 3 S21: 0.0906 S22: 0.0401 S23: -0.0421
REMARK 3 S31: 0.0171 S32: 0.0258 S33: 0.0000
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 6MJE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000237040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.127
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26122
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.19900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.79300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3N4R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M TRIS
REMARK 280 -HCL, PH 8.5, 25% PEG3350, CRYOPROTECT WITH ADDITIONAL 20%
REMARK 280 PEG400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 101.87750
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 50
REMARK 465 LYS A 51
REMARK 465 SER A 52
REMARK 465 SER A 53
REMARK 465 HIS A 54
REMARK 465 HIS A 55
REMARK 465 HIS A 56
REMARK 465 HIS A 57
REMARK 465 HIS A 58
REMARK 465 HIS A 59
REMARK 465 GLU A 60
REMARK 465 ASN A 61
REMARK 465 LYS A 117
REMARK 465 SER A 118
REMARK 465 GLN A 119
REMARK 465 ALA A 120
REMARK 465 GLU A 121
REMARK 465 ASN A 122
REMARK 465 THR A 123
REMARK 465 THR A 124
REMARK 465 GLU A 125
REMARK 465 VAL A 126
REMARK 465 ASP B 71
REMARK 465 LYS B 80
REMARK 465 HIS B 81
REMARK 465 ILE B 82
REMARK 465 GLN B 83
REMARK 465 GLY B 84
REMARK 465 PHE B 85
REMARK 465 ASN B 108
REMARK 465 SER B 109
REMARK 465 SER B 110
REMARK 465 MET C 50
REMARK 465 LYS C 51
REMARK 465 SER C 52
REMARK 465 SER C 53
REMARK 465 HIS C 54
REMARK 465 HIS C 55
REMARK 465 HIS C 56
REMARK 465 HIS C 57
REMARK 465 HIS C 58
REMARK 465 HIS C 59
REMARK 465 GLU C 60
REMARK 465 ASN C 61
REMARK 465 LYS C 117
REMARK 465 SER C 118
REMARK 465 GLN C 119
REMARK 465 ALA C 120
REMARK 465 GLU C 121
REMARK 465 ASN C 122
REMARK 465 THR C 123
REMARK 465 THR C 124
REMARK 465 GLU C 125
REMARK 465 VAL C 126
REMARK 465 ASP D 71
REMARK 465 LYS D 80
REMARK 465 HIS D 81
REMARK 465 ILE D 82
REMARK 465 GLN D 83
REMARK 465 GLY D 84
REMARK 465 PHE D 85
REMARK 465 ASN D 108
REMARK 465 SER D 109
REMARK 465 SER D 110
REMARK 465 MET E 50
REMARK 465 LYS E 51
REMARK 465 SER E 52
REMARK 465 SER E 53
REMARK 465 HIS E 54
REMARK 465 HIS E 55
REMARK 465 HIS E 56
REMARK 465 HIS E 57
REMARK 465 HIS E 58
REMARK 465 HIS E 59
REMARK 465 GLU E 60
REMARK 465 ASN E 61
REMARK 465 LYS E 117
REMARK 465 SER E 118
REMARK 465 GLN E 119
REMARK 465 ALA E 120
REMARK 465 GLU E 121
REMARK 465 ASN E 122
REMARK 465 THR E 123
REMARK 465 THR E 124
REMARK 465 GLU E 125
REMARK 465 VAL E 126
REMARK 465 ASP E 127
REMARK 465 ASP F 71
REMARK 465 LYS F 80
REMARK 465 HIS F 81
REMARK 465 ILE F 82
REMARK 465 GLN F 83
REMARK 465 GLY F 84
REMARK 465 PHE F 85
REMARK 465 ASN F 108
REMARK 465 SER F 109
REMARK 465 SER F 110
REMARK 465 MET G 50
REMARK 465 LYS G 51
REMARK 465 SER G 52
REMARK 465 SER G 53
REMARK 465 HIS G 54
REMARK 465 HIS G 55
REMARK 465 HIS G 56
REMARK 465 HIS G 57
REMARK 465 HIS G 58
REMARK 465 HIS G 59
REMARK 465 GLU G 60
REMARK 465 ASN G 61
REMARK 465 LYS G 117
REMARK 465 SER G 118
REMARK 465 GLN G 119
REMARK 465 ALA G 120
REMARK 465 GLU G 121
REMARK 465 ASN G 122
REMARK 465 THR G 123
REMARK 465 THR G 124
REMARK 465 GLU G 125
REMARK 465 VAL G 126
REMARK 465 ASP G 127
REMARK 465 ASP H 71
REMARK 465 LYS H 80
REMARK 465 HIS H 81
REMARK 465 ILE H 82
REMARK 465 GLN H 83
REMARK 465 GLY H 84
REMARK 465 PHE H 85
REMARK 465 ASN H 108
REMARK 465 SER H 109
REMARK 465 SER H 110
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 LEU A 62 CG CD1 CD2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 VAL A 181 CG1 CG2
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 LEU C 62 CG CD1 CD2
REMARK 470 LYS C 105 CG CD CE NZ
REMARK 470 ASP C 127 CG OD1 OD2
REMARK 470 LYS C 179 CG CD CE NZ
REMARK 470 LYS C 180 CG CD CE NZ
REMARK 470 VAL C 181 CG1 CG2
REMARK 470 LYS D 73 CG CD CE NZ
REMARK 470 LYS D 78 CG CD CE NZ
REMARK 470 LEU E 62 CG CD1 CD2
REMARK 470 LYS E 105 CG CD CE NZ
REMARK 470 LYS E 179 CG CD CE NZ
REMARK 470 LYS E 180 CG CD CE NZ
REMARK 470 VAL E 181 CG1 CG2
REMARK 470 LYS F 73 CG CD CE NZ
REMARK 470 LYS F 78 CG CD CE NZ
REMARK 470 LEU G 62 CG CD1 CD2
REMARK 470 LYS G 105 CG CD CE NZ
REMARK 470 LYS G 179 CG CD CE NZ
REMARK 470 LYS G 180 CG CD CE NZ
REMARK 470 VAL G 181 CG1 CG2
REMARK 470 LYS H 73 CG CD CE NZ
REMARK 470 LYS H 78 CG CD CE NZ
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 SER A 104 -156.58 -143.14
REMARK 500 SER C 104 -156.19 -139.78
REMARK 500 TYR E 63 74.12 -67.05
REMARK 500 SER E 104 -156.08 -142.10
REMARK 500 ASP G 92 -163.53 -129.40
REMARK 500 SER G 104 -155.05 -144.38
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 6MJE A 69 181 UNP A0A0W0CH22_CANGB
DBREF2 6MJE A A0A0W0CH22 69 181
DBREF1 6MJE B 71 110 UNP A0A1L4A9Z4_YEASX
DBREF2 6MJE B A0A1L4A9Z4 71 110
DBREF1 6MJE C 69 181 UNP A0A0W0CH22_CANGB
DBREF2 6MJE C A0A0W0CH22 69 181
DBREF1 6MJE D 71 110 UNP A0A1L4A9Z4_YEASX
DBREF2 6MJE D A0A1L4A9Z4 71 110
DBREF1 6MJE E 69 181 UNP A0A0W0CH22_CANGB
DBREF2 6MJE E A0A0W0CH22 69 181
DBREF1 6MJE F 71 110 UNP A0A1L4A9Z4_YEASX
DBREF2 6MJE F A0A1L4A9Z4 71 110
DBREF1 6MJE G 69 181 UNP A0A0W0CH22_CANGB
DBREF2 6MJE G A0A0W0CH22 69 181
DBREF1 6MJE H 71 110 UNP A0A1L4A9Z4_YEASX
DBREF2 6MJE H A0A1L4A9Z4 71 110
SEQADV 6MJE MET A 50 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE LYS A 51 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER A 52 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER A 53 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS A 54 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS A 55 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS A 56 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS A 57 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS A 58 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS A 59 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE GLU A 60 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ASN A 61 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE LEU A 62 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE TYR A 63 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE PHE A 64 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE GLN A 65 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER A 66 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ASN A 67 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ALA A 68 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE MET C 50 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE LYS C 51 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER C 52 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER C 53 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS C 54 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS C 55 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS C 56 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS C 57 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS C 58 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS C 59 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE GLU C 60 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ASN C 61 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE LEU C 62 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE TYR C 63 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE PHE C 64 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE GLN C 65 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER C 66 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ASN C 67 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ALA C 68 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE MET E 50 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE LYS E 51 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER E 52 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER E 53 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS E 54 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS E 55 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS E 56 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS E 57 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS E 58 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS E 59 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE GLU E 60 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ASN E 61 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE LEU E 62 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE TYR E 63 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE PHE E 64 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE GLN E 65 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER E 66 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ASN E 67 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ALA E 68 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE MET G 50 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE LYS G 51 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER G 52 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER G 53 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS G 54 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS G 55 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS G 56 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS G 57 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS G 58 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE HIS G 59 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE GLU G 60 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ASN G 61 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE LEU G 62 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE TYR G 63 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE PHE G 64 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE GLN G 65 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE SER G 66 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ASN G 67 UNP A0A0W0CH2 EXPRESSION TAG
SEQADV 6MJE ALA G 68 UNP A0A0W0CH2 EXPRESSION TAG
SEQRES 1 A 132 MET LYS SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 A 132 TYR PHE GLN SER ASN ALA GLU THR ILE GLU ILE ILE LYS
SEQRES 3 A 132 ASP LEU PHE GLU HIS LEU CYS GLY VAL ARG VAL HIS ARG
SEQRES 4 A 132 THR TYR GLU ASP ASP THR GLY LEU TRP PHE ASP THR SER
SEQRES 5 A 132 GLN GLY SER LYS ASN GLY ILE MET ASP TYR LYS LEU GLY
SEQRES 6 A 132 PHE VAL LYS SER GLN ALA GLU ASN THR THR GLU VAL ASP
SEQRES 7 A 132 THR GLU VAL ILE TYR VAL PRO LEU LEU LYS GLN ARG THR
SEQRES 8 A 132 ALA GLU GLU LEU GLN GLU LEU GLN LYS LYS LEU PRO ASP
SEQRES 9 A 132 TYR LEU PHE GLU THR LEU SER PHE PRO LEU ARG SER LEU
SEQRES 10 A 132 ASN GLN PHE TYR ILE LYS MET SER LYS SER LEU ASN LYS
SEQRES 11 A 132 LYS VAL
SEQRES 1 B 40 ASP LEU LYS PHE LYS ARG HIS LYS ASN LYS HIS ILE GLN
SEQRES 2 B 40 GLY PHE PRO THR LEU GLY GLU ARG LEU ASP ASN LEU GLN
SEQRES 3 B 40 ASP ILE LYS LYS ALA LYS ARG VAL GLU ASN PHE ASN SER
SEQRES 4 B 40 SER
SEQRES 1 C 132 MET LYS SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 C 132 TYR PHE GLN SER ASN ALA GLU THR ILE GLU ILE ILE LYS
SEQRES 3 C 132 ASP LEU PHE GLU HIS LEU CYS GLY VAL ARG VAL HIS ARG
SEQRES 4 C 132 THR TYR GLU ASP ASP THR GLY LEU TRP PHE ASP THR SER
SEQRES 5 C 132 GLN GLY SER LYS ASN GLY ILE MET ASP TYR LYS LEU GLY
SEQRES 6 C 132 PHE VAL LYS SER GLN ALA GLU ASN THR THR GLU VAL ASP
SEQRES 7 C 132 THR GLU VAL ILE TYR VAL PRO LEU LEU LYS GLN ARG THR
SEQRES 8 C 132 ALA GLU GLU LEU GLN GLU LEU GLN LYS LYS LEU PRO ASP
SEQRES 9 C 132 TYR LEU PHE GLU THR LEU SER PHE PRO LEU ARG SER LEU
SEQRES 10 C 132 ASN GLN PHE TYR ILE LYS MET SER LYS SER LEU ASN LYS
SEQRES 11 C 132 LYS VAL
SEQRES 1 D 40 ASP LEU LYS PHE LYS ARG HIS LYS ASN LYS HIS ILE GLN
SEQRES 2 D 40 GLY PHE PRO THR LEU GLY GLU ARG LEU ASP ASN LEU GLN
SEQRES 3 D 40 ASP ILE LYS LYS ALA LYS ARG VAL GLU ASN PHE ASN SER
SEQRES 4 D 40 SER
SEQRES 1 E 132 MET LYS SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 E 132 TYR PHE GLN SER ASN ALA GLU THR ILE GLU ILE ILE LYS
SEQRES 3 E 132 ASP LEU PHE GLU HIS LEU CYS GLY VAL ARG VAL HIS ARG
SEQRES 4 E 132 THR TYR GLU ASP ASP THR GLY LEU TRP PHE ASP THR SER
SEQRES 5 E 132 GLN GLY SER LYS ASN GLY ILE MET ASP TYR LYS LEU GLY
SEQRES 6 E 132 PHE VAL LYS SER GLN ALA GLU ASN THR THR GLU VAL ASP
SEQRES 7 E 132 THR GLU VAL ILE TYR VAL PRO LEU LEU LYS GLN ARG THR
SEQRES 8 E 132 ALA GLU GLU LEU GLN GLU LEU GLN LYS LYS LEU PRO ASP
SEQRES 9 E 132 TYR LEU PHE GLU THR LEU SER PHE PRO LEU ARG SER LEU
SEQRES 10 E 132 ASN GLN PHE TYR ILE LYS MET SER LYS SER LEU ASN LYS
SEQRES 11 E 132 LYS VAL
SEQRES 1 F 40 ASP LEU LYS PHE LYS ARG HIS LYS ASN LYS HIS ILE GLN
SEQRES 2 F 40 GLY PHE PRO THR LEU GLY GLU ARG LEU ASP ASN LEU GLN
SEQRES 3 F 40 ASP ILE LYS LYS ALA LYS ARG VAL GLU ASN PHE ASN SER
SEQRES 4 F 40 SER
SEQRES 1 G 132 MET LYS SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 G 132 TYR PHE GLN SER ASN ALA GLU THR ILE GLU ILE ILE LYS
SEQRES 3 G 132 ASP LEU PHE GLU HIS LEU CYS GLY VAL ARG VAL HIS ARG
SEQRES 4 G 132 THR TYR GLU ASP ASP THR GLY LEU TRP PHE ASP THR SER
SEQRES 5 G 132 GLN GLY SER LYS ASN GLY ILE MET ASP TYR LYS LEU GLY
SEQRES 6 G 132 PHE VAL LYS SER GLN ALA GLU ASN THR THR GLU VAL ASP
SEQRES 7 G 132 THR GLU VAL ILE TYR VAL PRO LEU LEU LYS GLN ARG THR
SEQRES 8 G 132 ALA GLU GLU LEU GLN GLU LEU GLN LYS LYS LEU PRO ASP
SEQRES 9 G 132 TYR LEU PHE GLU THR LEU SER PHE PRO LEU ARG SER LEU
SEQRES 10 G 132 ASN GLN PHE TYR ILE LYS MET SER LYS SER LEU ASN LYS
SEQRES 11 G 132 LYS VAL
SEQRES 1 H 40 ASP LEU LYS PHE LYS ARG HIS LYS ASN LYS HIS ILE GLN
SEQRES 2 H 40 GLY PHE PRO THR LEU GLY GLU ARG LEU ASP ASN LEU GLN
SEQRES 3 H 40 ASP ILE LYS LYS ALA LYS ARG VAL GLU ASN PHE ASN SER
SEQRES 4 H 40 SER
HELIX 1 AA1 SER A 66 GLY A 83 1 18
HELIX 2 AA2 THR A 140 LEU A 151 1 12
HELIX 3 AA3 PRO A 152 GLU A 157 5 6
HELIX 4 AA4 SER A 165 LYS A 179 1 15
HELIX 5 AA5 THR B 87 ALA B 101 1 15
HELIX 6 AA6 SER C 66 GLY C 83 1 18
HELIX 7 AA7 THR C 140 LEU C 151 1 12
HELIX 8 AA8 PRO C 152 GLU C 157 5 6
HELIX 9 AA9 SER C 165 LYS C 179 1 15
HELIX 10 AB1 THR D 87 ALA D 101 1 15
HELIX 11 AB2 SER E 66 GLY E 83 1 18
HELIX 12 AB3 THR E 140 LEU E 151 1 12
HELIX 13 AB4 PRO E 152 GLU E 157 5 6
HELIX 14 AB5 SER E 165 LYS E 179 1 15
HELIX 15 AB6 THR F 87 ALA F 101 1 15
HELIX 16 AB7 SER G 66 GLY G 83 1 18
HELIX 17 AB8 THR G 140 LEU G 151 1 12
HELIX 18 AB9 PRO G 152 GLU G 157 5 6
HELIX 19 AC1 SER G 165 LYS G 179 1 15
HELIX 20 AC2 THR H 87 ALA H 101 1 15
SHEET 1 AA1 6 VAL A 84 GLU A 91 0
SHEET 2 AA1 6 LEU A 96 GLY A 103 -1 O TRP A 97 N TYR A 90
SHEET 3 AA1 6 ILE A 108 VAL A 116 -1 O LEU A 113 N PHE A 98
SHEET 4 AA1 6 GLU A 129 LEU A 135 -1 O ILE A 131 N GLY A 114
SHEET 5 AA1 6 LEU A 159 PRO A 162 -1 O PHE A 161 N VAL A 130
SHEET 6 AA1 6 LYS B 102 ARG B 103 1 O LYS B 102 N SER A 160
SHEET 1 AA2 6 VAL C 84 GLU C 91 0
SHEET 2 AA2 6 LEU C 96 GLY C 103 -1 O TRP C 97 N TYR C 90
SHEET 3 AA2 6 ILE C 108 VAL C 116 -1 O TYR C 111 N THR C 100
SHEET 4 AA2 6 GLU C 129 LEU C 135 -1 O LEU C 135 N ASP C 110
SHEET 5 AA2 6 LEU C 159 PRO C 162 -1 O PHE C 161 N VAL C 130
SHEET 6 AA2 6 LYS D 102 ARG D 103 1 O LYS D 102 N SER C 160
SHEET 1 AA3 6 VAL E 84 GLU E 91 0
SHEET 2 AA3 6 LEU E 96 GLY E 103 -1 O TRP E 97 N TYR E 90
SHEET 3 AA3 6 ILE E 108 PHE E 115 -1 O LEU E 113 N PHE E 98
SHEET 4 AA3 6 GLU E 129 LEU E 135 -1 O VAL E 133 N LYS E 112
SHEET 5 AA3 6 LEU E 159 PRO E 162 -1 O PHE E 161 N VAL E 130
SHEET 6 AA3 6 LYS F 102 ARG F 103 1 O LYS F 102 N SER E 160
SHEET 1 AA4 6 VAL G 84 GLU G 91 0
SHEET 2 AA4 6 LEU G 96 GLY G 103 -1 O TRP G 97 N TYR G 90
SHEET 3 AA4 6 ILE G 108 PHE G 115 -1 O TYR G 111 N THR G 100
SHEET 4 AA4 6 GLU G 129 LEU G 135 -1 O LEU G 135 N ASP G 110
SHEET 5 AA4 6 LEU G 159 PRO G 162 -1 O PHE G 161 N VAL G 130
SHEET 6 AA4 6 LYS H 102 ARG H 103 1 O LYS H 102 N SER G 160
CRYST1 44.368 203.755 44.259 90.00 90.36 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 0.022539 0.000000 0.000142 0.00000
SCALE2 0.000000 0.004908 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022595 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
