HEADER CELL CYCLE 14-NOV-16 5MEC
TITLE CRYSTAL STRUCTURE OF YEAST CDT1 MIDDLE DOMAIN (RESIDUES 294-433)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION CYCLE PROTEIN CDT1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 272-438;
COMPND 5 SYNONYM: SIC1 INDISPENSABLE PROTEIN 2,TOPOISOMERASE-A HYPERSENSITIVE
COMPND 6 PROTEIN 11;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: RESIDUES 294-433 SEEN IN THE CRYSTAL STRUCTURE, WITH
COMPND 9 EXCEPTION OF ONE LOOP WHICH IS NOT VISIBLE. SEQUENCE PROVIDED IS THAT
COMPND 10 WHICH WAS EXPRESSED.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: TAH11, CDT1, SID2, YJR046W, J1641;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CDT1, MCM, WINGED HELIX, YEAST, DNA REPLICATION, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.E.PYE,J.FRIGOLA,J.F.X.DIFFLEY,P.CHEREPANOV
REVDAT 3 17-JAN-24 5MEC 1 REMARK
REVDAT 2 05-JUL-17 5MEC 1 JRNL
REVDAT 1 17-MAY-17 5MEC 0
JRNL AUTH J.FRIGOLA,J.HE,K.KINKELIN,V.E.PYE,L.RENAULT,M.E.DOUGLAS,
JRNL AUTH 2 D.REMUS,P.CHEREPANOV,A.COSTA,J.F.X.DIFFLEY
JRNL TITL CDT1 STABILIZES AN OPEN MCM RING FOR HELICASE LOADING.
JRNL REF NAT COMMUN V. 8 15720 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 28643783
JRNL DOI 10.1038/NCOMMS15720
REMARK 2
REMARK 2 RESOLUTION. 2.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 2.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.120
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 9255
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.760
REMARK 3 FREE R VALUE TEST SET COUNT : 808
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 39.4747 - 3.8697 1.00 2679 153 0.1592 0.1956
REMARK 3 2 3.8697 - 3.0718 1.00 2708 135 0.1865 0.2214
REMARK 3 3 3.0718 - 2.6836 0.99 2715 112 0.2346 0.3405
REMARK 3 4 2.6836 - 2.4383 0.99 2698 134 0.2273 0.2969
REMARK 3 5 2.4383 - 2.2636 0.99 2687 126 0.2528 0.2801
REMARK 3 6 2.2636 - 2.1301 0.99 2679 148 0.2698 0.3673
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.00
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 : 0.002 1110
REMARK 3 ANGLE : 0.572 1507
REMARK 3 CHIRALITY : 0.024 178
REMARK 3 PLANARITY : 0.003 189
REMARK 3 DIHEDRAL : 10.977 440
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 294:338)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5958 4.9900 10.1452
REMARK 3 T TENSOR
REMARK 3 T11: 0.2866 T22: 0.2150
REMARK 3 T33: 0.2903 T12: -0.0158
REMARK 3 T13: -0.0021 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.6575 L22: 0.4433
REMARK 3 L33: 0.1665 L12: 0.1672
REMARK 3 L13: -0.2003 L23: -0.2799
REMARK 3 S TENSOR
REMARK 3 S11: -0.0630 S12: -0.0009 S13: -0.0564
REMARK 3 S21: -0.0569 S22: 0.0171 S23: 0.0604
REMARK 3 S31: 0.0891 S32: -0.1800 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 339:375)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1139 8.1453 19.3607
REMARK 3 T TENSOR
REMARK 3 T11: 0.3183 T22: 0.3600
REMARK 3 T33: 0.2933 T12: 0.0275
REMARK 3 T13: 0.0205 T23: -0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 0.4193 L22: 0.2843
REMARK 3 L33: 0.3287 L12: 0.1935
REMARK 3 L13: 0.1076 L23: -0.2132
REMARK 3 S TENSOR
REMARK 3 S11: 0.0377 S12: -0.3655 S13: 0.2989
REMARK 3 S21: 0.0963 S22: -0.1448 S23: -0.1076
REMARK 3 S31: -0.2854 S32: -0.2631 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 376:417)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7516 4.7628 16.6740
REMARK 3 T TENSOR
REMARK 3 T11: 0.4098 T22: 0.5220
REMARK 3 T33: 0.3369 T12: -0.0015
REMARK 3 T13: 0.0105 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.4070 L22: 0.1141
REMARK 3 L33: 0.3511 L12: 0.1301
REMARK 3 L13: -0.3663 L23: -0.1865
REMARK 3 S TENSOR
REMARK 3 S11: 0.2468 S12: -0.3555 S13: 0.0145
REMARK 3 S21: 0.1654 S22: -0.1041 S23: -0.0369
REMARK 3 S31: 0.2354 S32: -0.7351 S33: 0.0007
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 418:433)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4901 16.0688 12.2084
REMARK 3 T TENSOR
REMARK 3 T11: 0.4170 T22: 0.4637
REMARK 3 T33: 0.5110 T12: 0.1965
REMARK 3 T13: 0.0513 T23: -0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 0.7513 L22: 1.7127
REMARK 3 L33: 0.7977 L12: 0.7826
REMARK 3 L13: -0.5335 L23: 0.0509
REMARK 3 S TENSOR
REMARK 3 S11: -0.2714 S12: -0.1518 S13: 0.3965
REMARK 3 S21: -0.1055 S22: 0.1190 S23: 0.7175
REMARK 3 S31: -0.1774 S32: -0.5782 S33: 0.0233
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 5MEC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1200002239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9296
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
REMARK 200 RESOLUTION RANGE LOW (A) : 39.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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: 2WVR CHAIN C, RESIDUES 188-315 TRUNCATED TO
REMARK 200 POLYALA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BTP PH 5.5, 2M AMMONIUM SULPHATE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, 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 22.56500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.68000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.68000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.56500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.16500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 270
REMARK 465 MET A 271
REMARK 465 SER A 272
REMARK 465 LYS A 273
REMARK 465 GLY A 274
REMARK 465 GLU A 275
REMARK 465 GLY A 276
REMARK 465 THR A 277
REMARK 465 ILE A 278
REMARK 465 ALA A 279
REMARK 465 ASN A 280
REMARK 465 HIS A 281
REMARK 465 LEU A 282
REMARK 465 LEU A 283
REMARK 465 GLU A 284
REMARK 465 GLN A 285
REMARK 465 GLN A 286
REMARK 465 ILE A 287
REMARK 465 LYS A 288
REMARK 465 ALA A 289
REMARK 465 PHE A 290
REMARK 465 PRO A 291
REMARK 465 LYS A 292
REMARK 465 VAL A 293
REMARK 465 ASP A 389
REMARK 465 ASN A 390
REMARK 465 LEU A 391
REMARK 465 THR A 392
REMARK 465 THR A 393
REMARK 465 LEU A 394
REMARK 465 THR A 395
REMARK 465 ASN A 396
REMARK 465 LYS A 397
REMARK 465 ARG A 434
REMARK 465 SER A 435
REMARK 465 SER A 436
REMARK 465 SER A 437
REMARK 465 ASN A 438
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 ARG A 388 CG CD NE CZ NH1 NH2
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 PRO A 338 172.21 -59.81
REMARK 500 ASN A 376 -155.88 -82.11
REMARK 500 LYS A 418 37.19 -93.22
REMARK 500 ASP A 419 -128.60 -100.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5MEC A 272 438 UNP P47112 CDT1_YEAST 272 438
SEQADV 5MEC GLY A 270 UNP P47112 EXPRESSION TAG
SEQADV 5MEC MET A 271 UNP P47112 EXPRESSION TAG
SEQRES 1 A 169 GLY MET SER LYS GLY GLU GLY THR ILE ALA ASN HIS LEU
SEQRES 2 A 169 LEU GLU GLN GLN ILE LYS ALA PHE PRO LYS VAL ALA GLN
SEQRES 3 A 169 GLN TYR TYR PRO ARG GLU LEU SER ILE LEU ARG LEU GLN
SEQRES 4 A 169 ASP ALA MET LYS PHE VAL LYS GLU LEU PHE THR VAL CYS
SEQRES 5 A 169 GLU THR VAL LEU SER LEU ASN ALA LEU SER ARG SER THR
SEQRES 6 A 169 GLY VAL PRO PRO GLU LEU HIS VAL LEU LEU PRO GLN ILE
SEQRES 7 A 169 SER SER MET MET LYS ARG LYS ILE VAL GLN ASP ASP ILE
SEQRES 8 A 169 LEU LYS LEU LEU THR ILE TRP SER ASP ALA TYR VAL VAL
SEQRES 9 A 169 GLU LEU ASN SER ARG GLY GLU LEU THR MET ASN LEU PRO
SEQRES 10 A 169 LYS ARG ASP ASN LEU THR THR LEU THR ASN LYS SER ARG
SEQRES 11 A 169 THR LEU ALA PHE VAL GLU ARG ALA GLU SER TRP TYR GLN
SEQRES 12 A 169 GLN VAL ILE ALA SER LYS ASP GLU ILE MET THR ASP VAL
SEQRES 13 A 169 PRO ALA PHE LYS ILE ASN LYS ARG ARG SER SER SER ASN
FORMUL 2 HOH *61(H2 O)
HELIX 1 AA1 TYR A 298 ALA A 329 1 32
HELIX 2 AA2 GLU A 339 LYS A 352 1 14
HELIX 3 AA3 VAL A 356 TRP A 367 1 12
HELIX 4 AA4 ARG A 399 SER A 417 1 19
SHEET 1 AA1 2 VAL A 372 LEU A 375 0
SHEET 2 AA1 2 LEU A 381 ASN A 384 -1 O ASN A 384 N VAL A 372
CRYST1 45.130 46.330 75.360 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 0.022158 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021584 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013270 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
