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HEADER HYDROLASE 07-APR-16 5J8J
TITLE A HISTONE DEACETYLASE FROM SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE HDA1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 457-698;
COMPND 5 EC: 3.5.1.98;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: HDA1, YNL021W, N2819;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROSSMANN FOLD, DEACETYLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHU,H.SHEN,X.LI,M.TENG
REVDAT 1 19-APR-17 5J8J 0
JRNL AUTH H.SHEN,Y.ZHU,C.WANG,H.YAN,M.TENG,X.LI
JRNL TITL STRUCTURAL AND HISTONE BINDING ABILITY CHARACTERIZATION OF
JRNL TITL 2 THE ARB2 DOMAIN OF A HISTONE DEACETYLASE HDA1 FROM
JRNL TITL 3 SACCHAROMYCES CEREVISIAE.
JRNL REF SCI REP V. 6 33905 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27665728
JRNL DOI 10.1038/SREP33905
REMARK 2
REMARK 2 RESOLUTION. 2.72 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 14934
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.230
REMARK 3 FREE R VALUE TEST SET COUNT : 781
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 40.2885 - 4.9328 0.97 2456 123 0.1746 0.2090
REMARK 3 2 4.9328 - 3.9164 0.99 2407 131 0.1706 0.2006
REMARK 3 3 3.9164 - 3.4216 0.99 2358 137 0.1918 0.2622
REMARK 3 4 3.4216 - 3.1089 0.98 2338 136 0.2282 0.3164
REMARK 3 5 3.1089 - 2.8861 0.98 2334 135 0.2557 0.3408
REMARK 3 6 2.8861 - 2.7160 0.95 2260 119 0.2798 0.3546
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.820
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 : 0.009 1979
REMARK 3 ANGLE : 1.281 2698
REMARK 3 CHIRALITY : 0.049 312
REMARK 3 PLANARITY : 0.006 343
REMARK 3 DIHEDRAL : 13.900 696
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): -46.2438 18.2399 -25.4993
REMARK 3 T TENSOR
REMARK 3 T11: 0.8134 T22: 0.7455
REMARK 3 T33: 0.8099 T12: -0.0211
REMARK 3 T13: 0.1091 T23: 0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 0.8873 L22: 2.5034
REMARK 3 L33: 2.5582 L12: -0.7118
REMARK 3 L13: 1.0061 L23: -0.2788
REMARK 3 S TENSOR
REMARK 3 S11: 0.1827 S12: 0.0380 S13: -0.0494
REMARK 3 S21: -0.1766 S22: -0.0960 S23: -0.0876
REMARK 3 S31: -0.0447 S32: 0.2345 S33: -0.0440
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 5J8J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220112.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 130 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14972
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE TRIHYDRATE PH
REMARK 280 4.6, 2.0 M SODIUM FORMATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.98800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.97600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.97600
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.98800
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: 3390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -28.98800
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 HIS A 448
REMARK 465 HIS A 449
REMARK 465 GLU A 659
REMARK 465 ASN A 660
REMARK 465 GLU A 661
REMARK 465 SER A 662
REMARK 465 ARG A 663
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 VAL A 476 CG1 CG2
REMARK 470 LEU A 480 CG CD1 CD2
REMARK 470 ASP A 484 CG OD1 OD2
REMARK 470 LEU A 485 CD1 CD2
REMARK 470 GLU A 498 CG CD OE1 OE2
REMARK 470 LYS A 515 CG CD CE NZ
REMARK 470 ARG A 516 NH1 NH2
REMARK 470 LYS A 582 CG CD CE NZ
REMARK 470 LYS A 589 CG CD CE NZ
REMARK 470 LYS A 616 CG CD CE NZ
REMARK 470 GLN A 626 CD OE1 NE2
REMARK 470 GLN A 655 CG CD OE1 NE2
REMARK 470 LYS A 658 CG CD CE NZ
REMARK 470 LYS A 664 CG CD CE NZ
REMARK 470 ARG A 666 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 667 CG CD CE NZ
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 CD2 TYR A 599 OD1 ASN A 620 1.74
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 LEU A 480 53.58 -106.55
REMARK 500 GLU A 559 146.79 -175.42
REMARK 500 ILE A 581 -59.95 63.24
REMARK 500 LYS A 589 103.71 76.76
REMARK 500 THR A 611 -14.39 -151.14
REMARK 500 ARG A 671 83.11 76.03
REMARK 500 ASP A 697 26.70 -72.64
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5J8J A 457 698 UNP P53973 HDA1_YEAST 457 698
SEQADV 5J8J HIS A 448 UNP P53973 EXPRESSION TAG
SEQADV 5J8J HIS A 449 UNP P53973 EXPRESSION TAG
SEQADV 5J8J HIS A 450 UNP P53973 EXPRESSION TAG
SEQADV 5J8J HIS A 451 UNP P53973 EXPRESSION TAG
SEQADV 5J8J HIS A 452 UNP P53973 EXPRESSION TAG
SEQADV 5J8J HIS A 453 UNP P53973 EXPRESSION TAG
SEQADV 5J8J GLY A 454 UNP P53973 EXPRESSION TAG
SEQADV 5J8J SER A 455 UNP P53973 EXPRESSION TAG
SEQADV 5J8J MET A 456 UNP P53973 EXPRESSION TAG
SEQRES 1 A 251 HIS HIS HIS HIS HIS HIS GLY SER MET LEU GLN LYS ALA
SEQRES 2 A 251 ILE ARG GLN GLN GLN GLN HIS TYR LEU SER ASP GLU PHE
SEQRES 3 A 251 ASN PHE VAL THR LEU PRO LEU VAL SER MET ASP LEU PRO
SEQRES 4 A 251 ASP ASN THR VAL LEU CYS THR PRO ASN ILE SER GLU SER
SEQRES 5 A 251 ASN THR ILE ILE ILE VAL VAL HIS ASP THR SER ASP ILE
SEQRES 6 A 251 TRP ALA LYS ARG ASN VAL ILE SER GLY THR ILE ASP LEU
SEQRES 7 A 251 SER SER SER VAL ILE ILE ASP ASN SER LEU ASP PHE ILE
SEQRES 8 A 251 LYS TRP GLY LEU ASP ARG LYS TYR GLY ILE ILE ASP VAL
SEQRES 9 A 251 ASN ILE PRO LEU THR LEU PHE GLU PRO ASP ASN TYR SER
SEQRES 10 A 251 GLY MET ILE THR SER GLN GLU VAL LEU ILE TYR LEU TRP
SEQRES 11 A 251 ASP ASN TYR ILE LYS TYR PHE PRO SER VAL ALA LYS ILE
SEQRES 12 A 251 ALA PHE ILE GLY ILE GLY ASP SER TYR SER GLY ILE VAL
SEQRES 13 A 251 HIS LEU LEU GLY HIS ARG ASP THR ARG ALA VAL THR LYS
SEQRES 14 A 251 THR VAL ILE ASN PHE LEU GLY ASP LYS GLN LEU LYS PRO
SEQRES 15 A 251 LEU VAL PRO LEU VAL ASP GLU THR LEU SER GLU TRP TYR
SEQRES 16 A 251 PHE LYS ASN SER LEU ILE PHE SER ASN ASN SER HIS GLN
SEQRES 17 A 251 CYS TRP LYS GLU ASN GLU SER ARG LYS PRO ARG LYS LYS
SEQRES 18 A 251 PHE GLY ARG VAL LEU ARG CYS ASP THR ASP GLY LEU ASN
SEQRES 19 A 251 ASN ILE ILE GLU GLU ARG PHE GLU GLU ALA THR ASP PHE
SEQRES 20 A 251 ILE LEU ASP SER
HELIX 1 AA1 HIS A 453 ASN A 474 1 22
HELIX 2 AA2 PRO A 486 ASN A 488 5 3
HELIX 3 AA3 ASN A 495 SER A 499 5 5
HELIX 4 AA4 ASP A 524 SER A 528 5 5
HELIX 5 AA5 SER A 534 ASP A 543 1 10
HELIX 6 AA6 ASN A 562 TYR A 580 1 19
HELIX 7 AA7 SER A 598 ARG A 609 1 12
HELIX 8 AA8 GLU A 636 ASN A 645 1 10
HELIX 9 AA9 ARG A 666 GLY A 670 5 5
HELIX 10 AB1 GLY A 679 ASP A 697 1 19
SHEET 1 AA1 8 VAL A 476 THR A 477 0
SHEET 2 AA1 8 VAL A 490 CYS A 492 -1 O CYS A 492 N VAL A 476
SHEET 3 AA1 8 GLY A 547 ILE A 553 -1 O ASP A 550 N LEU A 491
SHEET 4 AA1 8 ILE A 502 ASP A 508 1 N ILE A 503 O GLY A 547
SHEET 5 AA1 8 ILE A 590 ILE A 595 1 O ILE A 593 N VAL A 506
SHEET 6 AA1 8 THR A 615 GLY A 623 1 O ILE A 619 N GLY A 594
SHEET 7 AA1 8 SER A 646 SER A 650 1 O LEU A 647 N ASN A 620
SHEET 8 AA1 8 VAL A 672 ARG A 674 1 O LEU A 673 N ILE A 648
SHEET 1 AA2 2 ASP A 511 TRP A 513 0
SHEET 2 AA2 2 VAL A 529 ILE A 531 -1 O VAL A 529 N TRP A 513
LINK CG TYR A 599 OD1 ASN A 620 1555 1555 1.50
CRYST1 104.974 104.974 86.964 90.00 90.00 120.00 P 31 2 1 6
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 0.009526 0.005500 0.000000 0.00000
SCALE2 0.000000 0.011000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011499 0.00000
TER 1918 SER A 698
MASTER 294 0 0 10 10 0 0 6 1917 1 2 20
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