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HEADER TRANSCRIPTION 03-MAR-16 5IKK
TITLE STRUCTURE OF THE HISTONE DEACETYLASE CLR3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE CLR3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CRYPTIC LOCI REGULATOR 3;
COMPND 5 EC: 3.5.1.98;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE 972H-;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 284812;
SOURCE 5 GENE: CLR3, SPBC800.03;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PACEBAC1 MULTIBAC;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: P728
KEYWDS HDAC DOMAIN, ALPHA/BETA HYDROLASE DOMAIN, DIMER, ALPHA/BETA SANDWICH,
KEYWDS 2 HYDROLASE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BRUGGER,T.SCHALCH
REVDAT 2 04-MAY-16 5IKK 1 JRNL
REVDAT 1 20-APR-16 5IKK 0
JRNL AUTH G.JOB,C.BRUGGER,T.XU,B.R.LOWE,Y.PFISTER,C.QU,S.SHANKER,
JRNL AUTH 2 J.I.BANOS SANZ,J.F.PARTRIDGE,T.SCHALCH
JRNL TITL SHREC SILENCES HETEROCHROMATIN VIA DISTINCT REMODELING AND
JRNL TITL 2 DEACETYLATION MODULES.
JRNL REF MOL.CELL V. 62 207 2016
JRNL REFN ISSN 1097-2765
JRNL PMID 27105116
JRNL DOI 10.1016/J.MOLCEL.2016.03.016
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 31826
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790
REMARK 3 FREE R VALUE TEST SET COUNT : 1524
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 46.8236 - 5.3352 1.00 2944 148 0.1716 0.1949
REMARK 3 2 5.3352 - 4.2356 1.00 2831 141 0.1417 0.1865
REMARK 3 3 4.2356 - 3.7004 1.00 2807 141 0.1576 0.1941
REMARK 3 4 3.7004 - 3.3622 1.00 2750 138 0.1669 0.2114
REMARK 3 5 3.3622 - 3.1213 1.00 2780 139 0.1924 0.2554
REMARK 3 6 3.1213 - 2.9373 1.00 2780 139 0.2021 0.2165
REMARK 3 7 2.9373 - 2.7902 1.00 2736 138 0.2140 0.2606
REMARK 3 8 2.7902 - 2.6687 1.00 2749 137 0.2193 0.2796
REMARK 3 9 2.6687 - 2.5660 1.00 2745 138 0.2382 0.2814
REMARK 3 10 2.5660 - 2.4775 1.00 2740 138 0.2561 0.2767
REMARK 3 11 2.4775 - 2.4000 0.90 2440 127 0.2755 0.3360
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.30
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 : 0.006 4859
REMARK 3 ANGLE : 0.646 6551
REMARK 3 CHIRALITY : 0.028 719
REMARK 3 PLANARITY : 0.003 847
REMARK 3 DIHEDRAL : 11.392 1757
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 54 THROUGH 420)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0244 65.1010 -21.9546
REMARK 3 T TENSOR
REMARK 3 T11: 0.1810 T22: 0.2709
REMARK 3 T33: 0.1736 T12: -0.1439
REMARK 3 T13: -0.1133 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 2.4613 L22: 1.3436
REMARK 3 L33: 2.5269 L12: -0.4452
REMARK 3 L13: -0.3521 L23: 0.0725
REMARK 3 S TENSOR
REMARK 3 S11: 0.2747 S12: -0.6336 S13: -0.0272
REMARK 3 S21: 0.2356 S22: 0.0565 S23: -0.2170
REMARK 3 S31: -0.0872 S32: 0.3230 S33: -0.0841
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 421 THROUGH 680)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3293 17.9836 -49.4468
REMARK 3 T TENSOR
REMARK 3 T11: 0.3043 T22: 0.2368
REMARK 3 T33: 0.2962 T12: 0.0228
REMARK 3 T13: 0.0793 T23: 0.0802
REMARK 3 L TENSOR
REMARK 3 L11: 2.2424 L22: 1.4612
REMARK 3 L33: 2.2357 L12: -0.3123
REMARK 3 L13: -0.9046 L23: 0.2532
REMARK 3 S TENSOR
REMARK 3 S11: -0.0265 S12: 0.2166 S13: 0.0703
REMARK 3 S21: -0.3122 S22: -0.0550 S23: -0.3497
REMARK 3 S31: 0.1811 S32: 0.3509 S33: 0.1000
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 5IKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
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 : 31830
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 46.815
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.60000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
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: 2VQW (HDAC4)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ETHYLENEGLYCOL 10% PEG 8000 0.1M
REMARK 280 MOPS/HEPES 0.04M SODIUM NITRATE 0.04M SODIUM MONOPHOSPHATE 0.04M
REMARK 280 AMMONIUM SULFATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.31650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.31650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 30.24350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 93.62950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.24350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 93.62950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.31650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.24350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 93.62950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.31650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.24350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 93.62950
REMARK 290 SMTRY3 8 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: 10930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -127.0 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 -71.31650
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 THR A 31
REMARK 465 ASN A 32
REMARK 465 ASN A 33
REMARK 465 LYS A 34
REMARK 465 PRO A 35
REMARK 465 MET A 36
REMARK 465 SER A 37
REMARK 465 GLY A 38
REMARK 465 SER A 39
REMARK 465 GLU A 40
REMARK 465 ASN A 41
REMARK 465 THR A 42
REMARK 465 LEU A 43
REMARK 465 ASN A 44
REMARK 465 ASN A 45
REMARK 465 GLU A 46
REMARK 465 SER A 47
REMARK 465 HIS A 48
REMARK 465 GLU A 49
REMARK 465 MET A 50
REMARK 465 SER A 51
REMARK 465 GLN A 52
REMARK 465 ILE A 53
REMARK 465 VAL A 74
REMARK 465 ASP A 75
REMARK 465 ASP A 76
REMARK 465 ARG A 131
REMARK 465 VAL A 132
REMARK 465 THR A 133
REMARK 465 ASN A 134
REMARK 465 THR A 135
REMARK 465 GLU A 136
REMARK 465 GLU A 197
REMARK 465 PRO A 198
REMARK 465 HIS A 199
REMARK 465 LYS A 200
REMARK 465 PRO A 201
REMARK 465 GLY A 202
REMARK 465 GLY A 203
REMARK 465 PHE A 204
REMARK 465 CYS A 205
REMARK 465 SER A 462
REMARK 465 VAL A 463
REMARK 465 SER A 464
REMARK 465 ASN A 465
REMARK 465 VAL A 466
REMARK 465 PHE A 467
REMARK 465 VAL A 538
REMARK 465 THR A 539
REMARK 465 ASP A 540
REMARK 465 GLY A 541
REMARK 465 GLU A 542
REMARK 465 ASN A 543
REMARK 465 ALA A 544
REMARK 465 PRO A 545
REMARK 465 VAL A 546
REMARK 465 LYS A 681
REMARK 465 ALA A 682
REMARK 465 ARG A 683
REMARK 465 PRO A 684
REMARK 465 THR A 685
REMARK 465 SER A 686
REMARK 465 GLN A 687
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 VAL A 188 60.99 -114.04
REMARK 500 VAL A 307 -62.76 -123.75
REMARK 500 GLU A 364 -130.77 -125.26
REMARK 500 ASN A 469 10.08 59.87
REMARK 500 TYR A 563 -53.27 -129.27
REMARK 500 GLU A 618 -63.57 -123.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 703 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 68 NE2
REMARK 620 2 HIS A 77 NE2 103.2
REMARK 620 3 CYS A 162 SG 96.4 135.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 195 NE2
REMARK 620 2 ASP A 234 OD1 139.7
REMARK 620 3 ASP A 234 OD2 113.9 63.2
REMARK 620 4 HIS A 236 ND1 88.3 95.7 156.8
REMARK 620 5 ASP A 327 OD2 103.9 114.8 82.5 99.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 704 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 232 O
REMARK 620 2 ASP A 232 OD1 71.4
REMARK 620 3 ASP A 232 OD2 91.6 39.6
REMARK 620 4 ASP A 234 O 95.5 88.7 121.0
REMARK 620 5 HIS A 236 O 161.7 94.0 83.3 72.6
REMARK 620 6 SER A 255 OG 86.9 125.4 94.6 144.1 110.9
REMARK 620 7 LEU A 256 O 72.2 129.7 163.8 61.7 111.9 85.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 702 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 245 O
REMARK 620 2 ASP A 248 O 71.6
REMARK 620 3 VAL A 251 O 117.7 82.7
REMARK 620 4 ARG A 284 O 155.7 122.0 85.4
REMARK 620 5 HOH A 822 O 85.3 96.4 154.9 73.7
REMARK 620 6 HOH A 856 O 73.2 144.7 116.4 90.3 78.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 712 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 427 O
REMARK 620 2 ASP A 429 O 98.9
REMARK 620 3 VAL A 432 O 101.3 97.9
REMARK 620 4 HOH A 906 O 90.5 170.2 82.5
REMARK 620 5 HOH A 934 O 85.5 94.7 164.6 83.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 712
DBREF 5IKK A 31 687 UNP P56523 CLR3_SCHPO 31 687
SEQRES 1 A 657 THR ASN ASN LYS PRO MET SER GLY SER GLU ASN THR LEU
SEQRES 2 A 657 ASN ASN GLU SER HIS GLU MET SER GLN ILE LEU LYS LYS
SEQRES 3 A 657 SER GLY LEU CYS TYR ASP PRO ARG MET ARG PHE HIS ALA
SEQRES 4 A 657 THR LEU SER GLU VAL ASP ASP HIS PRO GLU ASP PRO ARG
SEQRES 5 A 657 ARG VAL LEU ARG VAL PHE GLU ALA ILE LYS LYS ALA GLY
SEQRES 6 A 657 TYR VAL SER ASN VAL PRO SER PRO SER ASP VAL PHE LEU
SEQRES 7 A 657 ARG ILE PRO ALA ARG GLU ALA THR LEU GLU GLU LEU LEU
SEQRES 8 A 657 GLN VAL HIS SER GLN GLU MET TYR ASP ARG VAL THR ASN
SEQRES 9 A 657 THR GLU LYS MET SER HIS GLU ASP LEU ALA ASN LEU GLU
SEQRES 10 A 657 LYS ILE SER ASP SER LEU TYR TYR ASN ASN GLU SER ALA
SEQRES 11 A 657 PHE CYS ALA ARG LEU ALA CYS GLY SER ALA ILE GLU THR
SEQRES 12 A 657 CYS THR ALA VAL VAL THR GLY GLN VAL LYS ASN ALA PHE
SEQRES 13 A 657 ALA VAL VAL ARG PRO PRO GLY HIS HIS ALA GLU PRO HIS
SEQRES 14 A 657 LYS PRO GLY GLY PHE CYS LEU PHE ASN ASN VAL SER VAL
SEQRES 15 A 657 THR ALA ARG SER MET LEU GLN ARG PHE PRO ASP LYS ILE
SEQRES 16 A 657 LYS ARG VAL LEU ILE VAL ASP TRP ASP ILE HIS HIS GLY
SEQRES 17 A 657 ASN GLY THR GLN MET ALA PHE TYR ASP ASP PRO ASN VAL
SEQRES 18 A 657 LEU TYR VAL SER LEU HIS ARG TYR GLU ASN GLY ARG PHE
SEQRES 19 A 657 TYR PRO GLY THR ASN TYR GLY CYS ALA GLU ASN CYS GLY
SEQRES 20 A 657 GLU GLY PRO GLY LEU GLY ARG THR VAL ASN ILE PRO TRP
SEQRES 21 A 657 SER CYS ALA GLY MET GLY ASP GLY ASP TYR ILE TYR ALA
SEQRES 22 A 657 PHE GLN ARG VAL VAL MET PRO VAL ALA TYR GLU PHE ASP
SEQRES 23 A 657 PRO ASP LEU VAL ILE VAL SER CYS GLY PHE ASP ALA ALA
SEQRES 24 A 657 ALA GLY ASP HIS ILE GLY GLN PHE LEU LEU THR PRO ALA
SEQRES 25 A 657 ALA TYR ALA HIS MET THR GLN MET LEU MET GLY LEU ALA
SEQRES 26 A 657 ASP GLY LYS VAL PHE ILE SER LEU GLU GLY GLY TYR ASN
SEQRES 27 A 657 LEU ASP SER ILE SER THR SER ALA LEU ALA VAL ALA GLN
SEQRES 28 A 657 SER LEU LEU GLY ILE PRO PRO GLY ARG LEU HIS THR THR
SEQRES 29 A 657 TYR ALA CYS PRO GLN ALA VAL ALA THR ILE ASN HIS VAL
SEQRES 30 A 657 THR LYS ILE GLN SER GLN TYR TRP ARG CYS MET ARG PRO
SEQRES 31 A 657 LYS HIS PHE ASP ALA ASN PRO LYS ASP ALA HIS VAL ASP
SEQRES 32 A 657 ARG LEU HIS ASP VAL ILE ARG THR TYR GLN ALA LYS LYS
SEQRES 33 A 657 LEU PHE GLU ASP TRP LYS ILE THR ASN MET PRO ILE LEU
SEQRES 34 A 657 ARG ASP SER VAL SER ASN VAL PHE ASN ASN GLN VAL LEU
SEQRES 35 A 657 CYS SER SER ASN PHE PHE GLN LYS ASP ASN LEU LEU VAL
SEQRES 36 A 657 ILE VAL HIS GLU SER PRO ARG VAL LEU GLY ASN GLY THR
SEQRES 37 A 657 SER GLU THR ASN VAL LEU ASN LEU ASN ASP SER LEU LEU
SEQRES 38 A 657 VAL ASP PRO VAL SER LEU TYR VAL GLU TRP ALA MET GLN
SEQRES 39 A 657 GLN ASP TRP GLY LEU ILE ASP ILE ASN ILE PRO GLU VAL
SEQRES 40 A 657 VAL THR ASP GLY GLU ASN ALA PRO VAL ASP ILE LEU SER
SEQRES 41 A 657 GLU VAL LYS GLU LEU CYS LEU TYR VAL TRP ASP ASN TYR
SEQRES 42 A 657 VAL GLU LEU SER ILE SER LYS ASN ILE PHE PHE ILE GLY
SEQRES 43 A 657 GLY GLY LYS ALA VAL HIS GLY LEU VAL ASN LEU ALA SER
SEQRES 44 A 657 SER ARG ASN VAL SER ASP ARG VAL LYS CYS MET VAL ASN
SEQRES 45 A 657 PHE LEU GLY THR GLU PRO LEU VAL GLY LEU LYS THR ALA
SEQRES 46 A 657 SER GLU GLU ASP LEU PRO THR TRP TYR TYR ARG HIS SER
SEQRES 47 A 657 LEU VAL PHE VAL SER SER SER ASN GLU CYS TRP LYS LYS
SEQRES 48 A 657 ALA LYS ARG ALA LYS ARG ARG TYR GLY ARG LEU MET GLN
SEQRES 49 A 657 SER GLU HIS THR GLU THR SER ASP MET MET GLU GLN HIS
SEQRES 50 A 657 TYR ARG ALA VAL THR GLN TYR LEU LEU HIS LEU LEU GLN
SEQRES 51 A 657 LYS ALA ARG PRO THR SER GLN
HET ZN A 701 1
HET K A 702 1
HET ZN A 703 1
HET K A 704 1
HET NO3 A 705 4
HET NO3 A 706 4
HET NO3 A 707 4
HET EDO A 708 10
HET EDO A 709 10
HET EDO A 710 10
HET SO4 A 711 5
HET MG A 712 1
HETNAM ZN ZINC ION
HETNAM K POTASSIUM ION
HETNAM NO3 NITRATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ZN 2(ZN 2+)
FORMUL 3 K 2(K 1+)
FORMUL 6 NO3 3(N O3 1-)
FORMUL 9 EDO 3(C2 H6 O2)
FORMUL 12 SO4 O4 S 2-
FORMUL 13 MG MG 2+
FORMUL 14 HOH *213(H2 O)
HELIX 1 AA1 ARG A 64 ALA A 69 1 6
HELIX 2 AA2 PRO A 81 ALA A 94 1 14
HELIX 3 AA3 THR A 116 ASP A 130 1 15
HELIX 4 AA4 SER A 139 LEU A 143 5 5
HELIX 5 AA5 ASN A 145 SER A 152 1 8
HELIX 6 AA6 SER A 159 THR A 179 1 21
HELIX 7 AA7 ASN A 208 PHE A 221 1 14
HELIX 8 AA8 GLY A 238 TYR A 246 1 9
HELIX 9 AA9 THR A 268 CYS A 272 5 5
HELIX 10 AB1 GLU A 278 LEU A 282 5 5
HELIX 11 AB2 GLY A 296 VAL A 307 1 12
HELIX 12 AB3 VAL A 307 ASP A 316 1 10
HELIX 13 AB4 THR A 340 MET A 352 1 13
HELIX 14 AB5 GLY A 353 GLY A 357 5 5
HELIX 15 AB6 ASN A 368 LEU A 384 1 17
HELIX 16 AB7 CYS A 397 SER A 412 1 16
HELIX 17 AB8 ARG A 434 LYS A 452 1 19
HELIX 18 AB9 ASN A 476 LYS A 480 5 5
HELIX 19 AC1 PRO A 514 GLN A 525 1 12
HELIX 20 AC2 ILE A 548 TYR A 563 1 16
HELIX 21 AC3 LYS A 579 ARG A 591 1 13
HELIX 22 AC4 GLU A 618 HIS A 627 1 10
HELIX 23 AC5 ASN A 636 LYS A 640 5 5
HELIX 24 AC6 LYS A 646 GLY A 650 5 5
HELIX 25 AC7 GLU A 659 HIS A 667 1 9
HELIX 26 AC8 HIS A 667 LEU A 679 1 13
SHEET 1 AA1 8 PHE A 107 ILE A 110 0
SHEET 2 AA1 8 SER A 57 TYR A 61 1 N SER A 57 O LEU A 108
SHEET 3 AA1 8 ASN A 184 VAL A 188 1 O ASN A 184 N GLY A 58
SHEET 4 AA1 8 VAL A 359 LEU A 363 1 O ILE A 361 N ALA A 185
SHEET 5 AA1 8 LEU A 319 CYS A 324 1 N VAL A 322 O PHE A 360
SHEET 6 AA1 8 VAL A 228 ASP A 232 1 N LEU A 229 O LEU A 319
SHEET 7 AA1 8 VAL A 251 ARG A 258 1 O LEU A 252 N ILE A 230
SHEET 8 AA1 8 THR A 285 TRP A 290 1 O ILE A 288 N SER A 255
SHEET 1 AA2 8 THR A 454 ASN A 455 0
SHEET 2 AA2 8 VAL A 471 CYS A 473 -1 O CYS A 473 N THR A 454
SHEET 3 AA2 8 GLY A 528 ASN A 533 -1 O ASP A 531 N LEU A 472
SHEET 4 AA2 8 ASN A 482 HIS A 488 1 N ASN A 482 O GLY A 528
SHEET 5 AA2 8 ASN A 571 GLY A 577 1 O ILE A 575 N VAL A 487
SHEET 6 AA2 8 VAL A 597 PHE A 603 1 O VAL A 601 N PHE A 574
SHEET 7 AA2 8 SER A 628 VAL A 632 1 O LEU A 629 N ASN A 602
SHEET 8 AA2 8 LEU A 652 GLN A 654 1 O MET A 653 N VAL A 630
SHEET 1 AA3 2 ARG A 492 LEU A 494 0
SHEET 2 AA3 2 LEU A 510 VAL A 512 -1 O VAL A 512 N ARG A 492
LINK NE2 HIS A 68 ZN ZN A 703 1555 1555 2.03
LINK NE2 HIS A 77 ZN ZN A 703 1555 1555 2.04
LINK SG CYS A 162 ZN ZN A 703 1555 1555 2.34
LINK NE2 HIS A 195 ZN ZN A 701 1555 1555 1.99
LINK O ASP A 232 K K A 704 1555 1555 2.82
LINK OD1 ASP A 232 K K A 704 1555 1555 2.82
LINK OD2 ASP A 232 K K A 704 1555 1555 3.44
LINK O ASP A 234 K K A 704 1555 1555 2.77
LINK OD1 ASP A 234 ZN ZN A 701 1555 1555 2.06
LINK OD2 ASP A 234 ZN ZN A 701 1555 1555 2.09
LINK O HIS A 236 K K A 704 1555 1555 2.89
LINK ND1 HIS A 236 ZN ZN A 701 1555 1555 2.04
LINK O PHE A 245 K K A 702 1555 1555 2.66
LINK O ASP A 248 K K A 702 1555 1555 2.84
LINK O VAL A 251 K K A 702 1555 1555 2.61
LINK OG SER A 255 K K A 704 1555 1555 2.79
LINK O LEU A 256 K K A 704 1555 1555 3.04
LINK O ARG A 284 K K A 702 1555 1555 2.83
LINK OD2 ASP A 327 ZN ZN A 701 1555 1555 1.99
LINK O PRO A 427 MG MG A 712 1555 1555 2.26
LINK O ASP A 429 MG MG A 712 1555 1555 2.13
LINK O VAL A 432 MG MG A 712 1555 1555 2.24
LINK K K A 702 O HOH A 822 1555 1555 2.81
LINK K K A 702 O HOH A 856 1555 1555 2.83
LINK MG MG A 712 O HOH A 906 1555 1555 2.08
LINK MG MG A 712 O HOH A 934 1555 1555 2.08
CISPEP 1 TYR A 265 PRO A 266 0 4.22
CISPEP 2 ARG A 419 PRO A 420 0 -1.06
SITE 1 AC1 4 HIS A 195 ASP A 234 HIS A 236 ASP A 327
SITE 1 AC2 6 PHE A 245 ASP A 248 VAL A 251 ARG A 284
SITE 2 AC2 6 HOH A 822 HOH A 856
SITE 1 AC3 3 HIS A 68 HIS A 77 CYS A 162
SITE 1 AC4 5 ASP A 232 ASP A 234 HIS A 236 SER A 255
SITE 2 AC4 5 LEU A 256
SITE 1 AC5 6 ARG A 64 MET A 65 ARG A 66 LYS A 452
SITE 2 AC5 6 ASN A 476 HOH A 808
SITE 1 AC6 6 TYR A 313 ASP A 316 HIS A 346 ARG A 390
SITE 2 AC6 6 LEU A 391 HOH A 967
SITE 1 AC7 4 SER A 412 GLN A 413 TYR A 414 ARG A 419
SITE 1 AC8 3 TYR A 302 ARG A 416 ARG A 419
SITE 1 AC9 8 ARG A 440 HIS A 488 ASP A 513 VAL A 515
SITE 2 AC9 8 SER A 516 ASP A 531 HOH A 925 HOH A 954
SITE 1 AD1 4 ASP A 80 GLY A 366 TYR A 367 LEU A 369
SITE 1 AD2 6 TYR A 129 GLU A 617 PRO A 621 LYS A 646
SITE 2 AD2 6 ARG A 647 ARG A 648
SITE 1 AD3 5 PRO A 427 ASP A 429 VAL A 432 HOH A 906
SITE 2 AD3 5 HOH A 934
CRYST1 60.487 187.259 142.633 90.00 90.00 90.00 C 2 2 21 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 0.016532 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005340 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007011 0.00000
TER 9290 GLN A 680
MASTER 450 0 12 26 18 0 19 6 4952 1 82 51
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