HEADER HYDROLASE 07-SEP-08 3EF1
TITLE THE STRUCTURE OF FCP1, AN ESSENTIAL RNA POLYMERASE II CTD PHOSPHATASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FCP1 HOMOLOGY DOMAIN, CATALYTICALLY ACTIVE FRAGMENT, UNP
COMPND 5 RESIDUES 140-580;
COMPND 6 SYNONYM: CTD PHOSPHATASE FCP1;
COMPND 7 EC: 3.1.3.16;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 4896;
SOURCE 5 GENE: FCP1, SPAC19B12.05C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B-SMT3
KEYWDS PHOSPHATASE, CTD, FCPH, BRCT, HYDROLASE, BEF3, ACYLPHOSPHATE ANALOG,
KEYWDS 2 COBALT, MAGNESIUM, MANGANESE, METAL-BINDING, NUCLEUS, PROTEIN
KEYWDS 3 PHOSPHATASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GHOSH,C.D.LIMA
REVDAT 3 25-OCT-17 3EF1 1 REMARK
REVDAT 2 19-JUN-13 3EF1 1 JRNL VERSN
REVDAT 1 02-DEC-08 3EF1 0
JRNL AUTH A.GHOSH,S.SHUMAN,C.D.LIMA
JRNL TITL THE STRUCTURE OF FCP1, AN ESSENTIAL RNA POLYMERASE II CTD
JRNL TITL 2 PHOSPHATASE.
JRNL REF MOL.CELL V. 32 478 2008
JRNL REFN ISSN 1097-2765
JRNL PMID 19026779
JRNL DOI 10.1016/J.MOLCEL.2008.09.021
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1787288.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 28751
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1450
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4207
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 236
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2979
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 163
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.06000
REMARK 3 B22 (A**2) : -6.17000
REMARK 3 B33 (A**2) : 2.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 30.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.680 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.940 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.420 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.770 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 64.11
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP-BFD-AGNI.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN-BFD-AGNI.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3EF1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29320
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0430
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: FCP1-BEF3-MG WAS OBTAINED BY
REMARK 280 INCUBATING 200 M FCP1(140-580) WITH 225 M CTD PEPTIDE
REMARK 280 (SPSYSPTSPS), 300 M BECL2, 5 MM NAF AND 5 MM MGCL2 ON ICE FOR 1
REMARK 280 H THEN CRYSTALLIZED BY SITTING DROP VAPOR DIFFUSION AGAINST 22%
REMARK 280 PEG-4000, 100 MM NA-CITRATE (PH 5.6), 100 MM AMMONIUM ACETATE, 5%
REMARK 280 HEXANE 1,6-DIOL, 5% AMINOCAPROIC ACID, 5% PROPANE-1,3-DIOL, 5
REMARK 280 MM DTT., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 26.83150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.58500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.22100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.58500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.83150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.22100
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 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 ASN A 327
REMARK 465 PHE A 328
REMARK 465 LEU A 329
REMARK 465 ALA A 330
REMARK 465 LYS A 331
REMARK 465 SER A 332
REMARK 465 THR A 333
REMARK 465 PRO A 334
REMARK 465 LEU A 335
REMARK 465 PRO A 336
REMARK 465 GLU A 337
REMARK 465 GLN A 338
REMARK 465 GLU A 339
REMARK 465 GLN A 340
REMARK 465 LEU A 341
REMARK 465 ILE A 342
REMARK 465 PRO A 343
REMARK 465 LEU A 344
REMARK 465 GLU A 345
REMARK 465 ILE A 346
REMARK 465 PRO A 347
REMARK 465 LYS A 348
REMARK 465 ASP A 349
REMARK 465 GLU A 350
REMARK 465 PRO A 351
REMARK 465 ASP A 352
REMARK 465 SER A 353
REMARK 465 VAL A 354
REMARK 465 ASP A 355
REMARK 465 GLU A 356
REMARK 465 ILE A 357
REMARK 465 ASN A 358
REMARK 465 GLU A 359
REMARK 465 GLU A 360
REMARK 465 ASN A 361
REMARK 465 GLU A 362
REMARK 465 GLU A 363
REMARK 465 THR A 364
REMARK 465 PRO A 365
REMARK 465 GLU A 366
REMARK 465 TYR A 367
REMARK 465 ASP A 368
REMARK 465 SER A 369
REMARK 465 SER A 370
REMARK 465 ASN A 371
REMARK 465 SER A 372
REMARK 465 SER A 373
REMARK 465 TYR A 374
REMARK 465 ALA A 375
REMARK 465 GLN A 376
REMARK 465 ASP A 377
REMARK 465 SER A 378
REMARK 465 SER A 379
REMARK 465 THR A 380
REMARK 465 ILE A 381
REMARK 465 PRO A 382
REMARK 465 GLU A 383
REMARK 465 LYS A 384
REMARK 465 THR A 385
REMARK 465 LEU A 386
REMARK 465 LEU A 387
REMARK 465 LYS A 388
REMARK 465 ASP A 389
REMARK 465 THR A 390
REMARK 465 PHE A 391
REMARK 465 LEU A 392
REMARK 465 GLN A 393
REMARK 465 ASN A 394
REMARK 465 ARG A 395
REMARK 465 GLU A 396
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 SER A 139 CB OG
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 ASP A 140 22.82 -71.42
REMARK 500 LEU A 171 -79.44 -95.04
REMARK 500 PRO A 211 -112.35 -18.67
REMARK 500 SER A 212 54.34 -113.65
REMARK 500 GLN A 265 -125.90 59.28
REMARK 500 GLU A 316 76.07 -114.87
REMARK 500 ASN A 325 64.69 -116.15
REMARK 500 GLU A 429 115.25 -27.40
REMARK 500 PRO A 432 89.52 -61.06
REMARK 500 ASN A 441 56.35 -109.18
REMARK 500 ARG A 442 68.83 -109.06
REMARK 500 ASP A 466 35.68 -91.93
REMARK 500 SER A 468 93.82 -53.08
REMARK 500 SER A 469 59.18 175.64
REMARK 500 ARG A 470 90.19 70.94
REMARK 500 ASN A 473 49.72 -95.91
REMARK 500 HIS A 474 -81.21 -90.97
REMARK 500 ALA A 538 62.19 -102.15
REMARK 500 LYS A 539 53.70 39.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EF0 RELATED DB: PDB
REMARK 900 FCP1-ALF4-MG
DBREF 3EF1 A 140 580 UNP Q9P376 FCP1_SCHPO 140 580
SEQADV 3EF1 SER A 139 UNP Q9P376 EXPRESSION TAG
SEQRES 1 A 442 SER ASP LEU THR VAL SER LEU GLU GLU ALA SER ARG LEU
SEQRES 2 A 442 GLU SER GLU ASN VAL LYS ARG LEU ARG GLN GLU LYS ARG
SEQRES 3 A 442 LEU SER LEU ILE VAL BFD LEU ASP GLN THR ILE ILE HIS
SEQRES 4 A 442 ALA THR VAL ASP PRO THR VAL GLY GLU TRP MET SER ASP
SEQRES 5 A 442 PRO GLY ASN VAL ASN TYR ASP VAL LEU ARG ASP VAL ARG
SEQRES 6 A 442 SER PHE ASN LEU GLN GLU GLY PRO SER GLY TYR THR SER
SEQRES 7 A 442 CYS TYR TYR ILE LYS PHE ARG PRO GLY LEU ALA GLN PHE
SEQRES 8 A 442 LEU GLN LYS ILE SER GLU LEU TYR GLU LEU HIS ILE TYR
SEQRES 9 A 442 THR MET GLY THR LYS ALA TYR ALA LYS GLU VAL ALA LYS
SEQRES 10 A 442 ILE ILE ASP PRO THR GLY LYS LEU PHE GLN ASP ARG VAL
SEQRES 11 A 442 LEU SER ARG ASP ASP SER GLY SER LEU ALA GLN LYS SER
SEQRES 12 A 442 LEU ARG ARG LEU PHE PRO CYS ASP THR SER MET VAL VAL
SEQRES 13 A 442 VAL ILE ASP ASP ARG GLY ASP VAL TRP ASP TRP ASN PRO
SEQRES 14 A 442 ASN LEU ILE LYS VAL VAL PRO TYR GLU PHE PHE VAL GLY
SEQRES 15 A 442 ILE GLY ASP ILE ASN SER ASN PHE LEU ALA LYS SER THR
SEQRES 16 A 442 PRO LEU PRO GLU GLN GLU GLN LEU ILE PRO LEU GLU ILE
SEQRES 17 A 442 PRO LYS ASP GLU PRO ASP SER VAL ASP GLU ILE ASN GLU
SEQRES 18 A 442 GLU ASN GLU GLU THR PRO GLU TYR ASP SER SER ASN SER
SEQRES 19 A 442 SER TYR ALA GLN ASP SER SER THR ILE PRO GLU LYS THR
SEQRES 20 A 442 LEU LEU LYS ASP THR PHE LEU GLN ASN ARG GLU ALA LEU
SEQRES 21 A 442 GLU GLU GLN ASN LYS GLU ARG VAL THR ALA LEU GLU LEU
SEQRES 22 A 442 GLN LYS SER GLU ARG PRO LEU ALA LYS GLN GLN ASN ALA
SEQRES 23 A 442 LEU LEU GLU ASP GLU GLY LYS PRO THR PRO SER HIS THR
SEQRES 24 A 442 LEU LEU HIS ASN ARG ASP HIS GLU LEU GLU ARG LEU GLU
SEQRES 25 A 442 LYS VAL LEU LYS ASP ILE HIS ALA VAL TYR TYR GLU GLU
SEQRES 26 A 442 GLU ASN ASP ILE SER SER ARG SER GLY ASN HIS LYS HIS
SEQRES 27 A 442 ALA ASN VAL GLY LEU ILE ILE PRO LYS MET LYS GLN LYS
SEQRES 28 A 442 VAL LEU LYS GLY CYS ARG LEU LEU PHE SER GLY VAL ILE
SEQRES 29 A 442 PRO LEU GLY VAL ASP VAL LEU SER SER ASP ILE ALA LYS
SEQRES 30 A 442 TRP ALA MET SER PHE GLY ALA GLU VAL VAL LEU ASP PHE
SEQRES 31 A 442 SER VAL PRO PRO THR HIS LEU ILE ALA ALA LYS ILE ARG
SEQRES 32 A 442 THR GLU LYS VAL LYS LYS ALA VAL SER MET GLY ASN ILE
SEQRES 33 A 442 LYS VAL VAL LYS LEU ASN TRP LEU THR GLU SER LEU SER
SEQRES 34 A 442 GLN TRP LYS ARG LEU PRO GLU SER ASP TYR LEU LEU TYR
MODRES 3EF1 BFD A 170 ASP ASPARTATE BERYLLIUM TRIFLUORIDE
HET BFD A 170 12
HET MG A 1 1
HETNAM BFD ASPARTATE BERYLLIUM TRIFLUORIDE
HETNAM MG MAGNESIUM ION
FORMUL 1 BFD C4 H6 BE F3 N O4 2-
FORMUL 2 MG MG 2+
FORMUL 3 HOH *163(H2 O)
HELIX 1 1 LEU A 141 GLU A 162 1 22
HELIX 2 2 PRO A 182 SER A 189 1 8
HELIX 3 3 TYR A 196 ARG A 200 5 5
HELIX 4 4 GLY A 225 SER A 234 1 10
HELIX 5 5 THR A 246 ASP A 258 1 13
HELIX 6 6 SER A 281 LEU A 285 5 5
HELIX 7 7 GLY A 300 ASP A 304 5 5
HELIX 8 8 ALA A 397 ARG A 416 1 20
HELIX 9 9 ARG A 416 GLU A 427 1 12
HELIX 10 10 PRO A 432 THR A 437 1 6
HELIX 11 11 HIS A 444 ASP A 466 1 23
HELIX 12 12 ASN A 478 LYS A 489 1 12
HELIX 13 13 SER A 511 SER A 519 1 9
HELIX 14 14 THR A 542 GLY A 552 1 11
HELIX 15 15 LEU A 559 TRP A 569 1 11
HELIX 16 16 PRO A 573 ASP A 576 5 4
SHEET 1 A 5 VAL A 268 LEU A 269 0
SHEET 2 A 5 TYR A 237 TYR A 242 1 N ILE A 241 O LEU A 269
SHEET 3 A 5 LEU A 165 VAL A 169 1 N VAL A 169 O HIS A 240
SHEET 4 A 5 VAL A 293 ASP A 297 1 O VAL A 294 N ILE A 168
SHEET 5 A 5 LEU A 309 LYS A 311 1 O ILE A 310 N VAL A 295
SHEET 1 B 3 ILE A 176 THR A 179 0
SHEET 2 B 3 TYR A 214 PHE A 222 -1 O TYR A 219 N THR A 179
SHEET 3 B 3 ARG A 203 GLU A 209 -1 N ARG A 203 O ILE A 220
SHEET 1 C 5 GLU A 523 VAL A 524 0
SHEET 2 C 5 ARG A 495 SER A 499 1 N LEU A 496 O GLU A 523
SHEET 3 C 5 HIS A 534 ALA A 537 1 O ILE A 536 N LEU A 497
SHEET 4 C 5 LYS A 555 LYS A 558 1 O LYS A 555 N LEU A 535
SHEET 5 C 5 LEU A 578 TYR A 580 -1 O LEU A 579 N VAL A 556
LINK C VAL A 169 N BFD A 170 1555 1555 1.33
LINK C BFD A 170 N LEU A 171 1555 1555 1.33
SITE 1 AC1 5 BFD A 170 ASP A 172 ASP A 298 HOH A 622
SITE 2 AC1 5 HOH A 623
CRYST1 53.663 88.442 113.170 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 0.018635 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011307 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008836 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
