HEADER TRANSFERASE 17-OCT-03 1R6X
TITLE THE CRYSTAL STRUCTURE OF A TRUNCATED FORM OF YEAST ATP SULFURYLASE,
TITLE 2 LACKING THE C-TERMINAL APS KINASE-LIKE DOMAIN, IN COMPLEX WITH
TITLE 3 SULFATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP:SULFATE ADENYLYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-393;
COMPND 5 SYNONYM: SULFATE ADENYLYLTRANSFERASE, SULFATE ADENYLATE TRANSFERASE,
COMPND 6 SAT, ATP-SULFURYLASE;
COMPND 7 EC: 2.7.7.4;
COMPND 8 ENGINEERED: YES
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: MET3, YJR010W, J1436;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTYB1
KEYWDS APS KINASE-LIKE DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.LALOR,T.SCHNYDER,V.SARIDAKIS,D.E.PILLOFF,A.DONG,H.TANG,T.S.LEYH,
AUTHOR 2 E.F.PAI
REVDAT 4 23-AUG-23 1R6X 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1R6X 1 VERSN
REVDAT 2 30-MAR-04 1R6X 1 JRNL
REVDAT 1 11-NOV-03 1R6X 0
JRNL AUTH D.J.LALOR,T.SCHNYDER,V.SARIDAKIS,D.E.PILLOFF,A.DONG,H.TANG,
JRNL AUTH 2 T.S.LEYH,E.F.PAI
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF A TRUNCATED FORM OF
JRNL TITL 2 SACCHAROMYCES CEREVISIAE ATP SULFURYLASE: C-TERMINAL DOMAIN
JRNL TITL 3 ESSENTIAL FOR OLIGOMER FORMATION BUT NOT FOR ACTIVITY
JRNL REF PROTEIN ENG. V. 16 1071 2003
JRNL REFN ISSN 0269-2139
JRNL PMID 14983089
JRNL DOI 10.1093/PROTEIN/GZG133
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 431027.230
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.0
REMARK 3 NUMBER OF REFLECTIONS : 66736
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) : 0.197
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1342
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5799
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE : 0.2250
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 116
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3098
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 432
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.05000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -1.28000
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) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.06
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.06
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
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) : 1.090 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.750 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.690 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 42.30
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020511.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90
REMARK 200 MONOCHROMATOR : BENT CYLINDRICAL GE(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67770
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 40.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1J70
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9M (NH4)SO4, 0.1M MES, 0.01 M
REMARK 280 COBALTOUS CHLORIDE, 8% GLYCEROL, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 25.09300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.58250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.55550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.58250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.09300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.55550
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 300 REMARK: THE ATP SULFURYLASE MONOMER IS THE ASYMMETRIC UNIT
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 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 388
REMARK 465 PRO A 389
REMARK 465 PRO A 390
REMARK 465 ARG A 391
REMARK 465 PRO A 392
REMARK 465 LYS A 393
REMARK 465 GLY A 394
REMARK 465 SER A 395
REMARK 465 SER A 396
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 TRP A 80 113.06 -165.86
REMARK 500 ASP A 99 -7.50 82.67
REMARK 500 GLU A 109 -28.84 -145.05
REMARK 500 TYR A 169 75.33 37.96
REMARK 500 THR A 228 -148.25 -116.18
REMARK 500 SER A 266 37.57 -95.31
REMARK 500 THR A 348 81.80 -62.45
REMARK 500 THR A 349 -146.22 -142.07
REMARK 500 LYS A 350 73.59 -101.40
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 CO A3000 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 168 OD2
REMARK 620 2 HIS A 235 NE2 111.8
REMARK 620 3 HIS A 236 NE2 112.2 90.3
REMARK 620 4 HOH A4265 O 72.4 94.2 171.8
REMARK 620 5 HOH A4355 O 71.1 176.8 87.3 87.8
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 SO4 A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 3000
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CLEAR ELECTRON DENSITY WAS NOT FOUND FOR AMINO
REMARK 999 ACIDS 343-351 AND 388-393. THE REGION 343-351
REMARK 999 IS A LOOP ON THE OUTSIDE OF THE PROTEIN AND
REMARK 999 AMINO ACIDS 388-393 ARE AT THE C-TERMINUS OF
REMARK 999 THE PROTEIN. BOTH OF THESE REGIONS ARE
REMARK 999 APPARENTLY MOBILE.
DBREF 1R6X A 2 393 UNP P08536 MET3_YEAST 2 393
SEQADV 1R6X GLY A 394 UNP P08536 CLONING ARTIFACT
SEQADV 1R6X SER A 395 UNP P08536 CLONING ARTIFACT
SEQADV 1R6X SER A 396 UNP P08536 CLONING ARTIFACT
SEQRES 1 A 395 PRO ALA PRO HIS GLY GLY ILE LEU GLN ASP LEU ILE ALA
SEQRES 2 A 395 ARG ASP ALA LEU LYS LYS ASN GLU LEU LEU SER GLU ALA
SEQRES 3 A 395 GLN SER SER ASP ILE LEU VAL TRP ASN LEU THR PRO ARG
SEQRES 4 A 395 GLN LEU CYS ASP ILE GLU LEU ILE LEU ASN GLY GLY PHE
SEQRES 5 A 395 SER PRO LEU THR GLY PHE LEU ASN GLU ASN ASP TYR SER
SEQRES 6 A 395 SER VAL VAL THR ASP SER ARG LEU ALA ASP GLY THR LEU
SEQRES 7 A 395 TRP THR ILE PRO ILE THR LEU ASP VAL ASP GLU ALA PHE
SEQRES 8 A 395 ALA ASN GLN ILE LYS PRO ASP THR ARG ILE ALA LEU PHE
SEQRES 9 A 395 GLN ASP ASP GLU ILE PRO ILE ALA ILE LEU THR VAL GLN
SEQRES 10 A 395 ASP VAL TYR LYS PRO ASN LYS THR ILE GLU ALA GLU LYS
SEQRES 11 A 395 VAL PHE ARG GLY ASP PRO GLU HIS PRO ALA ILE SER TYR
SEQRES 12 A 395 LEU PHE ASN VAL ALA GLY ASP TYR TYR VAL GLY GLY SER
SEQRES 13 A 395 LEU GLU ALA ILE GLN LEU PRO GLN HIS TYR ASP TYR PRO
SEQRES 14 A 395 GLY LEU ARG LYS THR PRO ALA GLN LEU ARG LEU GLU PHE
SEQRES 15 A 395 GLN SER ARG GLN TRP ASP ARG VAL VAL ALA PHE GLN THR
SEQRES 16 A 395 ARG ASN PRO MET HIS ARG ALA HIS ARG GLU LEU THR VAL
SEQRES 17 A 395 ARG ALA ALA ARG GLU ALA ASN ALA LYS VAL LEU ILE HIS
SEQRES 18 A 395 PRO VAL VAL GLY LEU THR LYS PRO GLY ASP ILE ASP HIS
SEQRES 19 A 395 HIS THR ARG VAL ARG VAL TYR GLN GLU ILE ILE LYS ARG
SEQRES 20 A 395 TYR PRO ASN GLY ILE ALA PHE LEU SER LEU LEU PRO LEU
SEQRES 21 A 395 ALA MET ARG MET SER GLY ASP ARG GLU ALA VAL TRP HIS
SEQRES 22 A 395 ALA ILE ILE ARG LYS ASN TYR GLY ALA SER HIS PHE ILE
SEQRES 23 A 395 VAL GLY ARG ASP HIS ALA GLY PRO GLY LYS ASN SER LYS
SEQRES 24 A 395 GLY VAL ASP PHE TYR GLY PRO TYR ASP ALA GLN GLU LEU
SEQRES 25 A 395 VAL GLU SER TYR LYS HIS GLU LEU ASP ILE GLU VAL VAL
SEQRES 26 A 395 PRO PHE ARG MET VAL THR TYR LEU PRO ASP GLU ASP ARG
SEQRES 27 A 395 TYR ALA PRO ILE ASP GLN ILE ASP THR THR LYS THR ARG
SEQRES 28 A 395 THR LEU ASN ILE SER GLY THR GLU LEU ARG ARG ARG LEU
SEQRES 29 A 395 ARG VAL GLY GLY GLU ILE PRO GLU TRP PHE SER TYR PRO
SEQRES 30 A 395 GLU VAL VAL LYS ILE LEU ARG GLU SER ASN PRO PRO ARG
SEQRES 31 A 395 PRO LYS GLY SER SER
HET SO4 A2002 5
HET SO4 A2004 5
HET SO4 A2005 5
HET CO A3000 1
HETNAM SO4 SULFATE ION
HETNAM CO COBALT (II) ION
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 CO CO 2+
FORMUL 6 HOH *432(H2 O)
HELIX 1 1 ASP A 11 ASP A 16 1 6
HELIX 2 2 LYS A 19 GLN A 28 1 10
HELIX 3 3 THR A 38 ASN A 50 1 13
HELIX 4 4 ASN A 61 SER A 72 1 12
HELIX 5 5 ASP A 89 GLN A 95 1 7
HELIX 6 6 ASN A 124 ARG A 134 1 11
HELIX 7 7 HIS A 139 VAL A 148 1 10
HELIX 8 8 THR A 175 ARG A 186 1 12
HELIX 9 9 HIS A 201 ALA A 215 1 15
HELIX 10 10 ASP A 234 ILE A 246 1 13
HELIX 11 11 LYS A 247 TYR A 249 5 3
HELIX 12 12 SER A 266 TYR A 281 1 16
HELIX 13 13 TYR A 308 ASP A 322 1 15
HELIX 14 14 PRO A 335 ASP A 338 5 4
HELIX 15 15 SER A 357 VAL A 367 1 11
HELIX 16 16 TYR A 377 ARG A 385 1 9
SHEET 1 A 5 LEU A 33 ASN A 36 0
SHEET 2 A 5 ARG A 101 GLN A 106 1 O ALA A 103 N LEU A 33
SHEET 3 A 5 ILE A 110 TYR A 121 -1 O ALA A 113 N LEU A 104
SHEET 4 A 5 TYR A 152 ALA A 160 -1 O TYR A 153 N TYR A 121
SHEET 5 A 5 GLY A 58 PHE A 59 -1 N PHE A 59 O GLY A 156
SHEET 1 B 5 LEU A 33 ASN A 36 0
SHEET 2 B 5 ARG A 101 GLN A 106 1 O ALA A 103 N LEU A 33
SHEET 3 B 5 ILE A 110 TYR A 121 -1 O ALA A 113 N LEU A 104
SHEET 4 B 5 TYR A 152 ALA A 160 -1 O TYR A 153 N TYR A 121
SHEET 5 B 5 LEU A 86 VAL A 88 -1 N VAL A 88 O TYR A 152
SHEET 1 C 5 ALA A 254 LEU A 256 0
SHEET 2 C 5 LYS A 218 ILE A 221 1 N ILE A 221 O PHE A 255
SHEET 3 C 5 VAL A 191 PHE A 194 1 N VAL A 192 O LYS A 218
SHEET 4 C 5 HIS A 285 VAL A 288 1 O HIS A 285 N ALA A 193
SHEET 5 C 5 GLU A 324 PRO A 327 1 O VAL A 326 N PHE A 286
SHEET 1 D 2 VAL A 331 LEU A 334 0
SHEET 2 D 2 ARG A 339 PRO A 342 -1 O ARG A 339 N LEU A 334
LINK OD2 ASP A 168 CO CO A3000 1555 1555 2.74
LINK NE2 HIS A 235 CO CO A3000 1555 1555 2.19
LINK NE2 HIS A 236 CO CO A3000 1555 1555 2.15
LINK CO CO A3000 O HOH A4265 1555 1555 2.18
LINK CO CO A3000 O HOH A4355 1555 1555 2.13
CISPEP 1 SER A 54 PRO A 55 0 0.75
SITE 1 AC1 7 GLN A 195 ARG A 197 ALA A 293 HOH A4071
SITE 2 AC1 7 HOH A4111 HOH A4205 HOH A4393
SITE 1 AC2 7 HIS A 166 TYR A 167 ASP A 168 ARG A 173
SITE 2 AC2 7 HOH A4184 HOH A4265 HOH A4407
SITE 1 AC3 3 ARG A 205 ARG A 213 HOH A4364
SITE 1 AC4 5 ASP A 168 HIS A 235 HIS A 236 HOH A4265
SITE 2 AC4 5 HOH A4355
CRYST1 50.186 59.111 131.165 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 0.019926 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016917 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007624 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
