HEADER HYDROLASE 12-DEC-06 2O8T
TITLE CRYSTAL STRUCTURE AND BINDING EPITOPES OF UROKINASE-TYPE
TITLE 2 PLASMINOGEN ACTIVATOR (C122A/N145Q) IN COMPLEX WITH
TITLE 3 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UROKINASE PLASMINOGEN ACTIVATOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 16-250 (159-411);
COMPND 5 SYNONYM: UPA;
COMPND 6 EC: 3.4.21.73;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: X-33;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: SELECTIVE;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA
KEYWDS UROKINASE-TYPE PLASMINOGEN ACTIVATOR, BENZAMIDINE,
KEYWDS 2 PHENYLGUANIDINE, CONTACT AREA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.ZHAO,C.YUAN,L.JIANG,Z.HUANG,M.HUANG
REVDAT 2 24-FEB-09 2O8T 1 VERSN
REVDAT 1 25-DEC-07 2O8T 0
JRNL AUTH G.ZHAO,C.YUAN,L.JIANG,Z.HUANG,M.HUANG
JRNL TITL CRYSTAL STRUCTURE AND BINDING EPITOPES OF
JRNL TITL 2 UROKINASE-TYPE PLASMINOGEN ACTIVATOR
JRNL TITL 3 (C122A/N145Q/S195A) IN COMPLEX WITH INHIBITORS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1510898.160
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 38545
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) : 0.242
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1364
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5800
REMARK 3 BIN R VALUE (WORKING SET) : 0.3280
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 97
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1825
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 227
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.73000
REMARK 3 B22 (A**2) : -1.73000
REMARK 3 B33 (A**2) : 3.46000
REMARK 3 B12 (A**2) : -0.02000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.71
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 59.53
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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 : PEG_PAR.TXT
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : 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 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2O8T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-06.
REMARK 100 THE RCSB ID CODE IS RCSB040831.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.4
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38545
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.06200
REMARK 200 R SYM FOR SHELL (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 18.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M SODIUM CITRATE (PH4.5)
REMARK 280 BUFFER, 1.95M (NH4)2SO4, 0.05% NAN3, 5% PEG400, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.45500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.90371
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.20333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 60.45500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 34.90371
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 14.20333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 60.45500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 34.90371
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 14.20333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.80742
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 28.40667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 69.80742
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 28.40667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 69.80742
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 28.40667
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 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 ARG A 36
REMARK 465 HIS A 37
REMARK 465 ARG A 37A
REMARK 465 GLY A 37B
REMARK 465 GLY A 37C
REMARK 465 SER A 37D
REMARK 465 ASP A 97
REMARK 465 THR A 97A
REMARK 465 LEU A 97B
REMARK 465 SER A 110
REMARK 465 LYS A 110A
REMARK 465 GLU A 110B
REMARK 465 GLY A 110C
REMARK 465 ARG A 110D
REMARK 465 LYS A 243
REMARK 465 GLU A 244
REMARK 465 GLU A 245
REMARK 465 ASN A 246
REMARK 465 GLY A 247
REMARK 465 LEU A 248
REMARK 465 ALA A 249
REMARK 465 LEU A 250
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 GLN A 27 63.55 -162.34
REMARK 500 VAL A 41 -63.31 -108.35
REMARK 500 SER A 54 -153.95 -148.25
REMARK 500 TYR A 127 35.70 39.14
REMARK 500 TYR A 171 -104.16 -93.76
REMARK 500 LEU A 203 36.18 -74.99
REMARK 500 GLN A 204 85.38 61.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A5104 DISTANCE = 5.78 ANGSTROMS
REMARK 525 HOH A5234 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH A5253 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A5274 DISTANCE = 6.63 ANGSTROMS
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 402
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 314
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 315
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 5084
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O8U RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(C122A/N145Q/S195A) IN COMPLEX WITH
REMARK 900 DIFFERENT INHIBITORS
REMARK 900 RELATED ID: 2O8W RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(C122A/N145Q/S195A) IN COMPLEX WITH
REMARK 900 DIFFERENT INHIBITORS
DBREF 2O8T A 16 250 UNP Q5PY49 Q5PY49_HUMAN 159 411
SEQADV 2O8T ALA A 122 UNP Q5PY49 CYS 279 ENGINEERED
SEQADV 2O8T GLN A 145 UNP Q5PY49 ASN 302 ENGINEERED
SEQRES 1 A 253 ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO
SEQRES 2 A 253 TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER
SEQRES 3 A 253 VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS
SEQRES 4 A 253 TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO
SEQRES 5 A 253 LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG
SEQRES 6 A 253 LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL
SEQRES 7 A 253 GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR
SEQRES 8 A 253 LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG
SEQRES 9 A 253 SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE
SEQRES 10 A 253 GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN
SEQRES 11 A 253 PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU
SEQRES 12 A 253 GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET
SEQRES 13 A 253 THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN
SEQRES 14 A 253 PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU
SEQRES 15 A 253 CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN
SEQRES 16 A 253 GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY
SEQRES 17 A 253 ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY
SEQRES 18 A 253 CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL
SEQRES 19 A 253 SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU
SEQRES 20 A 253 GLU ASN GLY LEU ALA LEU
HET SO4 A 402 5
HET SO4 A 403 5
HET 1PE A 314 16
HET 1PE A 315 16
HET PEG A5084 7
HETNAM SO4 SULFATE ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN 1PE PEG400
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 1PE 2(C10 H22 O6)
FORMUL 6 PEG C4 H10 O3
FORMUL 7 HOH *220(H2 O)
HELIX 1 1 THR A 23 GLN A 27 5 5
HELIX 2 2 ALA A 55 PHE A 59 5 5
HELIX 3 3 LYS A 61 ASP A 63 5 4
HELIX 4 4 SER A 164 GLN A 169 1 6
HELIX 5 5 TYR A 172 VAL A 176 5 5
HELIX 6 6 PHE A 234 THR A 242 1 9
SHEET 1 A 8 GLU A 20 PHE A 21 0
SHEET 2 A 8 LYS A 156 ILE A 163 -1 O MET A 157 N GLU A 20
SHEET 3 A 8 MET A 180 ALA A 184 -1 O CYS A 182 N ILE A 163
SHEET 4 A 8 GLY A 226 ARG A 230 -1 O TYR A 228 N LEU A 181
SHEET 5 A 8 MET A 207 TRP A 215 -1 N TRP A 215 O VAL A 227
SHEET 6 A 8 PRO A 198 SER A 202 -1 N CYS A 201 O THR A 208
SHEET 7 A 8 SER A 135 GLY A 140 -1 N GLU A 137 O VAL A 200
SHEET 8 A 8 LYS A 156 ILE A 163 -1 O VAL A 160 N CYS A 136
SHEET 1 B 7 PHE A 30 TYR A 34 0
SHEET 2 B 7 TYR A 40 SER A 48 -1 O VAL A 41 N ILE A 33
SHEET 3 B 7 TRP A 51 SER A 54 -1 O ILE A 53 N SER A 45
SHEET 4 B 7 ALA A 104 ARG A 109 -1 O LEU A 106 N VAL A 52
SHEET 5 B 7 MET A 81 LEU A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 B 7 ILE A 65 LEU A 68 -1 N VAL A 66 O PHE A 83
SHEET 7 B 7 PHE A 30 TYR A 34 -1 N TYR A 34 O ILE A 65
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 50 CYS A 111 1555 1555 2.03
SSBOND 3 CYS A 136 CYS A 201 1555 1555 2.04
SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.05
SITE 1 AC1 3 ILE A 47 LEU A 123 HOH A5100
SITE 1 AC2 9 HIS A 57 GLN A 192 GLY A 193 ASP A 194
SITE 2 AC2 9 SER A 195 HOH A5138 HOH A5182 HOH A5196
SITE 3 AC2 9 HOH A5280
SITE 1 AC3 11 ASN A 74 SER A 135 CYS A 136 GLU A 137
SITE 2 AC3 11 VAL A 159 SER A 202 GLN A 204 MET A 207
SITE 3 AC3 11 1PE A 315 HOH A5203 HOH A5284
SITE 1 AC4 5 VAL A 38 THR A 39 ASN A 74 1PE A 314
SITE 2 AC4 5 HOH A5143
SITE 1 AC5 4 GLY A 133 LEU A 162 ILE A 163 PRO A 185A
CRYST1 120.910 120.910 42.610 90.00 90.00 120.00 H 3 9
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 0.008271 0.004775 0.000000 0.00000
SCALE2 0.000000 0.009550 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023469 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
