HEADER HORMONE/GROWTH FACTOR 23-AUG-05 2ASK
TITLE STRUCTURE OF HUMAN ARTEMIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARTEMIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS
KEYWDS GLIAL CELL DERIVED FAMILY LIGAND, NEUROTRPHOIC GROWTH
KEYWDS 2 FACTOR, SULFATES, HORMONE/GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SILVIAN,P.JIN,P.CARMILLO,P.A.BORIACK-SJODIN,C.PELLETIER,
AUTHOR 2 M.RUSHE,B.J.GONG,D.SAH,B.PEPINSKY,A.ROSSOMANDO
REVDAT 2 24-FEB-09 2ASK 1 VERSN
REVDAT 1 13-JUN-06 2ASK 0
JRNL AUTH L.SILVIAN,P.JIN,P.CARMILLO,P.A.BORIACK-SJODIN,
JRNL AUTH 2 C.PELLETIER,M.RUSHE,B.J.GONG,D.SAH,B.PEPINSKY,
JRNL AUTH 3 A.ROSSOMANDO
JRNL TITL ARTEMIN CRYSTAL STRUCTURE REVEALS INSIGHTS INTO
JRNL TITL 2 HEPARAN SULFATE BINDING.
JRNL REF BIOCHEMISTRY V. 45 6801 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16734417
JRNL DOI 10.1021/BI060035X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 483024.530
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 28955
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 + TEST SET) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1426
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 29322
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.65
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4236
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 225
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1528
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 212
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.50000
REMARK 3 B22 (A**2) : 9.05000
REMARK 3 B33 (A**2) : -3.55000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.62000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.04
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) : 1.050 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.640 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.700 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.350 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.43
REMARK 3 BSOL : 60.83
REMARK 3
REMARK 3 NCS MODEL : 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 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2ASK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-05.
REMARK 100 THE RCSB ID CODE IS RCSB034263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-01; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 7
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; NULL
REMARK 200 RADIATION SOURCE : NSLS; NULL
REMARK 200 BEAMLINE : X4A; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; NULL
REMARK 200 MONOCHROMATOR : SI(111); CONFOCAL BLUE MIRRORS
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29225
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.31000
REMARK 200 R SYM FOR SHELL (I) : 0.31000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM SULFATE, MES, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 57.31550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.83700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.31550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.83700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 4740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -222.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 229.26200
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -220.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 237.90872
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -54.90328
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 ALA A 1
REMARK 465 GLY A 2
REMARK 465 GLY A 3
REMARK 465 PRO A 4
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 ARG A 7
REMARK 465 ALA A 8
REMARK 465 ARG A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 GLY A 12
REMARK 465 ALA B 1
REMARK 465 GLY B 2
REMARK 465 GLY B 3
REMARK 465 PRO B 4
REMARK 465 GLY B 5
REMARK 465 SER B 6
REMARK 465 ARG B 7
REMARK 465 ALA B 8
REMARK 465 ARG B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 GLY B 12
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 17 NE CZ NH1 NH2
REMARK 480 ARG A 33 CG CD NE CZ NH1 NH2
REMARK 480 ARG A 103 C NE CZ NH1 NH2
REMARK 480 ARG B 17 NE CZ NH1 NH2
REMARK 480 ARG B 48 NE CZ NH1 NH2
REMARK 480 ARG B 74 NE CZ NH1 NH2
REMARK 480 ARG B 85 CG CD NE CZ NH1 NH2
REMARK 480 ASP B 102 CG OD1 OD2
REMARK 480 ARG B 103 NE CZ NH1 NH2
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 PRO A 69 109.04 -58.22
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 SO4 B 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 506
DBREF 2ASK A 1 113 GB 55959167 CAI16797 108 220
DBREF 2ASK B 1 113 GB 55959167 CAI16797 108 220
SEQRES 1 A 113 ALA GLY GLY PRO GLY SER ARG ALA ARG ALA ALA GLY ALA
SEQRES 2 A 113 ARG GLY CYS ARG LEU ARG SER GLN LEU VAL PRO VAL ARG
SEQRES 3 A 113 ALA LEU GLY LEU GLY HIS ARG SER ASP GLU LEU VAL ARG
SEQRES 4 A 113 PHE ARG PHE CYS SER GLY SER CYS ARG ARG ALA ARG SER
SEQRES 5 A 113 PRO HIS ASP LEU SER LEU ALA SER LEU LEU GLY ALA GLY
SEQRES 6 A 113 ALA LEU ARG PRO PRO PRO GLY SER ARG PRO VAL SER GLN
SEQRES 7 A 113 PRO CYS CYS ARG PRO THR ARG TYR GLU ALA VAL SER PHE
SEQRES 8 A 113 MET ASP VAL ASN SER THR TRP ARG THR VAL ASP ARG LEU
SEQRES 9 A 113 SER ALA THR ALA CYS GLY CYS LEU GLY
SEQRES 1 B 113 ALA GLY GLY PRO GLY SER ARG ALA ARG ALA ALA GLY ALA
SEQRES 2 B 113 ARG GLY CYS ARG LEU ARG SER GLN LEU VAL PRO VAL ARG
SEQRES 3 B 113 ALA LEU GLY LEU GLY HIS ARG SER ASP GLU LEU VAL ARG
SEQRES 4 B 113 PHE ARG PHE CYS SER GLY SER CYS ARG ARG ALA ARG SER
SEQRES 5 B 113 PRO HIS ASP LEU SER LEU ALA SER LEU LEU GLY ALA GLY
SEQRES 6 B 113 ALA LEU ARG PRO PRO PRO GLY SER ARG PRO VAL SER GLN
SEQRES 7 B 113 PRO CYS CYS ARG PRO THR ARG TYR GLU ALA VAL SER PHE
SEQRES 8 B 113 MET ASP VAL ASN SER THR TRP ARG THR VAL ASP ARG LEU
SEQRES 9 B 113 SER ALA THR ALA CYS GLY CYS LEU GLY
HET SO4 B 501 5
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 9 HOH *212(H2 O)
HELIX 1 1 ARG A 26 GLY A 29 5 4
HELIX 2 2 CYS A 47 ARG A 51 5 5
HELIX 3 3 SER A 52 ALA A 64 1 13
HELIX 4 4 ARG B 26 GLY B 29 5 4
HELIX 5 5 CYS B 47 ARG B 51 5 5
HELIX 6 6 SER B 52 ALA B 64 1 13
SHEET 1 A 2 ARG A 17 PRO A 24 0
SHEET 2 A 2 LEU A 37 SER A 44 -1 O PHE A 42 N ARG A 19
SHEET 1 B 2 CYS A 80 MET A 92 0
SHEET 2 B 2 TRP A 98 LEU A 112 -1 O ARG A 99 N PHE A 91
SHEET 1 C 2 ARG B 17 PRO B 24 0
SHEET 2 C 2 LEU B 37 SER B 44 -1 O PHE B 42 N ARG B 19
SHEET 1 D 2 CYS B 80 MET B 92 0
SHEET 2 D 2 TRP B 98 LEU B 112 -1 O ARG B 99 N PHE B 91
SSBOND 1 CYS A 16 CYS A 81 1555 1555 2.28
SSBOND 2 CYS A 43 CYS A 109 1555 1555 2.29
SSBOND 3 CYS A 47 CYS A 111 1555 1555 2.37
SSBOND 4 CYS A 80 CYS B 80 1555 1555 2.13
SSBOND 5 CYS B 16 CYS B 81 1555 1555 2.25
SSBOND 6 CYS B 43 CYS B 109 1555 1555 2.28
SSBOND 7 CYS B 47 CYS B 111 1555 1555 2.76
SITE 1 AC1 5 ARG A 99 SER B 46 CYS B 47 ARG B 48
SITE 2 AC1 5 ARG B 49
SITE 1 AC2 4 SER A 46 ARG A 48 ARG A 49 HOH A 613
SITE 1 AC3 9 ARG A 14 SER A 46 ARG A 48 HOH A 514
SITE 2 AC3 9 HOH A 537 HOH A 588 GLY B 72 SER B 73
SITE 3 AC3 9 ARG B 99
SITE 1 AC4 9 HIS A 32 ARG A 33 SER A 34 ASP A 93
SITE 2 AC4 9 VAL A 94 HOH A 541 HOH A 572 HOH A 623
SITE 3 AC4 9 HOH B 516
SITE 1 AC5 10 ARG A 14 SER A 20 GLN A 21 LEU A 22
SITE 2 AC5 10 ARG A 39 HOH A 512 HOH A 534 HOH A 546
SITE 3 AC5 10 HOH A 560 ARG B 68
SITE 1 AC6 3 ARG A 48 ARG A 51 ALA A 59
CRYST1 114.631 33.674 55.580 90.00 98.95 90.00 C 1 2 1 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 0.008724 0.000000 0.001374 0.00000
SCALE2 0.000000 0.029697 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018214 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
