HEADER HORMONE/GROWTH FACTOR 09-MAR-05 1Z2V
TITLE CRYSTAL STRUCTURE OF GLU60 DELETION MUTANT OF HUMAN ACIDIC FIBROBLAST
TITLE 2 GROWTH FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HBGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, BETA-
COMPND 5 ENDOTHELIAL CELL GROWTH FACTOR, ECGF- BETA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FGF1, FGFA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A(+)
KEYWDS BETA-TREFOIL, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LEE,M.BLABER
REVDAT 4 23-AUG-23 1Z2V 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1Z2V 1 VERSN
REVDAT 2 17-OCT-06 1Z2V 1 JRNL
REVDAT 1 07-FEB-06 1Z2V 0
JRNL AUTH J.LEE,V.K.DUBEY,T.SOMASUNDARAM,M.BLABER
JRNL TITL CONVERSION OF TYPE I 4:6 TO 3:5 BETA-TURN TYPES IN HUMAN
JRNL TITL 2 ACIDIC FIBROBLAST GROWTH FACTOR: EFFECTS UPON STRUCTURE,
JRNL TITL 3 STABILITY, FOLDING, AND MITOGENIC FUNCTION.
JRNL REF PROTEINS V. 62 686 2006
JRNL REFN ISSN 0887-3585
JRNL PMID 16355415
JRNL DOI 10.1002/PROT.20808
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 : CNS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 26149
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R FREE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 783
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.96
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 78
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.40
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : CNS
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC BLUE CONFOCAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26149
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 25.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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 1JQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298.15K
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 54.63450
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 54.63450
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 36.61950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.99200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.61950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.99200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.63450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.61950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.99200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.63450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.61950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.99200
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 HIS A -1
REMARK 465 HIS A 0
REMARK 465 SER A 138
REMARK 465 SER A 139
REMARK 465 ASP A 140
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 SER B 138
REMARK 465 SER B 139
REMARK 465 ASP B 140
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 32 -164.05 -162.86
REMARK 500 GLU A 49 -76.94 -85.79
REMARK 500 ASN A 92 19.82 58.36
REMARK 500 HIS A 93 -49.42 -151.55
REMARK 500 ASP B 32 -159.09 -159.51
REMARK 500 GLU B 49 -103.66 -103.45
REMARK 500 HIS B 93 -51.99 -153.34
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 A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JQZ RELATED DB: PDB
REMARK 900 HUMAN ACIDIC FIBROBLAST GROWTH FACTOR, 140 AMINO ACID FORM WITH
REMARK 900 AMINO TERMINAL HIS TAG
DBREF 1Z2V A 1G 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 1Z2V B 1G 140 UNP P05230 FGF1_HUMAN 16 155
SEQADV 1Z2V HIS A 1C UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS A 1C UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS A 1C UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS A 1D UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS A 1E UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS A 1F UNP P05230 EXPRESSION TAG
SEQADV 1Z2V A UNP P05230 GLU 75 DELETION
SEQADV 1Z2V HIS B 1C UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS B 1C UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS B 1C UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS B 1D UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS B 1E UNP P05230 EXPRESSION TAG
SEQADV 1Z2V HIS B 1F UNP P05230 EXPRESSION TAG
SEQADV 1Z2V B UNP P05230 GLU 75 DELETION
SEQRES 1 A 145 HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN
SEQRES 2 A 145 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 3 A 145 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 4 A 145 THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU
SEQRES 5 A 145 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 6 A 145 THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU
SEQRES 7 A 145 TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU
SEQRES 8 A 145 GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER
SEQRES 9 A 145 LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS
SEQRES 10 A 145 LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR
SEQRES 11 A 145 GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER
SEQRES 12 A 145 SER ASP
SEQRES 1 B 145 HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN
SEQRES 2 B 145 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 3 B 145 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 4 B 145 THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU
SEQRES 5 B 145 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 6 B 145 THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU
SEQRES 7 B 145 TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU
SEQRES 8 B 145 GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER
SEQRES 9 B 145 LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS
SEQRES 10 B 145 LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR
SEQRES 11 B 145 GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER
SEQRES 12 B 145 SER ASP
HET SO4 A 300 5
HET SO4 A 302 5
HET SO4 B 301 5
HET SO4 B 303 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 HOH *230(H2 O)
HELIX 1 1 ASN A 80 CYS A 83 5 4
HELIX 2 2 HIS A 102 ASN A 106 5 5
HELIX 3 3 ARG A 119 THR A 123 5 5
HELIX 4 4 ASN B 80 CYS B 83 5 4
HELIX 5 5 HIS B 102 ASN B 106 5 5
HELIX 6 6 ARG B 119 THR B 123 5 5
HELIX 7 7 GLN B 127 LEU B 131 5 5
SHEET 1 A 4 VAL A 31 THR A 34 0
SHEET 2 A 4 HIS A 21 ILE A 25 -1 N ARG A 24 O ASP A 32
SHEET 3 A 4 LEU A 13 CYS A 16 -1 N CYS A 16 O HIS A 21
SHEET 4 A 4 LEU A 133 LEU A 135 -1 O LEU A 135 N LEU A 13
SHEET 1 B 4 GLN A 45 ALA A 48 0
SHEET 2 B 4 GLU A 53 LYS A 57 -1 O LYS A 57 N GLN A 45
SHEET 3 B 4 PHE A 85 GLU A 90 -1 O PHE A 85 N VAL A 54
SHEET 4 B 4 TYR A 94 SER A 99 -1 O ILE A 98 N LEU A 86
SHEET 1 C 2 TYR A 64 MET A 67 0
SHEET 2 C 2 LEU A 73 SER A 76 -1 O SER A 76 N TYR A 64
SHEET 1 D 4 VAL B 31 THR B 34 0
SHEET 2 D 4 HIS B 21 ILE B 25 -1 N ARG B 24 O ASP B 32
SHEET 3 D 4 LYS B 12 CYS B 16 -1 N CYS B 16 O HIS B 21
SHEET 4 D 4 LEU B 133 PRO B 136 -1 O LEU B 135 N LEU B 13
SHEET 1 E 4 GLN B 45 ALA B 48 0
SHEET 2 E 4 GLU B 53 LYS B 57 -1 O LYS B 57 N GLN B 45
SHEET 3 E 4 PHE B 85 GLU B 90 -1 O PHE B 85 N VAL B 54
SHEET 4 E 4 TYR B 94 SER B 99 -1 O ILE B 98 N LEU B 86
SHEET 1 F 2 TYR B 64 MET B 67 0
SHEET 2 F 2 LEU B 73 SER B 76 -1 O SER B 76 N TYR B 64
SITE 1 AC1 7 ASN A 18 LYS A 112 LYS A 113 LYS A 118
SITE 2 AC1 7 HOH A 341 HOH A 355 ASP B 70
SITE 1 AC2 6 ASN B 18 LYS B 112 LYS B 113 SO4 B 303
SITE 2 AC2 6 HOH B 331 HOH B 388
SITE 1 AC3 4 PRO A 121 ARG A 122 HIS A 124 ARG B 119
SITE 1 AC4 5 LYS B 112 LYS B 118 ARG B 122 SO4 B 301
SITE 2 AC4 5 HOH B 401
CRYST1 73.239 97.984 109.269 90.00 90.00 90.00 C 2 2 21 16
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 0.013654 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010206 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009152 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
