HEADER CYTOKINE 31-JUL-95 1INR
TITLE CYTOKINE SYNTHESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-10;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOKINE SYNTHESIS INHIBITORY FACTOR, CSIF;
COMPND 5 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
KEYWDS CYTOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.WALTER
REVDAT 3 13-JUL-11 1INR 1 VERSN
REVDAT 2 24-FEB-09 1INR 1 VERSN
REVDAT 1 14-OCT-96 1INR 0
JRNL AUTH M.R.WALTER,T.L.NAGABHUSHAN
JRNL TITL CRYSTAL STRUCTURE OF INTERLEUKIN 10 REVEALS AN INTERFERON
JRNL TITL 2 GAMMA-LIKE FOLD.
JRNL REF BIOCHEMISTRY V. 34 12118 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7547951
JRNL DOI 10.1021/BI00038A004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.J.COOK,W.T.WINDSOR,N.J.MURGOLA,S.H.TINDALL,
REMARK 1 AUTH 2 T.L.NAGABHUSHAN,M.R.WALTER
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION OF HUMAN
REMARK 1 TITL 2 INTERLEUKIN-10
REMARK 1 REF PROTEINS V. 22 187 1995
REMARK 1 REFN ISSN 0887-3585
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.0
REMARK 3 NUMBER OF REFLECTIONS : 9888
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.337
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1072
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 42
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.70
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) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 3.79
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.84
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.57
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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 1INR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-94
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10087
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 110.48500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 18.18500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 18.18500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 165.72750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 18.18500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 18.18500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 55.24250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 18.18500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 18.18500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 165.72750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 18.18500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 18.18500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.24250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 110.48500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 SER A 1
REMARK 465 PRO A 2
REMARK 465 GLY A 3
REMARK 465 GLN A 4
REMARK 465 GLY A 5
REMARK 465 THR A 6
REMARK 465 GLN A 7
REMARK 465 SER A 8
REMARK 465 GLU A 9
REMARK 465 ASN A 10
REMARK 465 SER A 11
REMARK 465 CYS A 12
REMARK 465 THR A 13
REMARK 465 HIS A 14
REMARK 465 PHE A 15
REMARK 465 PRO A 16
REMARK 465 GLY A 17
REMARK 465 GLN A 38
REMARK 465 MET A 39
REMARK 465 LYS A 40
REMARK 465 ASP A 41
REMARK 465 GLN A 42
REMARK 465 LEU A 43
REMARK 465 ASP A 44
REMARK 465 CYS A 108
REMARK 465 HIS A 109
REMARK 465 ARG A 110
REMARK 465 ASN A 160
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 ASN A 18 CG OD1
REMARK 470 ASN A 21 CG OD1
REMARK 470 TYR A 59 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 107 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 LYS A 34 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 LEU A 46 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 GLU A 54 CA - CB - CG ANGL. DEV. = -17.0 DEGREES
REMARK 500 GLU A 81 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 GLU A 81 CA - CB - CG ANGL. DEV. = 19.9 DEGREES
REMARK 500 VAL A 91 CG1 - CB - CG2 ANGL. DEV. = -14.7 DEGREES
REMARK 500 ARG A 102 CA - CB - CG ANGL. DEV. = -17.0 DEGREES
REMARK 500 ARG A 102 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 102 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TYR A 137 CB - CG - CD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP A 144 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ILE A 145 CG1 - CB - CG2 ANGL. DEV. = -14.7 DEGREES
REMARK 500 MET A 154 CA - CB - CG ANGL. DEV. = 12.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 75 -63.56 -103.45
REMARK 500 GLN A 132 -131.27 56.56
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 A 201 DISTANCE = 8.50 ANGSTROMS
DBREF 1INR A 1 160 UNP P22301 IL10_HUMAN 19 178
SEQRES 1 A 160 SER PRO GLY GLN GLY THR GLN SER GLU ASN SER CYS THR
SEQRES 2 A 160 HIS PHE PRO GLY ASN LEU PRO ASN MET LEU ARG ASP LEU
SEQRES 3 A 160 ARG ASP ALA PHE SER ARG VAL LYS THR PHE PHE GLN MET
SEQRES 4 A 160 LYS ASP GLN LEU ASP ASN LEU LEU LEU LYS GLU SER LEU
SEQRES 5 A 160 LEU GLU ASP PHE LYS GLY TYR LEU GLY CYS GLN ALA LEU
SEQRES 6 A 160 SER GLU MET ILE GLN PHE TYR LEU GLU GLU VAL MET PRO
SEQRES 7 A 160 GLN ALA GLU ASN GLN ASP PRO ASP ILE LYS ALA HIS VAL
SEQRES 8 A 160 ASN SER LEU GLY GLU ASN LEU LYS THR LEU ARG LEU ARG
SEQRES 9 A 160 LEU ARG ARG CYS HIS ARG PHE LEU PRO CYS GLU ASN LYS
SEQRES 10 A 160 SER LYS ALA VAL GLU GLN VAL LYS ASN ALA PHE ASN LYS
SEQRES 11 A 160 LEU GLN GLU LYS GLY ILE TYR LYS ALA MET SER GLU PHE
SEQRES 12 A 160 ASP ILE PHE ILE ASN TYR ILE GLU ALA TYR MET THR MET
SEQRES 13 A 160 LYS ILE ARG ASN
FORMUL 2 HOH *42(H2 O)
HELIX 1 1 ASN A 18 PHE A 37 1 20
HELIX 2 2 GLU A 50 PHE A 56 1 7
HELIX 3 3 GLY A 61 GLU A 74 1 14
HELIX 4 4 VAL A 76 GLN A 83 1 8
HELIX 5 5 LYS A 88 ARG A 106 5 19
HELIX 6 6 PRO A 113 GLU A 115 5 3
HELIX 7 7 LYS A 119 LEU A 131 1 13
HELIX 8 8 LYS A 134 SER A 141 5 8
HELIX 9 9 PHE A 143 MET A 156 1 14
SSBOND 1 CYS A 62 CYS A 114 1555 1555 1.94
CRYST1 36.370 36.370 220.970 90.00 90.00 90.00 P 43 21 2 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 0.027495 0.000000 0.000000 0.00000
SCALE2 0.000000 0.027495 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004526 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
