HEADER TRANSFORMING GROWTH FACTOR 14-DEC-95 1BMP
TITLE BONE MORPHOGENETIC PROTEIN-7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BONE MORPHOGENETIC PROTEIN-7;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OSTEOGENIC PROTEIN-1, HOP-1, BMP-7;
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 ORGAN: OVARY;
SOURCE 6 GENE: HOP-1 CDNA;
SOURCE 7 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 10 EXPRESSION_SYSTEM_GENE: HOP-1 CDNA;
SOURCE 11 OTHER_DETAILS: REFERENCE, T.K. SAMPATH, ET AL. (1992) J. BIOL. CHEM.
SOURCE 12 267, 20452-20362
KEYWDS MORPHOGEN, TRANSFORMING GROWTH FACTOR, CYTOKINE, BONE, CARTILAGE,
KEYWDS 2 GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.L.GRIFFITH,D.L.SCOTT
REVDAT 3 13-JUL-11 1BMP 1 VERSN
REVDAT 2 24-FEB-09 1BMP 1 VERSN
REVDAT 1 23-JUL-97 1BMP 0
JRNL AUTH D.L.GRIFFITH,P.C.KECK,T.K.SAMPATH,D.C.RUEGER,W.D.CARLSON
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT HUMAN OSTEOGENIC
JRNL TITL 2 PROTEIN 1: STRUCTURAL PARADIGM FOR THE TRANSFORMING GROWTH
JRNL TITL 3 FACTOR BETA SUPERFAMILY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 93 878 1996
JRNL REFN ISSN 0027-8424
JRNL PMID 8570652
JRNL DOI 10.1073/PNAS.93.2.878
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.L.GRIFFITH,H.OPPERMANN,D.C.RUEGER,T.K.SAMPATH,R.F.TUCKER,
REMARK 1 AUTH 2 W.D.CARLSON
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC DATA OF
REMARK 1 TITL 2 RECOMBINANT HUMAN OSTEOGENIC PROTEIN-1 (HOP-1)
REMARK 1 REF J.MOL.BIOL. V. 244 657 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT, X-PLOR
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL,BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 5418
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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 828
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.48
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.008 ; 0.030
REMARK 3 ANGLE DISTANCE (A) : 0.025 ; 0.050
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.138 ; 0.100
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.045 ; 0.100
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.211 ; 1.000
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.185 ; 1.000
REMARK 3 MULTIPLE TORSION (A) : 0.250 ; 1.000
REMARK 3 H-BOND (X...Y) (A) : 0.194 ; 1.000
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 23.200; 30.000
REMARK 3 STAGGERED (DEGREES) : 25.900; 50.000
REMARK 3 TRANSVERSE (DEGREES) : 35.100; 50.000
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 OTHER REFINEMENT REMARKS:
REMARK 3 LOOP REGION (RESIDUES 118 - 122) IS DISORDERED AND MODELED
REMARK 3 STEREOCHEMICALLY.
REMARK 3
REMARK 3 NOTE THAT RESIDUE 59 IS DESCRIBED AS TRANS IN THE PAPER
REMARK 3 CITED ON JRNL RECORDS ABOVE BUT THE CURRENT MODEL
REMARK 3 PRESENTED IN THIS ENTRY HAS RESIDUE 59 AS CIS.
REMARK 4
REMARK 4 1BMP 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 : 30-NOV-93
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5502
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.06700
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 28.06000
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 14.03000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 14.03000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.06000
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: 2370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 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 THR A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 SER A 8
REMARK 465 GLN A 9
REMARK 465 ASN A 10
REMARK 465 ARG A 11
REMARK 465 SER A 12
REMARK 465 LYS A 13
REMARK 465 THR A 14
REMARK 465 PRO A 15
REMARK 465 LYS A 16
REMARK 465 ASN A 17
REMARK 465 GLN A 18
REMARK 465 GLU A 19
REMARK 465 ALA A 20
REMARK 465 LEU A 21
REMARK 465 ARG A 22
REMARK 465 MET A 23
REMARK 465 ALA A 24
REMARK 465 ASN A 25
REMARK 465 VAL A 26
REMARK 465 ALA A 27
REMARK 465 GLU A 28
REMARK 465 ASN A 29
REMARK 465 SER A 30
REMARK 465 SER A 31
REMARK 465 SER A 32
REMARK 465 ASP A 33
REMARK 465 GLN A 34
REMARK 465 ARG A 35
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 52 19.70 -64.51
REMARK 500 TYR A 65 173.88 63.72
REMARK 500 TYR A 78 47.59 -81.65
REMARK 500 MET A 79 6.04 -154.22
REMARK 500 ASN A 80 96.27 22.96
REMARK 500 ASN A 95 78.50 -157.97
REMARK 500 ASP A 118 -178.51 -67.98
REMARK 500 ASP A 119 -178.81 -52.29
REMARK 500 SER A 120 -23.63 68.50
REMARK 500 ASN A 130 43.08 72.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 129 0.10 SIDE CHAIN
REMARK 500 ARG A 134 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU A 42 12.67
REMARK 500 TYR A 44 11.12
REMARK 500 VAL A 45 12.60
REMARK 500 ASP A 49 17.81
REMARK 500 TRP A 55 14.50
REMARK 500 ILE A 56 -13.16
REMARK 500 ILE A 57 11.66
REMARK 500 ALA A 58 -11.58
REMARK 500 PHE A 73 15.50
REMARK 500 ALA A 85 11.05
REMARK 500 VAL A 91 12.43
REMARK 500 PRO A 102 -10.21
REMARK 500 LEU A 109 -14.68
REMARK 500 VAL A 123 -10.37
REMARK 500 CYS A 136 -10.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 CYS A 103 23.5 L L OUTSIDE RANGE
REMARK 500 ILE A 124 22.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BMP A 1 139 UNP P18075 BMP7_HUMAN 293 431
SEQRES 1 A 139 SER THR GLY SER LYS GLN ARG SER GLN ASN ARG SER LYS
SEQRES 2 A 139 THR PRO LYS ASN GLN GLU ALA LEU ARG MET ALA ASN VAL
SEQRES 3 A 139 ALA GLU ASN SER SER SER ASP GLN ARG GLN ALA CYS LYS
SEQRES 4 A 139 LYS HIS GLU LEU TYR VAL SER PHE ARG ASP LEU GLY TRP
SEQRES 5 A 139 GLN ASP TRP ILE ILE ALA PRO GLU GLY TYR ALA ALA TYR
SEQRES 6 A 139 TYR CYS GLU GLY GLU CYS ALA PHE PRO LEU ASN SER TYR
SEQRES 7 A 139 MET ASN ALA THR ASN HIS ALA ILE VAL GLN THR LEU VAL
SEQRES 8 A 139 HIS PHE ILE ASN PRO GLU THR VAL PRO LYS PRO CYS CYS
SEQRES 9 A 139 ALA PRO THR GLN LEU ASN ALA ILE SER VAL LEU TYR PHE
SEQRES 10 A 139 ASP ASP SER SER ASN VAL ILE LEU LYS LYS TYR ARG ASN
SEQRES 11 A 139 MET VAL VAL ARG ALA CYS GLY CYS HIS
HELIX 1 1 HIS A 84 PHE A 93 1 10
SHEET 1 A 2 LYS A 39 HIS A 41 0
SHEET 2 A 2 TYR A 66 GLU A 68 -1 N GLU A 68 O LYS A 39
SHEET 1 B 2 TYR A 44 SER A 46 0
SHEET 2 B 2 GLY A 61 ALA A 63 -1 N TYR A 62 O VAL A 45
SHEET 1 C 2 ILE A 112 PHE A 117 0
SHEET 2 C 2 VAL A 123 TYR A 128 -1 N TYR A 128 O ILE A 112
SHEET 1 D 2 CYS A 103 GLN A 108 0
SHEET 2 D 2 ALA A 135 HIS A 139 -1 N HIS A 139 O CYS A 103
SSBOND 1 CYS A 38 CYS A 104 1555 1555 2.02
SSBOND 2 CYS A 67 CYS A 136 1555 1555 2.05
SSBOND 3 CYS A 71 CYS A 138 1555 1555 2.01
SSBOND 4 CYS A 103 CYS A 103 1555 4555 1.95
CISPEP 1 ALA A 58 PRO A 59 0 -27.14
CISPEP 2 PHE A 73 PRO A 74 0 20.83
CRYST1 99.460 99.460 42.090 90.00 90.00 120.00 P 32 2 1 6
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 0.010054 0.005805 0.000000 0.00000
SCALE2 0.000000 0.011610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023759 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
