HEADER CYTOKINE 05-NOV-96 1TVX
TITLE NEUTROPHIL ACTIVATING PEPTIDE-2 VARIANT FORM M6L WITH FIVE ADDITIONAL
TITLE 2 AMINO TERMINAL RESIDUES (DSDLY)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTROPHIL ACTIVATING PEPTIDE 2 VARIANT;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: NAP-2;
COMPND 5 ENGINEERED: YES;
COMPND 6 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CYTOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.MALKOWSKI,B.F.P.EDWARDS
REVDAT 3 09-AUG-23 1TVX 1 REMARK
REVDAT 2 24-FEB-09 1TVX 1 VERSN
REVDAT 1 11-JAN-97 1TVX 0
JRNL AUTH M.G.MALKOWSKI,J.B.LAZAR,P.H.JOHNSON,B.F.EDWARDS
JRNL TITL THE AMINO-TERMINAL RESIDUES IN THE CRYSTAL STRUCTURE OF
JRNL TITL 2 CONNECTIVE TISSUE ACTIVATING PEPTIDE-III (DES10) BLOCK THE
JRNL TITL 3 ELR CHEMOTACTIC SEQUENCE.
JRNL REF J.MOL.BIOL. V. 266 367 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9047370
JRNL DOI 10.1006/JMBI.1996.0796
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.G.MALKOWSKI,J.Y.WU,J.B.LAZAR,P.H.JOHNSON,B.F.EDWARDS
REMARK 1 TITL THE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN
REMARK 1 TITL 2 NEUTROPHIL-ACTIVATING PEPTIDE-2 (M6L) AT 1.9-A RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 270 7077 1995
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.T.BALDWIN,I.T.WEBER,R.ST.CHARLES,J.C.XUAN,E.APPELLA,
REMARK 1 AUTH 2 M.YAMADA,K.MATSUSHIMA,B.F.EDWARDS,G.M.CLORE,A.M.GRONENBORN,
REMARK 1 AUTH 3 ET AL.
REMARK 1 TITL CRYSTAL STRUCTURE OF INTERLEUKIN 8: SYMBIOSIS OF NMR AND
REMARK 1 TITL 2 CRYSTALLOGRAPHY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 88 502 1991
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.ST.CHARLES,D.A.WALZ,B.F.EDWARDS
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF BOVINE PLATELET FACTOR 4
REMARK 1 TITL 2 AT 3.0-A RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 264 2092 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 25118
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) : 0.196
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
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 : 2060
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 147
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 2.060
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.34
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.850
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 1TVX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176873.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 273
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : XENGEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25385
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 9.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03880
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NEUTROPHIL ACTIVATING PEPTIDE-2 (1NAP)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M CITRATE, 0.1M HEPES, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 38.38000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ASP A 16
REMARK 465 SER A 17
REMARK 465 ASP A 18
REMARK 465 LEU A 19
REMARK 465 TYR A 20
REMARK 465 ALA A 21
REMARK 465 GLU A 22
REMARK 465 GLU A 87
REMARK 465 SER A 88
REMARK 465 ALA A 89
REMARK 465 ASP A 90
REMARK 465 GLU B 87
REMARK 465 SER B 88
REMARK 465 ALA B 89
REMARK 465 ASP B 90
REMARK 465 ASP C 16
REMARK 465 SER C 17
REMARK 465 ASP C 18
REMARK 465 LEU C 19
REMARK 465 TYR C 20
REMARK 465 ALA C 21
REMARK 465 GLU C 22
REMARK 465 GLU C 87
REMARK 465 SER C 88
REMARK 465 ALA C 89
REMARK 465 ASP C 90
REMARK 465 GLU D 87
REMARK 465 SER D 88
REMARK 465 ALA D 89
REMARK 465 ASP D 90
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 ARG A 24 -160.72 -51.14
REMARK 500 ASN A 52 30.31 -89.38
REMARK 500 ARG B 24 -128.17 -107.44
REMARK 500 CYS B 51 128.23 -171.16
REMARK 500 ASN B 52 42.42 -94.45
REMARK 500 ARG C 24 -142.25 -151.56
REMARK 500 CYS C 51 99.50 -179.21
REMARK 500 ASN C 52 45.50 -90.65
REMARK 500 SER D 17 80.05 33.74
REMARK 500 ARG D 24 -123.43 -113.07
REMARK 500 CYS D 51 126.88 -175.76
REMARK 500 ASN D 52 47.45 -91.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THERE IS A TETRAMER IN THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 700 WHICH CONSISTS OF FOUR IDENTICAL MONOMERS. TWO MONOMERS
REMARK 700 COMBINE TO FORM AN EXTENDED SIX STRANDED BETA SHEET DIMER.
REMARK 700 TWO DIMERS ARE THEN ARRANGED BACK-TO-BACK TO FORM THE
REMARK 700 TETRAMER.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE NUMBERING SCHEME FOR ASP-CTAP FOLLOWS HOMOLOGY
REMARK 999 ALIGNMENT WITH THE FIRST PAIR OF CYSTEINE RESIDUES IN
REMARK 999 BOVINE PLATELET FACTOR FOUR. THE NUMBERING SCHEME IS
REMARK 999 SEQUENTIAL BEGINNING WITH RESIDUE 16 AND ENDING WITH
REMARK 999 RESIDUE 90. SEE FIGURE 1 IN THE JRNL REFERENCE LISTED
REMARK 999 ABOVE.
DBREF 1TVX A 16 90 UNP P02775 SCYB7_HUMAN 517 591
DBREF 1TVX B 16 90 UNP P02775 SCYB7_HUMAN 517 591
DBREF 1TVX C 16 90 UNP P02775 SCYB7_HUMAN 517 591
DBREF 1TVX D 16 90 UNP P02775 SCYB7_HUMAN 517 591
SEQRES 1 A 75 ASP SER ASP LEU TYR ALA GLU LEU ARG CYS LEU CYS ILE
SEQRES 2 A 75 LYS THR THR SER GLY ILE HIS PRO LYS ASN ILE GLN SER
SEQRES 3 A 75 LEU GLU VAL ILE GLY LYS GLY THR HIS CYS ASN GLN VAL
SEQRES 4 A 75 GLU VAL ILE ALA THR LEU LYS ASP GLY ARG LYS ILE CYS
SEQRES 5 A 75 LEU ASP PRO ASP ALA PRO ARG ILE LYS LYS ILE VAL GLN
SEQRES 6 A 75 LYS LYS LEU ALA GLY ASP GLU SER ALA ASP
SEQRES 1 B 75 ASP SER ASP LEU TYR ALA GLU LEU ARG CYS LEU CYS ILE
SEQRES 2 B 75 LYS THR THR SER GLY ILE HIS PRO LYS ASN ILE GLN SER
SEQRES 3 B 75 LEU GLU VAL ILE GLY LYS GLY THR HIS CYS ASN GLN VAL
SEQRES 4 B 75 GLU VAL ILE ALA THR LEU LYS ASP GLY ARG LYS ILE CYS
SEQRES 5 B 75 LEU ASP PRO ASP ALA PRO ARG ILE LYS LYS ILE VAL GLN
SEQRES 6 B 75 LYS LYS LEU ALA GLY ASP GLU SER ALA ASP
SEQRES 1 C 75 ASP SER ASP LEU TYR ALA GLU LEU ARG CYS LEU CYS ILE
SEQRES 2 C 75 LYS THR THR SER GLY ILE HIS PRO LYS ASN ILE GLN SER
SEQRES 3 C 75 LEU GLU VAL ILE GLY LYS GLY THR HIS CYS ASN GLN VAL
SEQRES 4 C 75 GLU VAL ILE ALA THR LEU LYS ASP GLY ARG LYS ILE CYS
SEQRES 5 C 75 LEU ASP PRO ASP ALA PRO ARG ILE LYS LYS ILE VAL GLN
SEQRES 6 C 75 LYS LYS LEU ALA GLY ASP GLU SER ALA ASP
SEQRES 1 D 75 ASP SER ASP LEU TYR ALA GLU LEU ARG CYS LEU CYS ILE
SEQRES 2 D 75 LYS THR THR SER GLY ILE HIS PRO LYS ASN ILE GLN SER
SEQRES 3 D 75 LEU GLU VAL ILE GLY LYS GLY THR HIS CYS ASN GLN VAL
SEQRES 4 D 75 GLU VAL ILE ALA THR LEU LYS ASP GLY ARG LYS ILE CYS
SEQRES 5 D 75 LEU ASP PRO ASP ALA PRO ARG ILE LYS LYS ILE VAL GLN
SEQRES 6 D 75 LYS LYS LEU ALA GLY ASP GLU SER ALA ASP
FORMUL 5 HOH *147(H2 O)
HELIX 1 1 PRO A 36 ASN A 38 5 3
HELIX 2 2 PRO A 73 LEU A 83 1 11
HELIX 3 3 PRO B 36 ASN B 38 5 3
HELIX 4 4 PRO B 73 LEU B 83 1 11
HELIX 5 5 PRO C 36 ASN C 38 5 3
HELIX 6 6 PRO C 73 LYS C 82 1 10
HELIX 7 7 PRO D 36 ASN D 38 5 3
HELIX 8 8 PRO D 73 ALA D 84 1 12
SHEET 1 A 6 LYS A 65 LEU A 68 0
SHEET 2 A 6 GLU A 55 LEU A 60 -1 N ALA A 58 O ILE A 66
SHEET 3 A 6 ILE A 39 ILE A 45 -1 N ILE A 45 O GLU A 55
SHEET 4 A 6 ILE B 39 ILE B 45 -1 N VAL B 44 O LEU A 42
SHEET 5 A 6 GLU B 55 LEU B 60 -1 N THR B 59 O GLN B 40
SHEET 6 A 6 LYS B 65 LEU B 68 -1 N LEU B 68 O VAL B 56
SHEET 1 B 6 LYS C 65 LEU C 68 0
SHEET 2 B 6 GLU C 55 LEU C 60 -1 N ALA C 58 O ILE C 66
SHEET 3 B 6 ILE C 39 ILE C 45 -1 N ILE C 45 O GLU C 55
SHEET 4 B 6 ILE D 39 ILE D 45 -1 N VAL D 44 O LEU C 42
SHEET 5 B 6 GLU D 55 LEU D 60 -1 N THR D 59 O GLN D 40
SHEET 6 B 6 LYS D 65 LEU D 68 -1 N LEU D 68 O VAL D 56
SSBOND 1 CYS A 25 CYS A 51 1555 1555 2.03
SSBOND 2 CYS A 27 CYS A 67 1555 1555 2.00
SSBOND 3 CYS B 25 CYS B 51 1555 1555 2.00
SSBOND 4 CYS B 27 CYS B 67 1555 1555 2.03
SSBOND 5 CYS C 25 CYS C 51 1555 1555 2.03
SSBOND 6 CYS C 27 CYS C 67 1555 1555 2.02
SSBOND 7 CYS D 25 CYS D 51 1555 1555 2.01
SSBOND 8 CYS D 27 CYS D 67 1555 1555 2.02
CRYST1 43.810 76.760 43.780 90.00 96.95 90.00 P 1 21 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 0.022826 0.000000 0.002782 0.00000
SCALE2 0.000000 0.013028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023011 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
