HEADER DISULFIDE OXIDOREDUCTASE 28-AUG-96 1FVJ
TITLE THE 2.06 ANGSTROM STRUCTURE OF THE H32Y MUTANT OF THE DISULFIDE BOND
TITLE 2 FORMATION PROTEIN (DSBA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISULFIDE BOND FORMATION PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DSBA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN DISULFIDE ISOMERASE, PROTEIN FOLDING, REDOX PROTEIN DISULFIDE
KEYWDS 2 OXIDOREDUCTASE, DISULFIDE OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.MARTIN,L.W.GUDDAT
REVDAT 5 09-AUG-23 1FVJ 1 REMARK
REVDAT 4 03-NOV-21 1FVJ 1 SEQADV
REVDAT 3 24-FEB-09 1FVJ 1 VERSN
REVDAT 2 01-APR-03 1FVJ 1 JRNL
REVDAT 1 15-MAY-97 1FVJ 0
JRNL AUTH L.W.GUDDAT,J.C.BARDWELL,R.GLOCKSHUBER,M.HUBER-WUNDERLICH,
JRNL AUTH 2 T.ZANDER,J.L.MARTIN
JRNL TITL STRUCTURAL ANALYSIS OF THREE HIS32 MUTANTS OF DSBA: SUPPORT
JRNL TITL 2 FOR AN ELECTROSTATIC ROLE OF HIS32 IN DSBA STABILITY.
JRNL REF PROTEIN SCI. V. 6 1893 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9300489
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.L.MARTIN,J.C.BARDWELL,J.KURIYAN
REMARK 1 TITL CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR
REMARK 1 TITL 2 DISULPHIDE BOND FORMATION IN VIVO
REMARK 1 REF NATURE V. 365 464 1993
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.L.MARTIN,G.WAKSMAN,J.C.BARDWELL,J.BECKWITH,J.KURIYAN
REMARK 1 TITL CRYSTALLIZATION OF DSBA, AN ESCHERICHIA COLI PROTEIN
REMARK 1 TITL 2 REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO
REMARK 1 REF J.MOL.BIOL. V. 230 1097 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.06 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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 26334
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) : 0.180
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2607
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) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2644
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.05
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 291
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 : 2904
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.90
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 50.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.380
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.98
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.030
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 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.500
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 1FVJ 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_1000173436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-93
REMARK 200 TEMPERATURE (KELVIN) : 289
REMARK 200 PH : 6.5
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS SOFTWARE
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26334
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
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 (%) : 91.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.05580
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.98
REMARK 200 R MERGE FOR SHELL (I) : 0.21900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1DSB
REMARK 200
REMARK 200 REMARK: DATA WERE REJECTED AS FOLLOWS: FOR PAIRS WITH DIFFERENCE >
REMARK 200 0.3*FHMEAN + 0.1FHSQ, THE PAIR WAS REJECTED IF DIFFERENCE > 3.0
REMARK 200 TIMES ABOVE CRITERION.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5
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 58.85000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.85000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.55000
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
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 300 REMARK: THERE ARE TWO MOLECULES IN THE ASYMMETRIC UNIT. EACH
REMARK 300 CONTAINS 189 RESIDUES, BUT THE LAST RESIDUE (189) IS NOT
REMARK 300 OBSERVED.
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 LYS A 189
REMARK 465 LYS B 189
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 GLU A 13 CG CD OE1 OE2
REMARK 470 LYS A 14 CG CD CE NZ
REMARK 470 GLU A 52 CG CD OE1 OE2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 ARG A 148 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 164 CG CD OE1 NE2
REMARK 470 LYS B 7 CG CD CE NZ
REMARK 470 GLU B 13 CG CD OE1 OE2
REMARK 470 LYS B 14 CG CD CE NZ
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 GLU B 52 CG CD OE1 OE2
REMARK 470 LYS B 132 CG CD CE NZ
REMARK 470 ARG B 148 CG CD 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 LYS A 7 -88.65 -102.58
REMARK 500 PHE A 63 11.06 -67.41
REMARK 500 ASN A 156 19.26 54.33
REMARK 500 LYS B 7 -84.57 -104.06
REMARK 500 PHE B 63 5.06 -63.19
REMARK 500 LYS B 98 -72.82 -83.70
REMARK 500 ASN B 156 17.55 54.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE ACTIVE SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE ACTIVE SITE.
DBREF 1FVJ A 1 189 UNP P24991 DSBA_ECOLI 20 208
DBREF 1FVJ B 1 189 UNP P24991 DSBA_ECOLI 20 208
SEQADV 1FVJ TYR A 32 UNP P24991 HIS 51 ENGINEERED MUTATION
SEQADV 1FVJ TYR B 32 UNP P24991 HIS 51 ENGINEERED MUTATION
SEQRES 1 A 189 ALA GLN TYR GLU ASP GLY LYS GLN TYR THR THR LEU GLU
SEQRES 2 A 189 LYS PRO VAL ALA GLY ALA PRO GLN VAL LEU GLU PHE PHE
SEQRES 3 A 189 SER PHE PHE CYS PRO TYR CYS TYR GLN PHE GLU GLU VAL
SEQRES 4 A 189 LEU HIS ILE SER ASP ASN VAL LYS LYS LYS LEU PRO GLU
SEQRES 5 A 189 GLY VAL LYS MET THR LYS TYR HIS VAL ASN PHE MET GLY
SEQRES 6 A 189 GLY ASP LEU GLY LYS ASP LEU THR GLN ALA TRP ALA VAL
SEQRES 7 A 189 ALA MET ALA LEU GLY VAL GLU ASP LYS VAL THR VAL PRO
SEQRES 8 A 189 LEU PHE GLU GLY VAL GLN LYS THR GLN THR ILE ARG SER
SEQRES 9 A 189 ALA SER ASP ILE ARG ASP VAL PHE ILE ASN ALA GLY ILE
SEQRES 10 A 189 LYS GLY GLU GLU TYR ASP ALA ALA TRP ASN SER PHE VAL
SEQRES 11 A 189 VAL LYS SER LEU VAL ALA GLN GLN GLU LYS ALA ALA ALA
SEQRES 12 A 189 ASP VAL GLN LEU ARG GLY VAL PRO ALA MET PHE VAL ASN
SEQRES 13 A 189 GLY LYS TYR GLN LEU ASN PRO GLN GLY MET ASP THR SER
SEQRES 14 A 189 ASN MET ASP VAL PHE VAL GLN GLN TYR ALA ASP THR VAL
SEQRES 15 A 189 LYS TYR LEU SER GLU LYS LYS
SEQRES 1 B 189 ALA GLN TYR GLU ASP GLY LYS GLN TYR THR THR LEU GLU
SEQRES 2 B 189 LYS PRO VAL ALA GLY ALA PRO GLN VAL LEU GLU PHE PHE
SEQRES 3 B 189 SER PHE PHE CYS PRO TYR CYS TYR GLN PHE GLU GLU VAL
SEQRES 4 B 189 LEU HIS ILE SER ASP ASN VAL LYS LYS LYS LEU PRO GLU
SEQRES 5 B 189 GLY VAL LYS MET THR LYS TYR HIS VAL ASN PHE MET GLY
SEQRES 6 B 189 GLY ASP LEU GLY LYS ASP LEU THR GLN ALA TRP ALA VAL
SEQRES 7 B 189 ALA MET ALA LEU GLY VAL GLU ASP LYS VAL THR VAL PRO
SEQRES 8 B 189 LEU PHE GLU GLY VAL GLN LYS THR GLN THR ILE ARG SER
SEQRES 9 B 189 ALA SER ASP ILE ARG ASP VAL PHE ILE ASN ALA GLY ILE
SEQRES 10 B 189 LYS GLY GLU GLU TYR ASP ALA ALA TRP ASN SER PHE VAL
SEQRES 11 B 189 VAL LYS SER LEU VAL ALA GLN GLN GLU LYS ALA ALA ALA
SEQRES 12 B 189 ASP VAL GLN LEU ARG GLY VAL PRO ALA MET PHE VAL ASN
SEQRES 13 B 189 GLY LYS TYR GLN LEU ASN PRO GLN GLY MET ASP THR SER
SEQRES 14 B 189 ASN MET ASP VAL PHE VAL GLN GLN TYR ALA ASP THR VAL
SEQRES 15 B 189 LYS TYR LEU SER GLU LYS LYS
FORMUL 3 HOH *160(H2 O)
HELIX 1 A1 CYS A 30 GLU A 37 1 8
HELIX 2 A1P HIS A 41 LEU A 50 1SEE REMARK 650 10
HELIX 3 A2 GLY A 66 LEU A 82 1 17
HELIX 4 A3 VAL A 84 GLN A 100 1 17
HELIX 5 A4 SER A 104 ALA A 115 1 12
HELIX 6 A5 LYS A 118 SER A 128 1 11
HELIX 7 A6 PHE A 129 GLN A 146 1 18
HELIX 8 A7 ASN A 170 LYS A 188 1 19
HELIX 9 B1 CYS B 30 GLU B 37 1 8
HELIX 10 B1P HIS B 41 LEU B 50 1SEE REMARK 650 10
HELIX 11 B2 GLY B 66 LEU B 82 1 17
HELIX 12 B3 VAL B 84 GLN B 100 1 17
HELIX 13 B4 SER B 104 ALA B 115 1 12
HELIX 14 B5 LYS B 118 SER B 128 1 11
HELIX 15 B6 PHE B 129 GLN B 146 1 18
HELIX 16 B7 ASN B 170 LYS B 188 1 19
SHEET 1 S1A 5 GLN A 8 LEU A 12 0
SHEET 2 S1A 5 LYS A 158 ASN A 162 -1
SHEET 3 S1A 5 ALA A 152 ASN A 156 -1
SHEET 4 S1A 5 GLN A 21 PHE A 28 -1
SHEET 5 S1A 5 LYS A 55 VAL A 61 1
SHEET 1 S1B 5 GLN B 8 LEU B 12 0
SHEET 2 S1B 5 LYS B 158 ASN B 162 -1
SHEET 3 S1B 5 ALA B 152 ASN B 156 -1
SHEET 4 S1B 5 GLN B 21 PHE B 28 -1
SHEET 5 S1B 5 LYS B 55 VAL B 61 1
SSBOND 1 CYS A 30 CYS A 33 1555 1555 2.02
SSBOND 2 CYS B 30 CYS B 33 1555 1555 2.03
CISPEP 1 VAL A 150 PRO A 151 0 -1.63
CISPEP 2 VAL B 150 PRO B 151 0 -0.11
SITE 1 CAA 5 CYS A 30 PRO A 31 TYR A 32 CYS A 33
SITE 2 CAA 5 PRO A 151
SITE 1 CAB 5 CYS B 30 PRO B 31 TYR B 32 CYS B 33
SITE 2 CAB 5 PRO B 151
CRYST1 117.700 65.100 76.400 90.00 126.30 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 0.008496 0.000000 0.006241 0.00000
SCALE2 0.000000 0.015361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016241 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
