HEADER ISOMERASE 26-APR-04 1T3B
TITLE X-RAY STRUCTURE OF DSBC FROM HAEMOPHILUS INFLUENZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.3.4.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 GENE: DSBC, XPRA, HI1213;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS OXIDOREDUCTASE, PROTEIN DISULFIDE ISOMERASE, PROTEIN FOLDING, REDOX
KEYWDS 2 PROTEIN, REDOX-ACTIVE CENTER, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZHANG,A.F.MONZINGO,L.SEGATORI,G.GEORGIOU,J.D.ROBERTUS
REVDAT 3 23-AUG-23 1T3B 1 REMARK
REVDAT 2 24-FEB-09 1T3B 1 VERSN
REVDAT 1 07-SEP-04 1T3B 0
JRNL AUTH M.ZHANG,A.F.MONZINGO,L.SEGATORI,G.GEORGIOU,J.D.ROBERTUS
JRNL TITL STRUCTURE OF DSBC FROM HAEMOPHILUS INFLUENZAE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 1512 2004
JRNL REFN ISSN 0907-4449
JRNL PMID 15333920
JRNL DOI 10.1107/S0907444904014593
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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 : 6999
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 374
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 : 1564
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 10
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.407
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 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: DUE TO THE EXTREME ANISOTROPY OF THE
REMARK 3 DATA, A THREE DIMENSIONAL ELLIPSOID WITH RESOLUTION LIMITS
REMARK 3 CORRESPONDING TO THE MAXIMUM DIFFRACTION IN EACH DIRECTION WAS
REMARK 3 DEFINED TO SELECT REFLECTIONS USED IN REFINEMENT. THESE
REMARK 3 DIFFRACTION LIMITS WERE 2.5, 3.3, 3.3. ANGSTROMS. THE 2.5 A
REMARK 3 DIRECTION CORRESPONDS TO THE C* AXIS, THE 3.3 A DIRECTIONS
REMARK 3 CORRESPONDS TO THE A* AND B* AXES.
REMARK 4
REMARK 4 1T3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022258.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7826
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 71.3
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 35.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.28400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 1EEJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM PHOSPHATE, GLYCEROL,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 51.69000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.46000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.46000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 77.53500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.46000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.46000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.84500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.46000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.46000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 77.53500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.46000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.46000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 25.84500
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 51.69000
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL DIMER IS GENERATED BY THE
REMARK 300 TWO-FOLD AXIS: -Y, -X, 3/2-Z
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 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 155.07000
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 1
REMARK 465 GLN A 211
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 LYS A 6 CG CD CE NZ
REMARK 470 ARG A 7 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 8 CG CD CE NZ
REMARK 470 GLN A 10 CG CD OE1 NE2
REMARK 470 SER A 11 OG
REMARK 470 PHE A 12 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 13 CG OD1 ND2
REMARK 470 ASN A 16 CG OD1 ND2
REMARK 470 ILE A 17 CD1
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 SER A 21 OG
REMARK 470 ILE A 24 CD1
REMARK 470 ASP A 33 CG OD1 OD2
REMARK 470 SER A 40 OG
REMARK 470 ASP A 42 CG OD1 OD2
REMARK 470 LYS A 44 CG CD CE NZ
REMARK 470 THR A 55 OG1 CG2
REMARK 470 ASN A 57 CG OD1 ND2
REMARK 470 LYS A 65 CG CD CE NZ
REMARK 470 ILE A 66 CD1
REMARK 470 LYS A 84 CG CD CE NZ
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 LYS A 134 CE NZ
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O LYS A 44 OE1 GLU A 53 8556 2.14
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 ALA A 3 -70.73 -60.83
REMARK 500 ALA A 4 76.65 -67.35
REMARK 500 ILE A 5 -78.65 -156.34
REMARK 500 LYS A 6 1.05 -43.80
REMARK 500 PHE A 12 27.87 -175.98
REMARK 500 ASN A 13 64.40 39.39
REMARK 500 SER A 15 -163.33 -75.55
REMARK 500 ASN A 16 63.09 -4.23
REMARK 500 LYS A 20 -179.75 -178.16
REMARK 500 PRO A 23 8.06 -63.57
REMARK 500 THR A 29 91.43 -59.34
REMARK 500 GLU A 48 36.37 -99.89
REMARK 500 TYR A 52 -158.36 -115.12
REMARK 500 GLU A 53 109.99 176.56
REMARK 500 THR A 55 -97.74 38.72
REMARK 500 ASN A 56 -38.55 -144.87
REMARK 500 PRO A 59 68.99 -61.57
REMARK 500 SER A 73 -1.49 -57.19
REMARK 500 LYS A 75 -49.90 -25.96
REMARK 500 LYS A 84 -71.38 -18.34
REMARK 500 ALA A 126 46.41 -72.00
REMARK 500 ASN A 129 61.28 -118.14
REMARK 500 ALA A 142 -177.90 -55.55
REMARK 500 ASP A 144 83.33 -151.51
REMARK 500 GLU A 160 -166.12 -69.20
REMARK 500 VAL A 161 149.80 -178.32
REMARK 500 ASN A 165 -65.50 -159.06
REMARK 500 GLU A 191 -152.75 -58.53
REMARK 500 LEU A 192 94.92 -177.99
REMARK 500 ILE A 193 31.40 -96.57
REMARK 500 PRO A 199 -75.16 -40.22
REMARK 500 ALA A 205 -36.21 -37.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR
DBREF 1T3B A 1 211 UNP P45111 DSBC_HAEIN 19 229
SEQRES 1 A 211 ASP ASP ALA ALA ILE LYS ARG LYS LEU GLN SER PHE ASN
SEQRES 2 A 211 ILE SER ASN ILE VAL ILE LYS SER SER PRO ILE SER GLY
SEQRES 3 A 211 ILE LYS THR ALA VAL THR ASP GLN GLY ILE LEU TYR VAL
SEQRES 4 A 211 SER GLU ASP GLY LYS TYR LEU PHE GLU GLY LYS LEU TYR
SEQRES 5 A 211 GLU LEU THR ASN ASN GLY PRO VAL ASP VAL ALA GLY LYS
SEQRES 6 A 211 ILE LEU VAL ASP LYS LEU ASN SER TYR LYS ASP GLU MET
SEQRES 7 A 211 ILE VAL TYR PRO ALA LYS ASN GLU LYS HIS VAL VAL THR
SEQRES 8 A 211 VAL PHE MET ASP ILE THR CYS HIS TYR CYS HIS LEU LEU
SEQRES 9 A 211 HIS GLN GLN LEU LYS GLU TYR ASN ASP LEU GLY ILE THR
SEQRES 10 A 211 VAL ARG TYR LEU ALA PHE PRO ARG ALA GLY MET ASN ASN
SEQRES 11 A 211 GLN THR ALA LYS GLN MET GLU ALA ILE TRP THR ALA LYS
SEQRES 12 A 211 ASP PRO VAL PHE ALA LEU ASN GLU ALA GLU LYS GLY ASN
SEQRES 13 A 211 LEU PRO LYS GLU VAL LYS THR PRO ASN ILE VAL LYS LYS
SEQRES 14 A 211 HIS TYR GLU LEU GLY ILE GLN PHE GLY VAL ARG GLY THR
SEQRES 15 A 211 PRO SER ILE VAL THR SER THR GLY GLU LEU ILE GLY GLY
SEQRES 16 A 211 TYR LEU LYS PRO ALA ASP LEU LEU ARG ALA LEU GLU GLU
SEQRES 17 A 211 THR ALA GLN
FORMUL 2 HOH *10(H2 O)
HELIX 1 1 ILE A 5 SER A 11 1 7
HELIX 2 2 VAL A 62 SER A 73 1 12
HELIX 3 3 TYR A 74 MET A 78 5 5
HELIX 4 4 CYS A 98 GLN A 106 1 9
HELIX 5 5 GLN A 107 LEU A 114 1 8
HELIX 6 6 ASN A 130 ALA A 142 1 13
HELIX 7 7 ASP A 144 LYS A 154 1 11
HELIX 8 8 ASN A 165 GLY A 178 1 14
HELIX 9 9 LYS A 198 THR A 209 1 12
SHEET 1 A 4 VAL A 18 LYS A 20 0
SHEET 2 A 4 ILE A 27 THR A 32 -1 N THR A 29 O LYS A 20
SHEET 3 A 4 GLY A 35 SER A 40 -1 O VAL A 39 N LYS A 28
SHEET 4 A 4 TYR A 45 PHE A 47 -1 O PHE A 47 N TYR A 38
SHEET 1 B 2 VAL A 60 VAL A 62 0
SHEET 2 B 2 LEU A 51 GLU A 53 -1 N GLU A 53 O VAL A 60
SHEET 1 C 5 ILE A 79 TYR A 81 0
SHEET 2 C 5 ILE A 116 ALA A 122 -1 O VAL A 118 N TYR A 81
SHEET 3 C 5 HIS A 88 MET A 94 1 O HIS A 88 N THR A 117
SHEET 4 C 5 PRO A 183 VAL A 186 -1 O VAL A 186 N THR A 91
SHEET 5 C 5 ILE A 193 GLY A 195 -1 N ILE A 193 O ILE A 185
SSBOND 1 CYS A 98 CYS A 101 1555 1555 2.06
CISPEP 1 THR A 182 PRO A 183 0 0.27
CRYST1 74.920 74.920 103.380 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 0.013348 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013348 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009673 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
