HEADER HYDROLASE 26-MAY-15 5BNF
TITLE APO STRUCTURE OF PORCINE CD38
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 54-285;
COMPND 5 SYNONYM: PORCINE CD38;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: CD38;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA
KEYWDS ADP-HYDROLASE, ADP-CYCLASE, CALCIUM SIGNALLING, CADPR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.Y.TING,C.P.F.LEUNG,R.M.GRAEFF,H.C.LEE,Q.HAO,M.KOTAKA
REVDAT 1 25-MAY-16 5BNF 0
JRNL AUTH K.Y.TING,C.F.LEUNG,R.M.GRAEFF,H.C.LEE,Q.HAO,M.KOTAKA
JRNL TITL PORCINE CD38 EXHIBITS PROMINENT SECONDARY NAD(+) CYCLASE
JRNL TITL 2 ACTIVITY.
JRNL REF PROTEIN SCI. V. 25 650 2016
JRNL REFN ESSN 1469-896X
JRNL PMID 26660500
JRNL DOI 10.1002/PRO.2859
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
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) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 21027
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM SELECTION
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1080
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 : 3624
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 203
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.61500
REMARK 3 B22 (A**2) : 0.18500
REMARK 3 B33 (A**2) : 0.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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) : 5.063 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.912 ; 8.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 9.703 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 12.016; 12.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 31.88
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5BNF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21063
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.49400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PEG 400, MAGNESIUM CHLORIDE,
REMARK 280 TRIS, PH 8.5, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 34.77050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.92800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.77050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.92800
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 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 LEU A 136
REMARK 465 ALA A 137
REMARK 465 HIS A 138
REMARK 465 GLN A 139
REMARK 465 TYR A 140
REMARK 465 THR A 141
REMARK 465 LYS A 142
REMARK 465 THR A 143
REMARK 465 GLN A 144
REMARK 465 PRO A 285
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 VAL A 77 -57.89 -128.87
REMARK 500 ASP A 125 -8.08 71.69
REMARK 500 ASP A 161 -2.24 67.86
REMARK 500 CYS A 165 145.06 -176.75
REMARK 500 CYS A 184 124.45 -170.01
REMARK 500 VAL A 229 -70.62 -112.80
REMARK 500 TYR A 283 -79.28 -90.79
REMARK 500 VAL B 77 -60.04 -101.27
REMARK 500 CYS B 184 119.63 -169.72
REMARK 500 SER B 186 49.95 -85.41
REMARK 500 LYS B 222 1.60 -66.64
REMARK 500 VAL B 229 -65.68 -122.61
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 381 DISTANCE = 5.89 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5BNI RELATED DB: PDB
DBREF 5BNF A 54 285 UNP F1S5D9 F1S5D9_PIG 54 285
DBREF 5BNF B 54 285 UNP F1S5D9 F1S5D9_PIG 54 285
SEQRES 1 A 232 TRP ASN GLY LYS GLY SER THR VAL ASP PHE GLN GLU ILE
SEQRES 2 A 232 ILE LEU ARG ARG CYS TYR THR TYR ILE ARG VAL VAL GLN
SEQRES 3 A 232 PRO GLU LEU GLY ASP ARG ASP CYS GLN LYS ILE LYS LYS
SEQRES 4 A 232 ALA PHE THR ASP ALA PHE ILE SER LYS ASP PRO CYS SER
SEQRES 5 A 232 ALA ARG GLU GLU ASP TYR ASP LEU LEU MET LYS LEU GLY
SEQRES 6 A 232 HIS GLN THR VAL PRO CYS ASP LYS THR VAL PHE TRP SER
SEQRES 7 A 232 LYS THR LYS GLU LEU ALA HIS GLN TYR THR LYS THR GLN
SEQRES 8 A 232 LYS GLY LEU PHE THR LEU GLU ASN THR LEU LEU GLY TYR
SEQRES 9 A 232 ILE ALA ASP ASP LEU SER TRP CYS GLY LYS VAL GLY SER
SEQRES 10 A 232 SER GLU ILE ASN LEU GLU SER CYS PRO ASP ARG ARG ASN
SEQRES 11 A 232 CYS ASN SER ASN PHE VAL SER VAL PHE TRP ASN LEU LEU
SEQRES 12 A 232 SER LYS ARG PHE ALA GLU ASN ALA CYS GLY MET VAL GLN
SEQRES 13 A 232 VAL PHE LEU ASN GLY SER ILE SER ASN ALA PHE ASP LYS
SEQRES 14 A 232 THR SER THR PHE GLY ARG VAL GLU VAL HIS SER LEU GLN
SEQRES 15 A 232 PRO SER LYS VAL HIS THR LEU LYS ALA TRP VAL ILE HIS
SEQRES 16 A 232 ASP SER GLY LYS THR PRO ARG ASP THR CYS SER GLY SER
SEQRES 17 A 232 SER ILE ASN GLU LEU GLN LEU ILE LEU ARG GLY LYS ASN
SEQRES 18 A 232 ILE LYS PHE THR CYS GLN GLU ASN TYR ARG PRO
SEQRES 1 B 232 TRP ASN GLY LYS GLY SER THR VAL ASP PHE GLN GLU ILE
SEQRES 2 B 232 ILE LEU ARG ARG CYS TYR THR TYR ILE ARG VAL VAL GLN
SEQRES 3 B 232 PRO GLU LEU GLY ASP ARG ASP CYS GLN LYS ILE LYS LYS
SEQRES 4 B 232 ALA PHE THR ASP ALA PHE ILE SER LYS ASP PRO CYS SER
SEQRES 5 B 232 ALA ARG GLU GLU ASP TYR ASP LEU LEU MET LYS LEU GLY
SEQRES 6 B 232 HIS GLN THR VAL PRO CYS ASP LYS THR VAL PHE TRP SER
SEQRES 7 B 232 LYS THR LYS GLU LEU ALA HIS GLN TYR THR LYS THR GLN
SEQRES 8 B 232 LYS GLY LEU PHE THR LEU GLU ASN THR LEU LEU GLY TYR
SEQRES 9 B 232 ILE ALA ASP ASP LEU SER TRP CYS GLY LYS VAL GLY SER
SEQRES 10 B 232 SER GLU ILE ASN LEU GLU SER CYS PRO ASP ARG ARG ASN
SEQRES 11 B 232 CYS ASN SER ASN PHE VAL SER VAL PHE TRP ASN LEU LEU
SEQRES 12 B 232 SER LYS ARG PHE ALA GLU ASN ALA CYS GLY MET VAL GLN
SEQRES 13 B 232 VAL PHE LEU ASN GLY SER ILE SER ASN ALA PHE ASP LYS
SEQRES 14 B 232 THR SER THR PHE GLY ARG VAL GLU VAL HIS SER LEU GLN
SEQRES 15 B 232 PRO SER LYS VAL HIS THR LEU LYS ALA TRP VAL ILE HIS
SEQRES 16 B 232 ASP SER GLY LYS THR PRO ARG ASP THR CYS SER GLY SER
SEQRES 17 B 232 SER ILE ASN GLU LEU GLN LEU ILE LEU ARG GLY LYS ASN
SEQRES 18 B 232 ILE LYS PHE THR CYS GLN GLU ASN TYR ARG PRO
FORMUL 3 HOH *203(H2 O)
HELIX 1 AA1 ASP A 62 VAL A 77 1 16
HELIX 2 AA2 GLN A 79 GLY A 83 5 5
HELIX 3 AA3 ASP A 86 ILE A 99 1 14
HELIX 4 AA4 ARG A 107 ASP A 110 5 4
HELIX 5 AA5 TYR A 111 GLY A 118 1 8
HELIX 6 AA6 THR A 149 ASN A 152 5 4
HELIX 7 AA7 THR A 153 ASP A 160 1 8
HELIX 8 AA8 ASN A 187 ASN A 203 1 17
HELIX 9 AA9 SER A 224 VAL A 229 1 6
HELIX 10 AB1 VAL A 229 LEU A 234 1 6
HELIX 11 AB2 GLY A 260 LYS A 273 1 14
HELIX 12 AB3 ASP B 62 VAL B 77 1 16
HELIX 13 AB4 GLN B 79 GLY B 83 5 5
HELIX 14 AB5 ASP B 86 ILE B 99 1 14
HELIX 15 AB6 ARG B 107 ASP B 110 5 4
HELIX 16 AB7 TYR B 111 GLY B 118 1 8
HELIX 17 AB8 LYS B 134 THR B 141 5 8
HELIX 18 AB9 THR B 149 ASN B 152 5 4
HELIX 19 AC1 THR B 153 ASP B 160 1 8
HELIX 20 AC2 ASN B 187 ALA B 204 1 18
HELIX 21 AC3 SER B 224 VAL B 229 1 6
HELIX 22 AC4 VAL B 229 LEU B 234 1 6
HELIX 23 AC5 GLY B 260 LYS B 273 1 14
SHEET 1 AA1 4 VAL A 128 TRP A 130 0
SHEET 2 AA1 4 GLY A 206 ASN A 213 1 O PHE A 211 N PHE A 129
SHEET 3 AA1 4 VAL A 239 ILE A 247 1 O TRP A 245 N LEU A 212
SHEET 4 AA1 4 LYS A 276 ASN A 282 1 O THR A 278 N ALA A 244
SHEET 1 AA2 4 VAL B 128 TRP B 130 0
SHEET 2 AA2 4 GLY B 206 ASN B 213 1 O PHE B 211 N PHE B 129
SHEET 3 AA2 4 VAL B 239 HIS B 248 1 O LYS B 243 N VAL B 208
SHEET 4 AA2 4 LYS B 276 TYR B 283 1 O THR B 278 N ALA B 244
SSBOND 1 CYS A 71 CYS A 87 1555 1555 2.03
SSBOND 2 CYS A 104 CYS A 184 1555 1555 2.05
SSBOND 3 CYS A 124 CYS A 205 1555 1555 2.04
SSBOND 4 CYS A 165 CYS A 178 1555 1555 2.04
SSBOND 5 CYS A 258 CYS A 279 1555 1555 2.04
SSBOND 6 CYS B 71 CYS B 87 1555 1555 2.04
SSBOND 7 CYS B 104 CYS B 184 1555 1555 2.04
SSBOND 8 CYS B 124 CYS B 205 1555 1555 2.04
SSBOND 9 CYS B 165 CYS B 178 1555 1555 2.04
SSBOND 10 CYS B 258 CYS B 279 1555 1555 2.05
CRYST1 69.541 103.856 63.689 90.00 90.00 90.00 P 21 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 0.014380 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015701 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
