HEADER TRANSFERASE 15-APR-02 1GXZ
TITLE CRYSTAL STRUCTURE OF THE EUKARYOTIC MONO-ADP-RIBOSYLTRANSFERASE
TITLE 2 ART2.2; CRYSTAL FORM B (P212121)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T-CELL ECTO-ADP-RIBOSYLTRANSFERASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADP-RIBOSYLTRANSFERASE, T-CELL NAD(P)(+)--ARGININE ADP-
COMPND 5 RIBOSYLTRANSFERASE 2, T-CELL MONO(ADP-RIBOSYL)TRANSFERASE 2,
COMPND 6 ALLOANTIGEN RT6.2, T-CELL SURFACE PROTEIN RT6.2;
COMPND 7 EC: 2.4.2.31;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NM522
KEYWDS TRANSFERASE, ADP-RIBOSYLTRANSFERASE, IMMUNO-REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MUELLER-DIECKMANN,G.E.SCHULZ
REVDAT 4 29-MAR-17 1GXZ 1 TITLE REMARK
REVDAT 3 24-FEB-09 1GXZ 1 VERSN
REVDAT 2 24-JUN-03 1GXZ 1 SHEET ATOM TER HETATM
REVDAT 2 2 1 CONECT
REVDAT 1 26-SEP-02 1GXZ 0
JRNL AUTH C.MUELLER-DIECKMANN,H.RITTER,F.HAAG,F.KOCH-NOLTE,G.E.SCHULZ
JRNL TITL STRUCTURE OF THE ECTO-ADP-RIBOSYL TRANSFERASE ART2.2 FROM
JRNL TITL 2 RAT
JRNL REF J.MOL.BIOL. V. 322 687 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12270706
JRNL DOI 10.1016/S0022-2836(02)00818-5
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.00
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) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27842
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) : 0.181
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1409
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4313
REMARK 3 BIN R VALUE (WORKING SET) : 0.1780
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 242
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3644
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 394
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.68000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : -1.44000
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) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.050 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.760 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.400 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.740 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 43.19
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 1GXZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-02.
REMARK 100 THE PDBE ID CODE IS EBI-9714.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.30
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
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 : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30925
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 33.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH8.3, 200 MM LI2SO4, 22 %
REMARK 280 PEG4000, PH 8.30
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 34.78000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.23500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.64000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.23500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.78000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.64000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 1
REMARK 465 THR A 2
REMARK 465 GLY A 3
REMARK 465 LEU B 1
REMARK 465 THR B 2
REMARK 465 GLY B 3
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 ASP A 8 -150.72 -138.60
REMARK 500 ARG A 61 -160.17 -128.21
REMARK 500 ASN A 96 72.43 -162.50
REMARK 500 HIS A 101 55.12 -94.17
REMARK 500 TYR A 102 28.73 -149.16
REMARK 500 ASP B 8 -157.27 -156.90
REMARK 500 HIS B 101 52.51 -105.12
REMARK 500 TYR B 102 29.82 -144.60
REMARK 500 ASN B 207 22.67 -147.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BRT A1227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BRT B1227
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GXY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE
REMARK 900 ART2.2 RELATED ENTRIES
REMARK 900 RELATED ID: 1GY0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE
REMARK 900 ART2.2
DBREF 1GXZ A 1 226 UNP P20974 NRT2_RAT 21 246
DBREF 1GXZ B 1 226 UNP P20974 NRT2_RAT 21 246
SEQRES 1 A 226 LEU THR GLY PRO LEU MET LEU ASP THR ALA PRO ASN ALA
SEQRES 2 A 226 PHE ASP ASP GLN TYR GLU GLY CYS VAL ASN LYS MET GLU
SEQRES 3 A 226 GLU LYS ALA PRO LEU LEU LEU GLN GLU ASP PHE ASN MET
SEQRES 4 A 226 ASN ALA LYS LEU LYS VAL ALA TRP GLU GLU ALA LYS LYS
SEQRES 5 A 226 ARG TRP ASN ASN ILE LYS PRO SER ARG SER TYR PRO LYS
SEQRES 6 A 226 GLY PHE ASN ASP PHE HIS GLY THR ALA LEU VAL ALA TYR
SEQRES 7 A 226 THR GLY SER ILE ALA VAL ASP PHE ASN ARG ALA VAL ARG
SEQRES 8 A 226 GLU PHE LYS GLU ASN PRO GLY GLN PHE HIS TYR LYS ALA
SEQRES 9 A 226 PHE HIS TYR TYR LEU THR ARG ALA LEU GLN LEU LEU SER
SEQRES 10 A 226 ASN GLY ASP CYS HIS SER VAL TYR ARG GLY THR LYS THR
SEQRES 11 A 226 ARG PHE HIS TYR THR GLY ALA GLY SER VAL ARG PHE GLY
SEQRES 12 A 226 GLN PHE THR SER SER SER LEU SER LYS LYS VAL ALA GLN
SEQRES 13 A 226 SER GLN GLU PHE PHE SER ASP HIS GLY THR LEU PHE ILE
SEQRES 14 A 226 ILE LYS THR CYS LEU GLY VAL TYR ILE LYS GLU PHE SER
SEQRES 15 A 226 PHE ARG PRO ASP GLN GLU GLU VAL LEU ILE PRO GLY TYR
SEQRES 16 A 226 GLU VAL TYR GLN LYS VAL ARG THR GLN GLY TYR ASN GLU
SEQRES 17 A 226 ILE PHE LEU ASP SER PRO LYS ARG LYS LYS SER ASN TYR
SEQRES 18 A 226 ASN CYS LEU TYR SER
SEQRES 1 B 226 LEU THR GLY PRO LEU MET LEU ASP THR ALA PRO ASN ALA
SEQRES 2 B 226 PHE ASP ASP GLN TYR GLU GLY CYS VAL ASN LYS MET GLU
SEQRES 3 B 226 GLU LYS ALA PRO LEU LEU LEU GLN GLU ASP PHE ASN MET
SEQRES 4 B 226 ASN ALA LYS LEU LYS VAL ALA TRP GLU GLU ALA LYS LYS
SEQRES 5 B 226 ARG TRP ASN ASN ILE LYS PRO SER ARG SER TYR PRO LYS
SEQRES 6 B 226 GLY PHE ASN ASP PHE HIS GLY THR ALA LEU VAL ALA TYR
SEQRES 7 B 226 THR GLY SER ILE ALA VAL ASP PHE ASN ARG ALA VAL ARG
SEQRES 8 B 226 GLU PHE LYS GLU ASN PRO GLY GLN PHE HIS TYR LYS ALA
SEQRES 9 B 226 PHE HIS TYR TYR LEU THR ARG ALA LEU GLN LEU LEU SER
SEQRES 10 B 226 ASN GLY ASP CYS HIS SER VAL TYR ARG GLY THR LYS THR
SEQRES 11 B 226 ARG PHE HIS TYR THR GLY ALA GLY SER VAL ARG PHE GLY
SEQRES 12 B 226 GLN PHE THR SER SER SER LEU SER LYS LYS VAL ALA GLN
SEQRES 13 B 226 SER GLN GLU PHE PHE SER ASP HIS GLY THR LEU PHE ILE
SEQRES 14 B 226 ILE LYS THR CYS LEU GLY VAL TYR ILE LYS GLU PHE SER
SEQRES 15 B 226 PHE ARG PRO ASP GLN GLU GLU VAL LEU ILE PRO GLY TYR
SEQRES 16 B 226 GLU VAL TYR GLN LYS VAL ARG THR GLN GLY TYR ASN GLU
SEQRES 17 B 226 ILE PHE LEU ASP SER PRO LYS ARG LYS LYS SER ASN TYR
SEQRES 18 B 226 ASN CYS LEU TYR SER
HET BRT A1227 10
HET BRT B1227 10
HETNAM BRT 5-BROMONICOTINAMIDE
FORMUL 3 BRT 2(C6 H5 BR N2 O)
FORMUL 5 HOH *394(H2 O)
HELIX 1 1 VAL A 22 MET A 39 1 18
HELIX 2 2 ALA A 41 ILE A 57 1 17
HELIX 3 3 ASN A 68 THR A 79 1 12
HELIX 4 4 SER A 81 GLU A 92 1 12
HELIX 5 5 LYS A 103 LEU A 116 1 14
HELIX 6 6 LYS A 152 GLN A 156 1 5
HELIX 7 7 VAL B 22 MET B 39 1 18
HELIX 8 8 ALA B 41 ILE B 57 1 17
HELIX 9 9 ASN B 68 THR B 79 1 12
HELIX 10 10 SER B 81 GLU B 92 1 12
HELIX 11 11 LYS B 103 LEU B 116 1 14
HELIX 12 12 LYS B 152 GLN B 156 1 5
SHEET 1 AA 2 LEU A 5 LEU A 7 0
SHEET 2 AA 2 ARG A 131 HIS A 133 1 N HIS A 133 O LEU A 5
SHEET 1 AB 5 HIS A 122 THR A 128 0
SHEET 2 AB 5 THR A 166 THR A 172 -1 O THR A 166 N THR A 128
SHEET 3 AB 5 GLU A 208 ARG A 216 1 O ILE A 209 N ILE A 169
SHEET 4 AB 5 GLU A 196 GLN A 204 -1 O VAL A 197 N LYS A 215
SHEET 5 AB 5 VAL A 140 ARG A 141 -1 O VAL A 140 N TYR A 198
SHEET 1 AC 3 VAL A 176 TYR A 177 0
SHEET 2 AC 3 GLU A 189 ILE A 192 -1 O LEU A 191 N VAL A 176
SHEET 3 AC 3 THR A 146 LEU A 150 -1 O SER A 148 N VAL A 190
SHEET 1 BA 2 LEU B 5 LEU B 7 0
SHEET 2 BA 2 ARG B 131 HIS B 133 1 N HIS B 133 O LEU B 5
SHEET 1 BB 5 HIS B 122 THR B 128 0
SHEET 2 BB 5 THR B 166 THR B 172 -1 O THR B 166 N THR B 128
SHEET 3 BB 5 GLU B 208 ARG B 216 1 O ILE B 209 N ILE B 169
SHEET 4 BB 5 GLU B 196 GLN B 204 -1 O VAL B 197 N LYS B 215
SHEET 5 BB 5 VAL B 140 ARG B 141 -1 O VAL B 140 N TYR B 198
SHEET 1 BC 3 VAL B 176 TYR B 177 0
SHEET 2 BC 3 GLU B 189 ILE B 192 -1 O LEU B 191 N VAL B 176
SHEET 3 BC 3 THR B 146 LEU B 150 -1 O SER B 148 N VAL B 190
SSBOND 1 CYS A 21 CYS A 223 1555 1555 2.03
SSBOND 2 CYS A 121 CYS A 173 1555 1555 2.03
SSBOND 3 CYS B 21 CYS B 223 1555 1555 2.03
SSBOND 4 CYS B 121 CYS B 173 1555 1555 2.04
SITE 1 AC1 9 ARG A 126 GLY A 127 SER A 147 SER A 148
SITE 2 AC1 9 SER A 149 PHE A 160 GLN A 187 HOH A2194
SITE 3 AC1 9 HOH A2195
SITE 1 AC2 7 ARG B 126 GLY B 127 SER B 147 SER B 148
SITE 2 AC2 7 PHE B 160 GLN B 187 HOH B2199
CRYST1 69.560 77.280 86.470 90.00 90.00 90.00 P 21 21 21 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 0.014376 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012940 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011565 0.00000
MTRIX1 1 -0.999330 0.015740 0.033030 34.35844 1
MTRIX2 1 0.017170 0.998910 0.043440 6.87940 1
MTRIX3 1 -0.032310 0.043980 -0.998510 42.48557 1
(ATOM LINES ARE NOT SHOWN.)
END
