HEADER LIGASE 06-APR-06 2DJZ
TITLE CRYSTAL STRUCTURE OF BIOTIN PROTEIN LIGASE FROM PYROCOCCUS HORIKOSHII
TITLE 2 OT3 IN COMPLEX WITH BIOTINYL-5'-AMP, K111A MUTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 235AA LONG HYPOTHETICAL BIOTIN-[ACETYL-COA-CARBOXYLASE]
COMPND 3 LIGASE;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: BIOTIN PROTEIN LIGASE;
COMPND 6 EC: 6.3.4.15;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: OT3;
SOURCE 5 GENE: BIRA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: (DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET 11A
KEYWDS BIOTIN BIOSYNTHESIS, DIMER, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BAGAUTDINOV,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 5 25-OCT-23 2DJZ 1 REMARK
REVDAT 4 10-NOV-21 2DJZ 1 REMARK SEQADV
REVDAT 3 13-JUL-11 2DJZ 1 VERSN
REVDAT 2 24-FEB-09 2DJZ 1 VERSN
REVDAT 1 06-OCT-06 2DJZ 0
JRNL AUTH B.BAGAUTDINOV,N.KUNISHIMA
JRNL TITL LIGAND STRUCTURES OF BIOTIN PROTEIN LIGASE FROM PYROCOCCUS
JRNL TITL 2 HORIKOSHII OT3
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.43
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) (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 36969
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 : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1827
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 180
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3619
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 396
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.43000
REMARK 3 B22 (A**2) : -4.71000
REMARK 3 B33 (A**2) : 6.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.21
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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: NULL
REMARK 4
REMARK 4 2DJZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025504.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36969
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 37.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.33500
REMARK 200 R SYM FOR SHELL (I) : 0.30000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.370
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: 2DEQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, ACETATE, NAOH, PH 5.2,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 41.39350
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY B 196
REMARK 465 ASP B 197
REMARK 465 GLY B 198
REMARK 465 ARG B 233
REMARK 465 PHE B 234
REMARK 465 LEU B 235
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 ILE A 8 -63.62 -121.75
REMARK 500 VAL A 132 -76.25 -111.82
REMARK 500 PRO A 152 109.73 -58.23
REMARK 500 ASP A 206 -176.10 -178.31
REMARK 500 ASP A 229 61.04 -102.25
REMARK 500 ASN B 50 13.66 57.36
REMARK 500 SER B 67 59.27 -145.49
REMARK 500 VAL B 132 -75.05 -112.57
REMARK 500 ASP B 206 -176.13 178.34
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 BT5 A 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BT5 A 1302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DEQ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH BIOTINYL-5'-AMP BUT WITH MUTATION
REMARK 900 K111G
REMARK 900 RELATED ID: 1WGW RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH BIOTINYL-5'-AMP BUT WITH NO MUTATION
REMARK 900 RELATED ID: PHO001000147.4 RELATED DB: TARGETDB
DBREF 2DJZ A 1 235 UNP O57883 O57883_PYRHO 1 235
DBREF 2DJZ B 1 235 UNP O57883 O57883_PYRHO 1 235
SEQADV 2DJZ ALA A 111 UNP O57883 LYS 111 ENGINEERED MUTATION
SEQADV 2DJZ ALA B 111 UNP O57883 LYS 111 ENGINEERED MUTATION
SEQRES 1 A 235 MET LEU GLY LEU LYS THR SER ILE ILE GLY ARG ARG VAL
SEQRES 2 A 235 ILE TYR PHE GLN GLU ILE THR SER THR ASN GLU PHE ALA
SEQRES 3 A 235 LYS THR SER TYR LEU GLU GLU GLY THR VAL ILE VAL ALA
SEQRES 4 A 235 ASP LYS GLN THR MET GLY HIS GLY ARG LEU ASN ARG LYS
SEQRES 5 A 235 TRP GLU SER PRO GLU GLY GLY LEU TRP LEU SER ILE VAL
SEQRES 6 A 235 LEU SER PRO LYS VAL PRO GLN LYS ASP LEU PRO LYS ILE
SEQRES 7 A 235 VAL PHE LEU GLY ALA VAL GLY VAL VAL GLU THR LEU LYS
SEQRES 8 A 235 GLU PHE SER ILE ASP GLY ARG ILE LYS TRP PRO ASN ASP
SEQRES 9 A 235 VAL LEU VAL ASN TYR LYS ALA ILE ALA GLY VAL LEU VAL
SEQRES 10 A 235 GLU GLY LYS GLY ASP LYS ILE VAL LEU GLY ILE GLY LEU
SEQRES 11 A 235 ASN VAL ASN ASN LYS VAL PRO ASN GLY ALA THR SER MET
SEQRES 12 A 235 LYS LEU GLU LEU GLY SER GLU VAL PRO LEU LEU SER VAL
SEQRES 13 A 235 PHE ARG SER LEU ILE THR ASN LEU ASP ARG LEU TYR LEU
SEQRES 14 A 235 ASN PHE LEU LYS ASN PRO MET ASP ILE LEU ASN LEU VAL
SEQRES 15 A 235 ARG ASP ASN MET ILE LEU GLY VAL ARG VAL LYS ILE LEU
SEQRES 16 A 235 GLY ASP GLY SER PHE GLU GLY ILE ALA GLU ASP ILE ASP
SEQRES 17 A 235 ASP PHE GLY ARG LEU ILE ILE ARG LEU ASP SER GLY GLU
SEQRES 18 A 235 VAL LYS LYS VAL ILE TYR GLY ASP VAL SER LEU ARG PHE
SEQRES 19 A 235 LEU
SEQRES 1 B 235 MET LEU GLY LEU LYS THR SER ILE ILE GLY ARG ARG VAL
SEQRES 2 B 235 ILE TYR PHE GLN GLU ILE THR SER THR ASN GLU PHE ALA
SEQRES 3 B 235 LYS THR SER TYR LEU GLU GLU GLY THR VAL ILE VAL ALA
SEQRES 4 B 235 ASP LYS GLN THR MET GLY HIS GLY ARG LEU ASN ARG LYS
SEQRES 5 B 235 TRP GLU SER PRO GLU GLY GLY LEU TRP LEU SER ILE VAL
SEQRES 6 B 235 LEU SER PRO LYS VAL PRO GLN LYS ASP LEU PRO LYS ILE
SEQRES 7 B 235 VAL PHE LEU GLY ALA VAL GLY VAL VAL GLU THR LEU LYS
SEQRES 8 B 235 GLU PHE SER ILE ASP GLY ARG ILE LYS TRP PRO ASN ASP
SEQRES 9 B 235 VAL LEU VAL ASN TYR LYS ALA ILE ALA GLY VAL LEU VAL
SEQRES 10 B 235 GLU GLY LYS GLY ASP LYS ILE VAL LEU GLY ILE GLY LEU
SEQRES 11 B 235 ASN VAL ASN ASN LYS VAL PRO ASN GLY ALA THR SER MET
SEQRES 12 B 235 LYS LEU GLU LEU GLY SER GLU VAL PRO LEU LEU SER VAL
SEQRES 13 B 235 PHE ARG SER LEU ILE THR ASN LEU ASP ARG LEU TYR LEU
SEQRES 14 B 235 ASN PHE LEU LYS ASN PRO MET ASP ILE LEU ASN LEU VAL
SEQRES 15 B 235 ARG ASP ASN MET ILE LEU GLY VAL ARG VAL LYS ILE LEU
SEQRES 16 B 235 GLY ASP GLY SER PHE GLU GLY ILE ALA GLU ASP ILE ASP
SEQRES 17 B 235 ASP PHE GLY ARG LEU ILE ILE ARG LEU ASP SER GLY GLU
SEQRES 18 B 235 VAL LYS LYS VAL ILE TYR GLY ASP VAL SER LEU ARG PHE
SEQRES 19 B 235 LEU
HET BT5 A1301 38
HET BT5 A1302 38
HETNAM BT5 BIOTINYL-5-AMP
FORMUL 3 BT5 2(C20 H28 N7 O9 P S)
FORMUL 5 HOH *396(H2 O)
HELIX 1 1 SER A 21 SER A 29 1 9
HELIX 2 2 GLY A 47 ARG A 51 5 5
HELIX 3 3 PRO A 71 PRO A 76 5 6
HELIX 4 4 LYS A 77 PHE A 93 1 17
HELIX 5 5 SER A 142 GLY A 148 1 7
HELIX 6 6 PRO A 152 ASN A 174 1 23
HELIX 7 7 MET A 176 ASN A 185 1 10
HELIX 8 8 SER B 21 SER B 29 1 9
HELIX 9 9 GLY B 47 ARG B 51 5 5
HELIX 10 10 PRO B 71 PRO B 76 5 6
HELIX 11 11 LYS B 77 PHE B 93 1 17
HELIX 12 12 SER B 142 GLY B 148 1 7
HELIX 13 13 PRO B 152 ASN B 174 1 23
HELIX 14 14 MET B 176 MET B 186 1 11
SHEET 1 A14 ARG A 98 LYS A 100 0
SHEET 2 A14 ASP A 104 VAL A 107 -1 O LEU A 106 N ARG A 98
SHEET 3 A14 LYS A 110 GLU A 118 -1 O ILE A 112 N VAL A 105
SHEET 4 A14 ILE A 124 LEU A 130 -1 O VAL A 125 N GLU A 118
SHEET 5 A14 LEU A 60 LEU A 66 -1 N LEU A 66 O ILE A 124
SHEET 6 A14 THR A 35 ALA A 39 -1 N ILE A 37 O SER A 63
SHEET 7 A14 ARG A 12 PHE A 16 1 N ILE A 14 O VAL A 36
SHEET 8 A14 ARG B 12 ILE B 19 -1 O TYR B 15 N VAL A 13
SHEET 9 A14 THR B 35 GLN B 42 1 O VAL B 36 N ILE B 14
SHEET 10 A14 LEU B 60 LEU B 66 -1 O SER B 63 N ILE B 37
SHEET 11 A14 ILE B 124 LEU B 130 -1 O ILE B 124 N LEU B 66
SHEET 12 A14 LYS B 110 GLY B 119 -1 N GLU B 118 O VAL B 125
SHEET 13 A14 ASP B 104 VAL B 107 -1 N VAL B 105 O ILE B 112
SHEET 14 A14 ARG B 98 LYS B 100 -1 N ARG B 98 O LEU B 106
SHEET 1 B 5 VAL A 222 VAL A 225 0
SHEET 2 B 5 LEU A 213 ARG A 216 -1 N LEU A 213 O VAL A 225
SHEET 3 B 5 SER A 199 ILE A 207 -1 N ASP A 206 O ILE A 214
SHEET 4 B 5 ARG A 191 LEU A 195 -1 N ILE A 194 O PHE A 200
SHEET 5 B 5 SER A 231 PHE A 234 -1 O ARG A 233 N LYS A 193
SHEET 1 C 5 VAL B 222 VAL B 225 0
SHEET 2 C 5 LEU B 213 ARG B 216 -1 N LEU B 213 O VAL B 225
SHEET 3 C 5 PHE B 200 ILE B 207 -1 N ASP B 206 O ILE B 214
SHEET 4 C 5 VAL B 190 LEU B 195 -1 N ILE B 194 O PHE B 200
SHEET 5 C 5 ASP B 229 SER B 231 -1 O SER B 231 N LYS B 193
CISPEP 1 TRP A 101 PRO A 102 0 -0.02
CISPEP 2 TRP B 101 PRO B 102 0 0.09
SITE 1 AC1 22 SER A 21 THR A 22 ASN A 23 GLN A 42
SITE 2 AC1 22 GLY A 45 HIS A 46 GLY A 47 ARG A 48
SITE 3 AC1 22 ARG A 51 LYS A 52 TRP A 53 GLU A 54
SITE 4 AC1 22 LEU A 62 ASN A 103 ASP A 104 GLY A 114
SITE 5 AC1 22 ILE A 128 GLY A 129 ASN A 131 PRO A 137
SITE 6 AC1 22 ALA A 140 HOH A1382
SITE 1 AC2 23 HOH A1367 SER B 21 THR B 22 ASN B 23
SITE 2 AC2 23 GLN B 42 GLY B 45 HIS B 46 GLY B 47
SITE 3 AC2 23 ARG B 48 ARG B 51 LYS B 52 TRP B 53
SITE 4 AC2 23 GLU B 54 LEU B 62 ASN B 103 ASP B 104
SITE 5 AC2 23 GLY B 114 VAL B 115 ILE B 128 ASN B 131
SITE 6 AC2 23 PRO B 137 ALA B 140 HOH B 313
CRYST1 38.194 82.787 72.324 90.00 101.52 90.00 P 1 21 1 4
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 0.026182 0.000000 0.005336 0.00000
SCALE2 0.000000 0.012079 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014111 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
