HEADER MEMBRANE PROTEIN 21-FEB-07 2OY5
TITLE THE CRYSTAL STRUCTURE OF OSPA MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER SURFACE PROTEIN A;
COMPND 3 CHAIN: O;
COMPND 4 FRAGMENT: RESIDUES 27-273;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;
SOURCE 3 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;
SOURCE 4 ORGANISM_TAXID: 139;
SOURCE 5 GENE: OSPA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS BETA-SHEET, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MAKABE,V.TERECHKO,M.BIANCALANA,S.YAN,S.KOIDE
REVDAT 5 30-AUG-23 2OY5 1 REMARK
REVDAT 4 20-OCT-21 2OY5 1 SEQADV
REVDAT 3 30-MAY-18 2OY5 1 JRNL
REVDAT 2 24-FEB-09 2OY5 1 VERSN
REVDAT 1 04-MAR-08 2OY5 0
JRNL AUTH M.BIANCALANA,K.MAKABE,S.YAN,S.KOIDE
JRNL TITL AROMATIC CLUSTER MUTATIONS PRODUCE FOCAL MODULATIONS OF
JRNL TITL 2 BETA-SHEET STRUCTURE.
JRNL REF PROTEIN SCI. V. 24 841 2015
JRNL REFN ESSN 1469-896X
JRNL PMID 25645104
JRNL DOI 10.1002/PRO.2657
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 25029
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 + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1340
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1809
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1885
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 293
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 1.56000
REMARK 3 B33 (A**2) : -1.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.19000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.286
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1958 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1764 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2659 ; 1.365 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4174 ; 0.860 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 269 ; 5.479 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 70 ;34.079 ;26.857
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 379 ;12.179 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;20.063 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 326 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2169 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 340 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 205 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1321 ; 0.166 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 832 ; 0.147 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 891 ; 0.070 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 118 ; 0.133 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 7 ; 0.109 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 12 ; 0.182 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.208 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1653 ; 1.035 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 531 ; 0.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2051 ; 1.180 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 823 ; 2.254 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 598 ; 3.114 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2OY5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041729.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28857
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.62300
REMARK 200 R SYM FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2G8C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG4000, 8.5% ISOPROPANOL, 0.1M
REMARK 280 HEPES, 15% GLYCEROL, PH 7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 28.80100
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O
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 O 23
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 O 60 4.07 80.02
REMARK 500 ALA O 83 2.65 83.54
REMARK 500 SER O 107 -33.51 -135.56
REMARK 500 LYS O 119 -3.17 84.81
REMARK 500 SER O 229 -1.32 78.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OL6 RELATED DB: PDB
REMARK 900 RELATED ID: 2OL7 RELATED DB: PDB
REMARK 900 RELATED ID: 2OL8 RELATED DB: PDB
REMARK 900 RELATED ID: 2OY1 RELATED DB: PDB
REMARK 900 RELATED ID: 2OY7 RELATED DB: PDB
REMARK 900 RELATED ID: 2OY8 RELATED DB: PDB
REMARK 900 RELATED ID: 2OYB RELATED DB: PDB
DBREF 2OY5 O 27 273 UNP Q45040 Q45040_BORBU 27 273
SEQADV 2OY5 GLY O 23 UNP Q45040 EXPRESSION TAG
SEQADV 2OY5 SER O 24 UNP Q45040 EXPRESSION TAG
SEQADV 2OY5 HIS O 25 UNP Q45040 EXPRESSION TAG
SEQADV 2OY5 MET O 26 UNP Q45040 EXPRESSION TAG
SEQADV 2OY5 SER O 37 UNP Q45040 GLU 37 ENGINEERED MUTATION
SEQADV 2OY5 SER O 45 UNP Q45040 GLU 45 ENGINEERED MUTATION
SEQADV 2OY5 SER O 46 UNP Q45040 LYS 46 ENGINEERED MUTATION
SEQADV 2OY5 ALA O 48 UNP Q45040 LYS 48 ENGINEERED MUTATION
SEQADV 2OY5 ALA O 60 UNP Q45040 LYS 60 ENGINEERED MUTATION
SEQADV 2OY5 SER O 64 UNP Q45040 LYS 64 ENGINEERED MUTATION
SEQADV 2OY5 ALA O 83 UNP Q45040 LYS 83 ENGINEERED MUTATION
SEQADV 2OY5 SER O 104 UNP Q45040 GLU 104 ENGINEERED MUTATION
SEQADV 2OY5 SER O 107 UNP Q45040 LYS 107 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 111 UNP Q45040 SER 111 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 113 UNP Q45040 LYS 113 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 115 UNP Q45040 THR 115 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 121 UNP Q45040 SER 121 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 123 UNP Q45040 GLU 123 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 125 UNP Q45040 LYS 125 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 134 UNP Q45040 GLU 134 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 136 UNP Q45040 ILE 136 ENGINEERED MUTATION
SEQADV 2OY5 TYR O 138 UNP Q45040 THR 138 ENGINEERED MUTATION
SEQADV 2OY5 SER O 239 UNP Q45040 LYS 239 ENGINEERED MUTATION
SEQADV 2OY5 SER O 240 UNP Q45040 GLU 240 ENGINEERED MUTATION
SEQADV 2OY5 SER O 254 UNP Q45040 LYS 254 ENGINEERED MUTATION
SEQRES 1 O 251 GLY SER HIS MET LYS ASN SER VAL SER VAL ASP LEU PRO
SEQRES 2 O 251 GLY SER MET LYS VAL LEU VAL SER LYS SER SER ASN ALA
SEQRES 3 O 251 ASP GLY LYS TYR ASP LEU ILE ALA THR VAL ASP ALA LEU
SEQRES 4 O 251 GLU LEU SER GLY THR SER ASP LYS ASN ASN GLY SER GLY
SEQRES 5 O 251 VAL LEU GLU GLY VAL LYS ALA ASP ALA SER LYS VAL LYS
SEQRES 6 O 251 LEU THR ILE SER ASP ASP LEU GLY GLN THR THR LEU GLU
SEQRES 7 O 251 VAL PHE LYS SER ASP GLY SER THR LEU VAL TYR LYS TYR
SEQRES 8 O 251 VAL TYR SER LYS ASP LYS SER TYR THR TYR GLU TYR PHE
SEQRES 9 O 251 ASN GLU LYS GLY GLU VAL SER TYR LYS TYR ILE TYR ARG
SEQRES 10 O 251 ALA ASP GLY THR ARG LEU GLU TYR THR GLY ILE LYS SER
SEQRES 11 O 251 ASP GLY SER GLY LYS ALA LYS GLU VAL LEU LYS GLY TYR
SEQRES 12 O 251 VAL LEU GLU GLY THR LEU THR ALA GLU LYS THR THR LEU
SEQRES 13 O 251 VAL VAL LYS GLU GLY THR VAL THR LEU SER LYS ASN ILE
SEQRES 14 O 251 SER LYS SER GLY GLU VAL SER VAL GLU LEU ASN ASP THR
SEQRES 15 O 251 ASP SER SER ALA ALA THR LYS LYS THR ALA ALA TRP ASN
SEQRES 16 O 251 SER GLY THR SER THR LEU THR ILE THR VAL ASN SER LYS
SEQRES 17 O 251 LYS THR LYS ASP LEU VAL PHE THR SER SER ASN THR ILE
SEQRES 18 O 251 THR VAL GLN GLN TYR ASP SER ASN GLY THR SER LEU GLU
SEQRES 19 O 251 GLY SER ALA VAL GLU ILE THR LYS LEU ASP GLU ILE LYS
SEQRES 20 O 251 ASN ALA LEU LYS
FORMUL 2 HOH *293(H2 O)
HELIX 1 1 PRO O 35 SER O 37 5 3
HELIX 2 2 LYS O 264 LEU O 272 1 9
SHEET 1 A 4 SER O 29 LEU O 34 0
SHEET 2 A 4 MET O 38 SER O 43 -1 O MET O 38 N LEU O 34
SHEET 3 A 4 TYR O 52 VAL O 58 -1 O ILE O 55 N LEU O 41
SHEET 4 A 4 LEU O 61 SER O 67 -1 O LEU O 63 N ALA O 56
SHEET 1 B12 GLY O 74 VAL O 79 0
SHEET 2 B12 LYS O 85 ILE O 90 -1 O LEU O 88 N LEU O 76
SHEET 3 B12 GLN O 96 PHE O 102 -1 O PHE O 102 N LYS O 85
SHEET 4 B12 LEU O 109 SER O 116 -1 O VAL O 110 N VAL O 101
SHEET 5 B12 TYR O 121 PHE O 126 -1 O GLU O 124 N LYS O 112
SHEET 6 B12 VAL O 132 TYR O 138 -1 O TYR O 138 N TYR O 121
SHEET 7 B12 ARG O 144 THR O 148 -1 O TYR O 147 N LYS O 135
SHEET 8 B12 GLY O 156 VAL O 161 -1 O LYS O 157 N THR O 148
SHEET 9 B12 VAL O 166 LEU O 171 -1 O LEU O 167 N GLU O 160
SHEET 10 B12 LYS O 175 GLU O 182 -1 O VAL O 179 N GLU O 168
SHEET 11 B12 VAL O 185 SER O 192 -1 O LEU O 187 N VAL O 180
SHEET 12 B12 VAL O 197 ASP O 203 -1 O SER O 198 N ASN O 190
SHEET 1 C 5 LYS O 212 ASN O 217 0
SHEET 2 C 5 THR O 222 VAL O 227 -1 O THR O 224 N ALA O 215
SHEET 3 C 5 LYS O 230 PHE O 237 -1 O THR O 232 N ILE O 225
SHEET 4 C 5 ILE O 243 GLN O 247 -1 O GLN O 246 N ASP O 234
SHEET 5 C 5 VAL O 260 GLU O 261 -1 O VAL O 260 N VAL O 245
CRYST1 37.004 57.602 67.746 90.00 95.43 90.00 P 1 21 1 2
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 0.027024 0.000000 0.002570 0.00000
SCALE2 0.000000 0.017361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014828 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
