HEADER IMMUNE SYSTEM 23-JUL-12 4G8E
TITLE CRYSTAL STRUCTURE OF CLONE18 TCR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA CHAIN CLONE 18 TCR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BETA CHAIN CLONE 18 TCR;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS TCR, T CELL, CD1B, GMM, LIPID RECOGNITION, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GRAS,M.BHATI,J.ROSSJOHN
REVDAT 5 13-SEP-23 4G8E 1 REMARK
REVDAT 4 15-NOV-17 4G8E 1 REMARK
REVDAT 3 10-JUL-13 4G8E 1 JRNL
REVDAT 2 03-JUL-13 4G8E 1 JRNL
REVDAT 1 08-MAY-13 4G8E 0
JRNL AUTH I.VAN RHIJN,A.KASMAR,A.DE JONG,S.GRAS,M.BHATI,
JRNL AUTH 2 M.E.DOORENSPLEET,N.DE VRIES,D.I.GODFREY,J.D.ALTMAN,
JRNL AUTH 3 W.DE JAGER,J.ROSSJOHN,D.B.MOODY
JRNL TITL A CONSERVED HUMAN T CELL POPULATION TARGETS MYCOBACTERIAL
JRNL TITL 2 ANTIGENS PRESENTED BY CD1B.
JRNL REF NAT.IMMUNOL. V. 14 706 2013
JRNL REFN ISSN 1529-2908
JRNL PMID 23727893
JRNL DOI 10.1038/NI.2630
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 20660
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1059
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.32
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.62
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2762
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.4810
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2621
REMARK 3 BIN R VALUE (WORKING SET) : 0.4768
REMARK 3 BIN FREE R VALUE : 0.5685
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
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 : 3479
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.36730
REMARK 3 B22 (A**2) : -5.06190
REMARK 3 B33 (A**2) : 6.42910
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.22480
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.614
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.409
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.905
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.855
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3564 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4836 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1205 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 97 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 515 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3564 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 454 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3962 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.51
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 23.28
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G8E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073867.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-12
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.956
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.490
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: PDB ENTRY 2NW2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG1500, 10% PROPRIONATE
REMARK 280 -CACODYLATE-BIS TRIS PROPANE PH 7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 42.04500
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: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 ALA B 112
REMARK 465 ARG B 113
REMARK 465 GLY B 114
REMARK 465 LEU B 115
REMARK 465 LYS B 116
REMARK 465 HIS B 117
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN B 157 CD
REMARK 480 GLU B 240 CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLU A 15 O LEU A 94 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 8 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 LYS B 68 C - N - CA ANGL. DEV. = 15.5 DEGREES
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 GLN A 2 -92.12 -5.77
REMARK 500 PRO A 8 137.78 22.56
REMARK 500 VAL A 57 -30.49 -131.18
REMARK 500 LYS A 69 44.99 34.22
REMARK 500 SER A 99 107.83 -59.97
REMARK 500 THR A 109 -121.66 55.15
REMARK 500 PHE A 112 -37.72 26.46
REMARK 500 LYS A 142 -107.90 -73.68
REMARK 500 SER A 144 -7.27 100.82
REMARK 500 ASP A 145 -50.63 66.70
REMARK 500 LYS A 146 -6.17 52.92
REMARK 500 SER A 147 114.10 51.57
REMARK 500 ASP A 172 150.10 -47.48
REMARK 500 LYS A 173 128.03 -6.73
REMARK 500 LYS A 194 90.17 -41.88
REMARK 500 SER A 216 -35.34 -140.04
REMARK 500 MET B 48 -146.15 16.57
REMARK 500 GLU B 59 -32.20 -33.16
REMARK 500 LYS B 68 168.77 -0.36
REMARK 500 SER B 100 -166.39 -160.97
REMARK 500 PRO B 109 135.79 -25.56
REMARK 500 ASP B 171 25.36 -69.66
REMARK 500 PRO B 222 4.59 -68.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G8F RELATED DB: PDB
REMARK 900 RELATED ID: 4G8G RELATED DB: PDB
REMARK 900 RELATED ID: 4G8I RELATED DB: PDB
REMARK 900 RELATED ID: 4G9D RELATED DB: PDB
REMARK 900 RELATED ID: 4G9F RELATED DB: PDB
DBREF 4G8E A 1 217 PDB 4G8E 4G8E 1 217
DBREF 4G8E B 3 262 PDB 4G8E 4G8E 3 262
SEQRES 1 A 201 GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR
SEQRES 2 A 201 GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR
SEQRES 3 A 201 SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA
SEQRES 4 A 201 GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP
SEQRES 5 A 201 GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER
SEQRES 6 A 201 ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU
SEQRES 7 A 201 GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LEU
SEQRES 8 A 201 ASN THR GLY GLY PHE LYS THR ILE PHE GLY ALA GLY THR
SEQRES 9 A 201 ARG LEU PHE VAL LYS ALA ASN ILE GLN ASN PRO ASP PRO
SEQRES 10 A 201 ALA VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS
SEQRES 11 A 201 SER VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN
SEQRES 12 A 201 VAL SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP
SEQRES 13 A 201 LYS CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER
SEQRES 14 A 201 ASN SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA
SEQRES 15 A 201 CYS ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP
SEQRES 16 A 201 THR PHE PHE PRO SER PRO
SEQRES 1 B 247 GLY VAL THR GLN THR PRO LYS PHE ARG VAL LEU LYS THR
SEQRES 2 B 247 GLY GLN SER MET THR LEU LEU CYS ALA GLN ASP MET ASN
SEQRES 3 B 247 HIS GLU TYR MET TYR TRP TYR ARG GLN ASP PRO GLY MET
SEQRES 4 B 247 GLY LEU ARG LEU ILE HIS TYR SER VAL GLY GLU GLY THR
SEQRES 5 B 247 THR ALA LYS GLY GLU VAL PRO ASP GLY TYR ASN VAL SER
SEQRES 6 B 247 ARG LEU LYS LYS GLN ASN PHE LEU LEU GLY LEU GLU SER
SEQRES 7 B 247 ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS ALA SER
SEQRES 8 B 247 ARG PRO PRO LEU THR ALA ARG GLY LEU LYS HIS THR GLY
SEQRES 9 B 247 GLU LEU PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU
SEQRES 10 B 247 GLU ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL
SEQRES 11 B 247 PHE GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS
SEQRES 12 B 247 ALA THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP
SEQRES 13 B 247 HIS VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL
SEQRES 14 B 247 HIS SER GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU
SEQRES 15 B 247 GLN PRO ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER
SEQRES 16 B 247 ARG LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG
SEQRES 17 B 247 ASN HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER
SEQRES 18 B 247 GLU ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL
SEQRES 19 B 247 THR GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
FORMUL 3 HOH *146(H2 O)
HELIX 1 1 GLN A 95 SER A 99 5 5
HELIX 2 2 ALA B 95 THR B 99 5 5
HELIX 3 3 ASP B 134 VAL B 138 5 5
HELIX 4 4 SER B 149 GLN B 157 1 9
HELIX 5 5 ALA B 216 ASN B 221 1 6
SHEET 1 A 4 ASN A 3 ASP A 5 0
SHEET 2 A 4 VAL A 19 TYR A 25 -1 O THR A 24 N ILE A 4
SHEET 3 A 4 TYR A 86 LEU A 91 -1 O SER A 87 N CYS A 23
SHEET 4 A 4 PHE A 79 SER A 84 -1 N PHE A 82 O TYR A 88
SHEET 1 B 5 GLU A 10 THR A 14 0
SHEET 2 B 5 THR A 120 LYS A 125 1 O LYS A 125 N ALA A 13
SHEET 3 B 5 ALA A 100 ASN A 108 -1 N ALA A 100 O LEU A 122
SHEET 4 B 5 LEU A 39 GLN A 44 -1 N PHE A 40 O ALA A 105
SHEET 5 B 5 THR A 51 ASN A 56 -1 O ASN A 56 N LEU A 39
SHEET 1 C 4 GLU A 10 THR A 14 0
SHEET 2 C 4 THR A 120 LYS A 125 1 O LYS A 125 N ALA A 13
SHEET 3 C 4 ALA A 100 ASN A 108 -1 N ALA A 100 O LEU A 122
SHEET 4 C 4 LYS A 113 PHE A 116 -1 O ILE A 115 N VAL A 106
SHEET 1 D 8 VAL A 168 MET A 178 0
SHEET 2 D 8 PHE A 183 SER A 192 -1 O SER A 185 N LEU A 176
SHEET 3 D 8 VAL A 148 THR A 152 -1 N CYS A 149 O ALA A 190
SHEET 4 D 8 ALA A 134 ASP A 140 -1 N TYR A 136 O LEU A 150
SHEET 5 D 8 GLU B 142 GLU B 147 -1 O GLU B 147 N ARG A 139
SHEET 6 D 8 LYS B 158 PHE B 168 -1 O VAL B 162 N PHE B 146
SHEET 7 D 8 TYR B 206 SER B 215 -1 O LEU B 212 N LEU B 161
SHEET 8 D 8 VAL B 188 THR B 190 -1 N CYS B 189 O ARG B 211
SHEET 1 E 8 VAL A 168 MET A 178 0
SHEET 2 E 8 PHE A 183 SER A 192 -1 O SER A 185 N LEU A 176
SHEET 3 E 8 VAL A 148 THR A 152 -1 N CYS A 149 O ALA A 190
SHEET 4 E 8 ALA A 134 ASP A 140 -1 N TYR A 136 O LEU A 150
SHEET 5 E 8 GLU B 142 GLU B 147 -1 O GLU B 147 N ARG A 139
SHEET 6 E 8 LYS B 158 PHE B 168 -1 O VAL B 162 N PHE B 146
SHEET 7 E 8 TYR B 206 SER B 215 -1 O LEU B 212 N LEU B 161
SHEET 8 E 8 LEU B 195 LYS B 196 -1 N LEU B 195 O ALA B 207
SHEET 1 F 4 VAL B 4 THR B 7 0
SHEET 2 F 4 MET B 19 GLN B 25 -1 O ALA B 24 N THR B 5
SHEET 3 F 4 PHE B 87 LEU B 91 -1 O LEU B 91 N MET B 19
SHEET 4 F 4 TYR B 76 ARG B 80 -1 N ASN B 77 O GLY B 90
SHEET 1 G 6 PHE B 10 LYS B 14 0
SHEET 2 G 6 SER B 127 LEU B 132 1 O THR B 130 N LEU B 13
SHEET 3 G 6 SER B 100 ARG B 107 -1 N TYR B 102 O SER B 127
SHEET 4 G 6 TYR B 31 GLN B 44 -1 N TYR B 42 O PHE B 103
SHEET 5 G 6 LEU B 50 GLY B 58 -1 O ILE B 53 N TRP B 41
SHEET 6 G 6 THR B 61 ALA B 67 -1 O ALA B 67 N TYR B 55
SHEET 1 H 4 PHE B 10 LYS B 14 0
SHEET 2 H 4 SER B 127 LEU B 132 1 O THR B 130 N LEU B 13
SHEET 3 H 4 SER B 100 ARG B 107 -1 N TYR B 102 O SER B 127
SHEET 4 H 4 PHE B 122 PHE B 123 -1 O PHE B 122 N SER B 106
SHEET 1 I 4 LYS B 182 VAL B 184 0
SHEET 2 I 4 VAL B 173 VAL B 179 -1 N VAL B 179 O LYS B 182
SHEET 3 I 4 HIS B 225 PHE B 232 -1 O GLN B 229 N SER B 176
SHEET 4 I 4 GLN B 251 TRP B 258 -1 O ALA B 257 N PHE B 226
SSBOND 1 CYS A 23 CYS A 104 1555 1555 2.25
SSBOND 2 CYS A 149 CYS A 199 1555 1555 2.85
SSBOND 3 CYS B 23 CYS B 104 1555 1555 2.27
SSBOND 4 CYS B 163 CYS B 228 1555 1555 1.92
CISPEP 1 PRO A 8 THR A 9 0 -4.73
CISPEP 2 ALA A 46 GLY A 47 0 -4.57
CISPEP 3 ASP A 59 GLY A 60 0 2.82
CISPEP 4 SER A 195 ASP A 196 0 4.81
CISPEP 5 THR B 7 PRO B 8 0 -0.15
CISPEP 6 MET B 48 GLY B 49 0 0.91
CISPEP 7 GLY B 69 GLU B 70 0 5.70
CISPEP 8 ASP B 74 GLY B 75 0 1.38
CISPEP 9 PRO B 109 LEU B 110 0 5.51
CISPEP 10 THR B 118 GLY B 119 0 1.18
CISPEP 11 TYR B 169 PRO B 170 0 0.03
CRYST1 46.420 84.090 58.280 90.00 111.88 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 0.021542 0.000000 0.008651 0.00000
SCALE2 0.000000 0.011892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018490 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
