HEADER IMMUNE SYSTEM 01-JAN-19 6J2E
TITLE CRYSTAL STRUCTURE OF BAT (PTEROPUS ALECTO) MHC CLASS I PTAL-N*01:01 IN
TITLE 2 COMPLEX WITH EBOLA VIRUS-DERIVED PEPTIDE EBOV-NP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS I ANTIGEN;
COMPND 3 CHAIN: A, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 7 CHAIN: B, E;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: EBOV-NP1;
COMPND 11 CHAIN: C, F;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PTEROPUS ALECTO;
SOURCE 3 ORGANISM_COMMON: BLACK FLYING FOX;
SOURCE 4 ORGANISM_TAXID: 9402;
SOURCE 5 GENE: PTAL-N;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: B2M;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 17 MOL_ID: 3;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 ORGANISM_SCIENTIFIC: EBOLA VIRUS SP.;
SOURCE 20 ORGANISM_TAXID: 205488
KEYWDS IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.LU,K.F.LIU,C.YUE,Q.LU,H.CHENG,Y.CHAI,J.X.QI,G.F.GAO,W.J.LIU
REVDAT 3 04-DEC-19 6J2E 1 TITLE
REVDAT 2 25-SEP-19 6J2E 1 TITLE COMPND
REVDAT 1 18-SEP-19 6J2E 0
JRNL AUTH D.LU,K.LIU,D.ZHANG,C.YUE,Q.LU,H.CHENG,L.WANG,Y.CHAI,J.QI,
JRNL AUTH 2 L.F.WANG,G.F.GAO,W.J.LIU
JRNL TITL PEPTIDE PRESENTATION BY BAT MHC CLASS I PROVIDES NEW INSIGHT
JRNL TITL 2 INTO THE ANTIVIRAL IMMUNITY OF BATS.
JRNL REF PLOS BIOL. V. 17 00436 2019
JRNL REFN ESSN 1545-7885
JRNL PMID 31498797
JRNL DOI 10.1371/JOURNAL.PBIO.3000436
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
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) : 49.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 52961
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2702
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.2975 - 5.5866 0.99 2873 145 0.1849 0.2254
REMARK 3 2 5.5866 - 4.4352 1.00 2765 154 0.1680 0.2086
REMARK 3 3 4.4352 - 3.8748 1.00 2742 157 0.1687 0.2096
REMARK 3 4 3.8748 - 3.5206 1.00 2720 151 0.1837 0.2183
REMARK 3 5 3.5206 - 3.2684 1.00 2712 143 0.1955 0.2532
REMARK 3 6 3.2684 - 3.0757 1.00 2737 149 0.2144 0.2412
REMARK 3 7 3.0757 - 2.9217 1.00 2693 150 0.2211 0.2848
REMARK 3 8 2.9217 - 2.7945 1.00 2711 135 0.2352 0.3391
REMARK 3 9 2.7945 - 2.6869 1.00 2721 124 0.2253 0.2645
REMARK 3 10 2.6869 - 2.5942 1.00 2717 148 0.2331 0.3482
REMARK 3 11 2.5942 - 2.5131 1.00 2694 142 0.2264 0.2605
REMARK 3 12 2.5131 - 2.4413 1.00 2693 157 0.2311 0.2673
REMARK 3 13 2.4413 - 2.3770 1.00 2693 134 0.2309 0.3241
REMARK 3 14 2.3770 - 2.3190 1.00 2645 158 0.2329 0.2925
REMARK 3 15 2.3190 - 2.2663 1.00 2737 130 0.2389 0.3074
REMARK 3 16 2.2663 - 2.2181 1.00 2660 164 0.2351 0.3105
REMARK 3 17 2.2181 - 2.1737 0.98 2594 148 0.2407 0.3061
REMARK 3 18 2.1737 - 2.1327 0.89 2382 114 0.2542 0.3259
REMARK 3 19 2.1327 - 2.0946 0.66 1770 99 0.2576 0.3183
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 6542
REMARK 3 ANGLE : 0.909 8894
REMARK 3 CHIRALITY : 0.056 892
REMARK 3 PLANARITY : 0.005 1184
REMARK 3 DIHEDRAL : 8.903 3844
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6J2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010355.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : SDMS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54243
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.3650
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SUCCINIC ACID PH 7.0, 15%(W/V)
REMARK 280 POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 88.81250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.81250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 50.37000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.29800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 50.37000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.29800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 88.81250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 50.37000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.29800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 88.81250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 50.37000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.29800
REMARK 290 SMTRY3 8 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 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 29 -122.56 52.55
REMARK 500 GLN A 227 75.70 -117.90
REMARK 500 ALA A 243 -165.80 -129.15
REMARK 500 ASN B 21 -168.81 -128.23
REMARK 500 TRP B 60 -3.57 76.74
REMARK 500 LYS B 75 -24.64 -157.13
REMARK 500 ASP C 7 -105.94 58.17
REMARK 500 ASP D 29 -123.15 50.04
REMARK 500 LEU D 183 40.45 -92.81
REMARK 500 ALA D 243 -169.97 -128.24
REMARK 500 ASP F 7 -134.34 49.93
REMARK 500 PHE F 9 75.03 -167.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 6J2E A 1 277 UNP A0A125R585_PTEAL
DBREF2 6J2E A A0A125R585 25 301
DBREF 6J2E B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 6J2E C 1 10 PDB 6J2E 6J2E 1 10
DBREF1 6J2E D 1 277 UNP A0A125R585_PTEAL
DBREF2 6J2E D A0A125R585 25 301
DBREF 6J2E E 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 6J2E F 1 10 PDB 6J2E 6J2E 1 10
SEQRES 1 A 277 GLY PHE HIS SER LEU ARG TYR PHE TYR THR ALA TRP SER
SEQRES 2 A 277 ARG PRO GLY SER GLY GLU PRO ARG PHE VAL ALA VAL GLY
SEQRES 3 A 277 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 277 ASN ALA SER PRO ARG ALA GLU PRO ARG ALA PRO TRP MET
SEQRES 5 A 277 ASP LEU VAL GLU GLN GLN ASP PRO GLN TYR TRP ASP ARG
SEQRES 6 A 277 ASN THR ARG ASN ALA ARG ASP ALA ALA GLN THR TYR ARG
SEQRES 7 A 277 VAL GLY LEU ASP ASN VAL ARG GLY TYR TYR ASN GLN SER
SEQRES 8 A 277 GLU ALA GLY SER HIS THR ILE GLN ARG MET TYR GLY CYS
SEQRES 9 A 277 ASP VAL GLY PRO HIS GLY ARG LEU LEU ARG GLY TYR ASP
SEQRES 10 A 277 GLN LEU ALA TYR ASP GLY ALA ASP TYR ILE ALA LEU ASN
SEQRES 11 A 277 GLU ASP LEU ARG SER TRP THR ALA ALA ASP LEU ALA ALA
SEQRES 12 A 277 GLN ASN THR ARG ARG LYS TRP GLU GLU ALA GLY TYR ALA
SEQRES 13 A 277 GLU ARG ASP ARG ALA TYR LEU GLU GLY GLU CYS VAL GLU
SEQRES 14 A 277 TRP LEU LEU LYS HIS LEU GLU ASN GLY ARG GLU THR LEU
SEQRES 15 A 277 LEU ARG ALA ASP PRO PRO LYS THR HIS ILE THR HIS HIS
SEQRES 16 A 277 PRO ILE SER ASP ARG GLU VAL THR LEU ARG CYS TRP ALA
SEQRES 17 A 277 LEU GLY PHE TYR PRO GLU GLU ILE THR LEU THR TRP GLN
SEQRES 18 A 277 HIS ASP GLY GLU ASP GLN THR GLN GLU MET GLU LEU VAL
SEQRES 19 A 277 GLU THR ARG PRO ASP GLY ASN GLY ALA PHE GLN LYS TRP
SEQRES 20 A 277 ALA ALA LEU VAL VAL PRO SER GLY GLU GLU GLN ARG TYR
SEQRES 21 A 277 THR CYS HIS VAL GLN HIS GLU GLY LEU PRO GLN PRO LEU
SEQRES 22 A 277 THR LEU ARG TRP
SEQRES 1 B 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 B 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 B 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 B 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 B 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 B 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 B 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 10 ASP PHE GLN GLU SER ALA ASP SER PHE LEU
SEQRES 1 D 277 GLY PHE HIS SER LEU ARG TYR PHE TYR THR ALA TRP SER
SEQRES 2 D 277 ARG PRO GLY SER GLY GLU PRO ARG PHE VAL ALA VAL GLY
SEQRES 3 D 277 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 D 277 ASN ALA SER PRO ARG ALA GLU PRO ARG ALA PRO TRP MET
SEQRES 5 D 277 ASP LEU VAL GLU GLN GLN ASP PRO GLN TYR TRP ASP ARG
SEQRES 6 D 277 ASN THR ARG ASN ALA ARG ASP ALA ALA GLN THR TYR ARG
SEQRES 7 D 277 VAL GLY LEU ASP ASN VAL ARG GLY TYR TYR ASN GLN SER
SEQRES 8 D 277 GLU ALA GLY SER HIS THR ILE GLN ARG MET TYR GLY CYS
SEQRES 9 D 277 ASP VAL GLY PRO HIS GLY ARG LEU LEU ARG GLY TYR ASP
SEQRES 10 D 277 GLN LEU ALA TYR ASP GLY ALA ASP TYR ILE ALA LEU ASN
SEQRES 11 D 277 GLU ASP LEU ARG SER TRP THR ALA ALA ASP LEU ALA ALA
SEQRES 12 D 277 GLN ASN THR ARG ARG LYS TRP GLU GLU ALA GLY TYR ALA
SEQRES 13 D 277 GLU ARG ASP ARG ALA TYR LEU GLU GLY GLU CYS VAL GLU
SEQRES 14 D 277 TRP LEU LEU LYS HIS LEU GLU ASN GLY ARG GLU THR LEU
SEQRES 15 D 277 LEU ARG ALA ASP PRO PRO LYS THR HIS ILE THR HIS HIS
SEQRES 16 D 277 PRO ILE SER ASP ARG GLU VAL THR LEU ARG CYS TRP ALA
SEQRES 17 D 277 LEU GLY PHE TYR PRO GLU GLU ILE THR LEU THR TRP GLN
SEQRES 18 D 277 HIS ASP GLY GLU ASP GLN THR GLN GLU MET GLU LEU VAL
SEQRES 19 D 277 GLU THR ARG PRO ASP GLY ASN GLY ALA PHE GLN LYS TRP
SEQRES 20 D 277 ALA ALA LEU VAL VAL PRO SER GLY GLU GLU GLN ARG TYR
SEQRES 21 D 277 THR CYS HIS VAL GLN HIS GLU GLY LEU PRO GLN PRO LEU
SEQRES 22 D 277 THR LEU ARG TRP
SEQRES 1 E 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 E 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 E 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 E 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 E 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 E 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 E 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 E 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 F 10 ASP PHE GLN GLU SER ALA ASP SER PHE LEU
FORMUL 7 HOH *370(H2 O)
HELIX 1 AA1 ALA A 49 LEU A 54 1 6
HELIX 2 AA2 GLN A 61 ASN A 89 1 29
HELIX 3 AA3 ASP A 140 ALA A 153 1 14
HELIX 4 AA4 GLY A 154 GLY A 165 1 12
HELIX 5 AA5 GLY A 165 GLY A 178 1 14
HELIX 6 AA6 GLY A 178 LEU A 183 1 6
HELIX 7 AA7 GLU A 256 GLN A 258 5 3
HELIX 8 AA8 ALA D 49 VAL D 55 1 7
HELIX 9 AA9 GLN D 61 ASN D 89 1 29
HELIX 10 AB1 ASP D 140 GLY D 154 1 15
HELIX 11 AB2 GLY D 154 GLY D 165 1 12
HELIX 12 AB3 GLY D 165 GLY D 178 1 14
HELIX 13 AB4 GLY D 178 LEU D 183 1 6
HELIX 14 AB5 GLU D 256 GLN D 258 5 3
SHEET 1 AA1 8 GLU A 46 PRO A 47 0
SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 AA1 8 GLY A 18 VAL A 28 -1 N VAL A 28 O THR A 31
SHEET 4 AA1 8 HIS A 3 ARG A 14 -1 N ARG A 6 O TYR A 27
SHEET 5 AA1 8 THR A 97 VAL A 106 -1 O TYR A 102 N TYR A 7
SHEET 6 AA1 8 LEU A 112 TYR A 121 -1 O LEU A 113 N ASP A 105
SHEET 7 AA1 8 ALA A 124 LEU A 129 -1 O LEU A 129 N ASP A 117
SHEET 8 AA1 8 TRP A 136 ALA A 138 -1 O THR A 137 N ALA A 128
SHEET 1 AA2 4 LYS A 189 PRO A 196 0
SHEET 2 AA2 4 GLU A 201 PHE A 211 -1 O TRP A 207 N HIS A 191
SHEET 3 AA2 4 PHE A 244 PRO A 253 -1 O ALA A 248 N CYS A 206
SHEET 4 AA2 4 GLU A 232 LEU A 233 -1 N GLU A 232 O ALA A 249
SHEET 1 AA3 4 LYS A 189 PRO A 196 0
SHEET 2 AA3 4 GLU A 201 PHE A 211 -1 O TRP A 207 N HIS A 191
SHEET 3 AA3 4 PHE A 244 PRO A 253 -1 O ALA A 248 N CYS A 206
SHEET 4 AA3 4 ARG A 237 PRO A 238 -1 N ARG A 237 O GLN A 245
SHEET 1 AA4 4 GLU A 225 ASP A 226 0
SHEET 2 AA4 4 THR A 217 HIS A 222 -1 N HIS A 222 O GLU A 225
SHEET 3 AA4 4 TYR A 260 GLN A 265 -1 O HIS A 263 N THR A 219
SHEET 4 AA4 4 LEU A 273 ARG A 276 -1 O LEU A 275 N CYS A 262
SHEET 1 AA5 4 LYS B 6 SER B 11 0
SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21
SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 AA6 4 LYS B 6 SER B 11 0
SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21
SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 AA7 4 GLU B 44 ARG B 45 0
SHEET 2 AA7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 AA7 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 AA8 8 GLU D 46 PRO D 47 0
SHEET 2 AA8 8 THR D 31 ASP D 37 -1 N ARG D 35 O GLU D 46
SHEET 3 AA8 8 ARG D 21 VAL D 28 -1 N VAL D 28 O THR D 31
SHEET 4 AA8 8 HIS D 3 TRP D 12 -1 N ARG D 6 O TYR D 27
SHEET 5 AA8 8 THR D 97 VAL D 106 -1 O VAL D 106 N HIS D 3
SHEET 6 AA8 8 LEU D 112 TYR D 121 -1 O LEU D 113 N ASP D 105
SHEET 7 AA8 8 ALA D 124 LEU D 129 -1 O LEU D 129 N ASP D 117
SHEET 8 AA8 8 TRP D 136 ALA D 138 -1 O THR D 137 N ALA D 128
SHEET 1 AA9 4 LYS D 189 PRO D 196 0
SHEET 2 AA9 4 GLU D 201 PHE D 211 -1 O TRP D 207 N HIS D 191
SHEET 3 AA9 4 PHE D 244 PRO D 253 -1 O ALA D 248 N CYS D 206
SHEET 4 AA9 4 GLU D 232 LEU D 233 -1 N GLU D 232 O ALA D 249
SHEET 1 AB1 4 LYS D 189 PRO D 196 0
SHEET 2 AB1 4 GLU D 201 PHE D 211 -1 O TRP D 207 N HIS D 191
SHEET 3 AB1 4 PHE D 244 PRO D 253 -1 O ALA D 248 N CYS D 206
SHEET 4 AB1 4 ARG D 237 PRO D 238 -1 N ARG D 237 O GLN D 245
SHEET 1 AB2 4 GLU D 225 ASP D 226 0
SHEET 2 AB2 4 THR D 217 HIS D 222 -1 N HIS D 222 O GLU D 225
SHEET 3 AB2 4 TYR D 260 GLN D 265 -1 O HIS D 263 N THR D 219
SHEET 4 AB2 4 LEU D 273 LEU D 275 -1 O LEU D 275 N CYS D 262
SHEET 1 AB3 4 LYS E 6 SER E 11 0
SHEET 2 AB3 4 ASN E 21 PHE E 30 -1 O ASN E 24 N TYR E 10
SHEET 3 AB3 4 PHE E 62 PHE E 70 -1 O PHE E 70 N ASN E 21
SHEET 4 AB3 4 GLU E 50 HIS E 51 -1 N GLU E 50 O TYR E 67
SHEET 1 AB4 4 LYS E 6 SER E 11 0
SHEET 2 AB4 4 ASN E 21 PHE E 30 -1 O ASN E 24 N TYR E 10
SHEET 3 AB4 4 PHE E 62 PHE E 70 -1 O PHE E 70 N ASN E 21
SHEET 4 AB4 4 SER E 55 PHE E 56 -1 N SER E 55 O TYR E 63
SHEET 1 AB5 4 GLU E 44 ARG E 45 0
SHEET 2 AB5 4 GLU E 36 LYS E 41 -1 N LYS E 41 O GLU E 44
SHEET 3 AB5 4 TYR E 78 ASN E 83 -1 O ALA E 79 N LEU E 40
SHEET 4 AB5 4 LYS E 91 LYS E 94 -1 O LYS E 91 N VAL E 82
SSBOND 1 CYS A 104 CYS A 167 1555 1555 2.09
SSBOND 2 CYS A 206 CYS A 262 1555 1555 2.02
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.05
SSBOND 4 CYS D 104 CYS D 167 1555 1555 2.09
SSBOND 5 CYS D 206 CYS D 262 1555 1555 2.02
SSBOND 6 CYS E 25 CYS E 80 1555 1555 2.03
CISPEP 1 TYR A 212 PRO A 213 0 3.71
CISPEP 2 HIS B 31 PRO B 32 0 4.18
CISPEP 3 TYR D 212 PRO D 213 0 2.62
CISPEP 4 HIS E 31 PRO E 32 0 4.49
CRYST1 100.740 102.596 177.625 90.00 90.00 90.00 C 2 2 21 16
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 0.009927 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009747 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005630 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
