HEADER IMMUNE SYSTEM 23-JUL-17 5WJL
TITLE CRYSTAL STRUCTURE OF HLA-A*11:01 WITH GTS1 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-11 ALPHA CHAIN;
COMPND 3 CHAIN: A, D, G;
COMPND 4 SYNONYM: MHC CLASS I ANTIGEN A*11;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 8 CHAIN: B, E, H;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: GTS1 PEPTIDE;
COMPND 12 CHAIN: C, F, I;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-A, HLAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET30;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: DENGUE VIRUS 1;
SOURCE 24 ORGANISM_TAXID: 11053;
SOURCE 25 OTHER_DETAILS: GL BIOCHEM
KEYWDS HLA, TCR, DENGUE, CD8 T CELLS, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GRAS,J.ROSSJOHN
REVDAT 4 04-OCT-23 5WJL 1 REMARK
REVDAT 3 25-OCT-17 5WJL 1 JRNL
REVDAT 2 11-OCT-17 5WJL 1 JRNL
REVDAT 1 20-SEP-17 5WJL 0
JRNL AUTH A.CULSHAW,K.LADELL,S.GRAS,J.E.MCLAREN,K.L.MINERS,C.FARENC,
JRNL AUTH 2 H.VAN DEN HEUVEL,E.GOSTICK,W.DEJNIRATTISAI,
JRNL AUTH 3 A.WANGTEERAPRASERT,T.DUANGCHINDA,P.CHOTIYARNWONG,
JRNL AUTH 4 W.LIMPITIKUL,S.VASANAWATHANA,P.MALASIT,T.DONG,J.ROSSJOHN,
JRNL AUTH 5 J.MONGKOLSAPAYA,D.A.PRICE,G.R.SCREATON
JRNL TITL GERMLINE BIAS DICTATES CROSS-SEROTYPE REACTIVITY IN A COMMON
JRNL TITL 2 DENGUE-VIRUS-SPECIFIC CD8(+) T CELL RESPONSE.
JRNL REF NAT. IMMUNOL. V. 18 1228 2017
JRNL REFN ESSN 1529-2916
JRNL PMID 28945243
JRNL DOI 10.1038/NI.3850
REMARK 2
REMARK 2 RESOLUTION. 3.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36205
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1815
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 : 18
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2952
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2474
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2815
REMARK 3 BIN R VALUE (WORKING SET) : 0.2448
REMARK 3 BIN FREE R VALUE : 0.3001
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.64
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 137
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 : 9426
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 87.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -22.83550
REMARK 3 B22 (A**2) : 6.86380
REMARK 3 B33 (A**2) : 15.97160
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -14.73390
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.562
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.358
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
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 : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9677 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 13125 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3347 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 279 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1403 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9677 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1197 ; 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 : 10834 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.24
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.09
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 23.48
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 5WJL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000229144.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36207
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 46.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.82300
REMARK 200 R SYM FOR SHELL (I) : 0.01900
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: PHASER
REMARK 200 STARTING MODEL: 3GSO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4-1.8M NH4SO4, 0.1M NA-CACODYLATE
REMARK 280 PH6.5, 200MM NACL, 2% ETHYLEN GLYCOL, PH 8.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 77.75000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.09900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 77.75000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 75.09900
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, 3
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: 4560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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: 4620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 350
REMARK 350 BIOMOLECULE: 3
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: 4350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I
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: 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 OD2 ASP H 59 OG SER H 61 1.21
REMARK 500 CG ASP H 59 OG SER H 61 1.98
REMARK 500 OH TYR G 159 O GLY I 1 2.16
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 ASP A 29 -122.25 54.08
REMARK 500 PHE A 33 -25.53 -140.19
REMARK 500 ALA A 40 130.76 -39.27
REMARK 500 TYR A 85 27.66 -77.82
REMARK 500 ASN A 86 74.41 23.29
REMARK 500 PHE A 109 147.97 -32.80
REMARK 500 LEU A 110 -52.47 -139.71
REMARK 500 TYR A 123 -61.23 -109.30
REMARK 500 ALA A 199 136.60 178.02
REMARK 500 GLN B 8 87.56 -162.04
REMARK 500 ALA B 15 92.00 -57.66
REMARK 500 HIS B 31 130.30 -170.95
REMARK 500 PRO B 32 174.04 -58.77
REMARK 500 ARG B 45 107.82 -40.42
REMARK 500 TRP B 60 -1.21 87.10
REMARK 500 ALA B 79 -152.79 -144.53
REMARK 500 PRO C 6 -88.66 -37.90
REMARK 500 ARG D 17 3.01 -50.28
REMARK 500 PRO D 20 155.29 -48.44
REMARK 500 ASP D 29 -118.05 59.30
REMARK 500 ASN D 86 74.32 59.81
REMARK 500 LEU D 110 -54.66 -128.30
REMARK 500 TYR D 123 -68.14 -96.74
REMARK 500 ASP D 137 -153.69 -142.38
REMARK 500 SER D 195 -167.85 -122.19
REMARK 500 PRO D 210 -169.15 -73.68
REMARK 500 LEU D 270 142.04 -39.34
REMARK 500 PRO E 5 150.13 -47.97
REMARK 500 ASN E 21 -158.05 -132.82
REMARK 500 HIS E 31 130.05 -171.74
REMARK 500 LYS E 48 65.75 69.92
REMARK 500 TRP E 60 3.48 92.04
REMARK 500 PRO F 6 -92.74 -36.36
REMARK 500 ILE F 7 78.68 59.15
REMARK 500 ARG G 17 7.18 -56.97
REMARK 500 ASP G 29 -134.97 51.36
REMARK 500 TRP G 51 -9.33 -58.67
REMARK 500 PHE G 109 146.24 -30.41
REMARK 500 LEU G 110 -58.01 -130.99
REMARK 500 TYR G 123 -63.65 -106.11
REMARK 500 ASP G 137 -148.42 -135.30
REMARK 500 ASP G 227 -4.47 100.38
REMARK 500 SER G 251 123.36 -36.57
REMARK 500 GLU G 253 9.11 -67.02
REMARK 500 PRO H 5 101.44 -58.39
REMARK 500 SER H 28 -161.40 -110.34
REMARK 500 HIS H 31 131.10 163.63
REMARK 500 LEU H 54 107.17 -47.32
REMARK 500 TRP H 60 0.54 86.29
REMARK 500 PHE H 62 178.81 -54.53
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 316 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 317 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 318 DISTANCE = 7.31 ANGSTROMS
REMARK 525 HOH A 319 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH A 320 DISTANCE = 9.24 ANGSTROMS
REMARK 525 HOH B 106 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH B 107 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH C 202 DISTANCE = 9.65 ANGSTROMS
REMARK 525 HOH D 417 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH D 418 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH D 419 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH D 420 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH D 421 DISTANCE = 7.19 ANGSTROMS
REMARK 525 HOH D 422 DISTANCE = 8.08 ANGSTROMS
REMARK 525 HOH D 423 DISTANCE = 10.60 ANGSTROMS
REMARK 525 HOH D 424 DISTANCE = 10.92 ANGSTROMS
REMARK 525 HOH D 425 DISTANCE = 12.24 ANGSTROMS
REMARK 525 HOH D 426 DISTANCE = 13.27 ANGSTROMS
REMARK 525 HOH D 427 DISTANCE = 14.43 ANGSTROMS
REMARK 525 HOH D 428 DISTANCE = 14.93 ANGSTROMS
REMARK 525 HOH E 204 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH E 205 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH E 206 DISTANCE = 13.81 ANGSTROMS
REMARK 525 HOH F 103 DISTANCE = 8.18 ANGSTROMS
REMARK 525 HOH G 313 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH G 314 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH G 315 DISTANCE = 7.33 ANGSTROMS
REMARK 525 HOH G 316 DISTANCE = 7.73 ANGSTROMS
REMARK 525 HOH G 317 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH G 318 DISTANCE = 8.38 ANGSTROMS
REMARK 525 HOH G 319 DISTANCE = 9.18 ANGSTROMS
REMARK 525 HOH G 320 DISTANCE = 10.31 ANGSTROMS
REMARK 525 HOH H 104 DISTANCE = 11.75 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 101
DBREF 5WJL A 1 274 UNP P13746 1A11_HUMAN 25 298
DBREF 5WJL B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5WJL C 1 10 PDB 5WJL 5WJL 1 10
DBREF 5WJL D 1 274 UNP P13746 1A11_HUMAN 25 298
DBREF 5WJL E 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5WJL F 1 10 PDB 5WJL 5WJL 1 10
DBREF 5WJL G 1 274 UNP P13746 1A11_HUMAN 25 298
DBREF 5WJL H 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5WJL I 1 10 PDB 5WJL 5WJL 1 10
SEQADV 5WJL MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 5WJL MET E 0 UNP P61769 INITIATING METHIONINE
SEQADV 5WJL MET H 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 274 GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER
SEQRES 2 A 274 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 274 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 274 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 274 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLN GLU THR ARG
SEQRES 6 A 274 ASN VAL LYS ALA GLN SER GLN THR ASP ARG VAL ASP LEU
SEQRES 7 A 274 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ASP GLY
SEQRES 8 A 274 SER HIS THR ILE GLN ILE MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 274 PRO ASP GLY ARG PHE LEU ARG GLY TYR ARG GLN ASP ALA
SEQRES 10 A 274 TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 A 274 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 A 274 LYS ARG LYS TRP GLU ALA ALA HIS ALA ALA GLU GLN GLN
SEQRES 13 A 274 ARG ALA TYR LEU GLU GLY ARG CYS VAL GLU TRP LEU ARG
SEQRES 14 A 274 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 274 ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE SER
SEQRES 16 A 274 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 274 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 274 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 274 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 274 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 274 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 274 TRP
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 10 GLY THR SER GLY SER PRO ILE VAL ASN ARG
SEQRES 1 D 274 GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER
SEQRES 2 D 274 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 D 274 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 D 274 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 D 274 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLN GLU THR ARG
SEQRES 6 D 274 ASN VAL LYS ALA GLN SER GLN THR ASP ARG VAL ASP LEU
SEQRES 7 D 274 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ASP GLY
SEQRES 8 D 274 SER HIS THR ILE GLN ILE MET TYR GLY CYS ASP VAL GLY
SEQRES 9 D 274 PRO ASP GLY ARG PHE LEU ARG GLY TYR ARG GLN ASP ALA
SEQRES 10 D 274 TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 D 274 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 D 274 LYS ARG LYS TRP GLU ALA ALA HIS ALA ALA GLU GLN GLN
SEQRES 13 D 274 ARG ALA TYR LEU GLU GLY ARG CYS VAL GLU TRP LEU ARG
SEQRES 14 D 274 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 D 274 ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE SER
SEQRES 16 D 274 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 D 274 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 D 274 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 D 274 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 D 274 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS
SEQRES 21 D 274 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 D 274 TRP
SEQRES 1 E 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 E 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 E 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 E 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 E 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 E 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 E 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 E 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 F 10 GLY THR SER GLY SER PRO ILE VAL ASN ARG
SEQRES 1 G 274 GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER
SEQRES 2 G 274 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 G 274 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 G 274 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 G 274 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLN GLU THR ARG
SEQRES 6 G 274 ASN VAL LYS ALA GLN SER GLN THR ASP ARG VAL ASP LEU
SEQRES 7 G 274 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ASP GLY
SEQRES 8 G 274 SER HIS THR ILE GLN ILE MET TYR GLY CYS ASP VAL GLY
SEQRES 9 G 274 PRO ASP GLY ARG PHE LEU ARG GLY TYR ARG GLN ASP ALA
SEQRES 10 G 274 TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 G 274 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 G 274 LYS ARG LYS TRP GLU ALA ALA HIS ALA ALA GLU GLN GLN
SEQRES 13 G 274 ARG ALA TYR LEU GLU GLY ARG CYS VAL GLU TRP LEU ARG
SEQRES 14 G 274 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 G 274 ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE SER
SEQRES 16 G 274 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 G 274 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 G 274 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 G 274 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 G 274 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS
SEQRES 21 G 274 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 G 274 TRP
SEQRES 1 H 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 H 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 H 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 H 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 H 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 H 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 H 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 H 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 I 10 GLY THR SER GLY SER PRO ILE VAL ASN ARG
HET CL C 101 1
HET CL D 301 1
HET CL E 101 1
HETNAM CL CHLORIDE ION
FORMUL 10 CL 3(CL 1-)
FORMUL 13 HOH *91(H2 O)
HELIX 1 AA1 ALA A 49 GLN A 54 1 6
HELIX 2 AA2 GLY A 56 TYR A 85 1 30
HELIX 3 AA3 ASP A 137 HIS A 151 1 15
HELIX 4 AA4 HIS A 151 GLY A 162 1 12
HELIX 5 AA5 GLY A 162 GLY A 175 1 14
HELIX 6 AA6 GLY A 175 GLN A 180 1 6
HELIX 7 AA7 GLY A 252 GLN A 255 5 4
HELIX 8 AA8 ALA D 49 GLU D 55 5 7
HELIX 9 AA9 GLY D 56 ASN D 86 1 31
HELIX 10 AB1 ASP D 137 ALA D 150 1 14
HELIX 11 AB2 HIS D 151 GLY D 162 1 12
HELIX 12 AB3 GLY D 162 GLY D 175 1 14
HELIX 13 AB4 GLY D 175 GLN D 180 1 6
HELIX 14 AB5 ALA G 49 GLU G 53 5 5
HELIX 15 AB6 GLY G 56 TYR G 85 1 30
HELIX 16 AB7 MET G 138 ALA G 150 1 13
HELIX 17 AB8 HIS G 151 GLY G 162 1 12
HELIX 18 AB9 GLY G 162 GLY G 175 1 14
HELIX 19 AC1 GLY G 175 GLN G 180 1 6
HELIX 20 AC2 GLY G 252 GLN G 255 5 4
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 ARG A 21 VAL A 28 -1 N GLY A 26 O PHE A 33
SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N THR A 10 O ILE A 23
SHEET 5 AA1 8 THR A 94 VAL A 103 -1 O ILE A 95 N SER A 11
SHEET 6 AA1 8 PHE A 109 TYR A 118 -1 O ALA A 117 N GLN A 96
SHEET 7 AA1 8 LYS A 121 LEU A 126 -1 O TYR A 123 N ASP A 116
SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 AA2 4 LYS A 186 HIS A 192 0
SHEET 2 AA2 4 ALA A 199 PHE A 208 -1 O ARG A 202 N THR A 190
SHEET 3 AA2 4 PHE A 241 VAL A 249 -1 O VAL A 247 N LEU A 201
SHEET 4 AA2 4 THR A 228 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 AA3 4 LYS A 186 HIS A 192 0
SHEET 2 AA3 4 ALA A 199 PHE A 208 -1 O ARG A 202 N THR A 190
SHEET 3 AA3 4 PHE A 241 VAL A 249 -1 O VAL A 247 N LEU A 201
SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 AA4 4 GLU A 222 GLN A 224 0
SHEET 2 AA4 4 ILE A 213 ARG A 219 -1 N TRP A 217 O GLN A 224
SHEET 3 AA4 4 TYR A 257 HIS A 263 -1 O THR A 258 N GLN A 218
SHEET 4 AA4 4 LEU A 270 ARG A 273 -1 O LEU A 272 N CYS A 259
SHEET 1 AA5 4 VAL B 9 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 VAL B 9 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 ARG B 81 N ASP B 38
SHEET 4 AA7 4 LYS B 91 ILE B 92 -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 VAL D 12 -1 N VAL D 12 O ARG D 21
SHEET 5 AA8 8 THR D 94 VAL D 103 -1 O VAL D 103 N HIS D 3
SHEET 6 AA8 8 PHE D 109 TYR D 118 -1 O TYR D 113 N GLY D 100
SHEET 7 AA8 8 LYS D 121 LEU D 126 -1 O LEU D 126 N ARG D 114
SHEET 8 AA8 8 TRP D 133 ALA D 135 -1 O THR D 134 N ALA D 125
SHEET 1 AA9 4 LYS D 186 PRO D 193 0
SHEET 2 AA9 4 GLU D 198 PHE D 208 -1 O LEU D 206 N LYS D 186
SHEET 3 AA9 4 PHE D 241 PRO D 250 -1 O ALA D 245 N CYS D 203
SHEET 4 AA9 4 THR D 228 LEU D 230 -1 N GLU D 229 O ALA D 246
SHEET 1 AB1 4 LYS D 186 PRO D 193 0
SHEET 2 AB1 4 GLU D 198 PHE D 208 -1 O LEU D 206 N LYS D 186
SHEET 3 AB1 4 PHE D 241 PRO D 250 -1 O ALA D 245 N CYS D 203
SHEET 4 AB1 4 ARG D 234 PRO D 235 -1 N ARG D 234 O GLN D 242
SHEET 1 AB2 4 GLU D 222 ASP D 223 0
SHEET 2 AB2 4 THR D 214 ARG D 219 -1 N ARG D 219 O GLU D 222
SHEET 3 AB2 4 TYR D 257 GLN D 262 -1 O HIS D 260 N THR D 216
SHEET 4 AB2 4 THR D 271 ARG D 273 -1 O LEU D 272 N CYS D 259
SHEET 1 AB3 4 VAL E 9 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 VAL E 9 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 ARG E 81 N ASP E 38
SHEET 4 AB5 4 LYS E 91 LYS E 94 -1 O LYS E 91 N VAL E 82
SHEET 1 AB6 8 GLU G 46 PRO G 47 0
SHEET 2 AB6 8 THR G 31 ASP G 37 -1 N ARG G 35 O GLU G 46
SHEET 3 AB6 8 ARG G 21 VAL G 28 -1 N VAL G 28 O THR G 31
SHEET 4 AB6 8 HIS G 3 VAL G 12 -1 N ARG G 6 O TYR G 27
SHEET 5 AB6 8 THR G 94 VAL G 103 -1 O TYR G 99 N TYR G 7
SHEET 6 AB6 8 PHE G 109 TYR G 118 -1 O TYR G 113 N GLY G 100
SHEET 7 AB6 8 LYS G 121 LEU G 126 -1 O ILE G 124 N ASP G 116
SHEET 8 AB6 8 TRP G 133 ALA G 135 -1 O THR G 134 N ALA G 125
SHEET 1 AB7 4 HIS G 188 SER G 195 0
SHEET 2 AB7 4 GLU G 198 PHE G 208 -1 O THR G 200 N HIS G 192
SHEET 3 AB7 4 PHE G 241 PRO G 250 -1 O ALA G 245 N CYS G 203
SHEET 4 AB7 4 THR G 228 LEU G 230 -1 N GLU G 229 O ALA G 246
SHEET 1 AB8 4 HIS G 188 SER G 195 0
SHEET 2 AB8 4 GLU G 198 PHE G 208 -1 O THR G 200 N HIS G 192
SHEET 3 AB8 4 PHE G 241 PRO G 250 -1 O ALA G 245 N CYS G 203
SHEET 4 AB8 4 ARG G 234 PRO G 235 -1 N ARG G 234 O GLN G 242
SHEET 1 AB9 4 GLU G 222 ASP G 223 0
SHEET 2 AB9 4 THR G 214 ARG G 219 -1 N ARG G 219 O GLU G 222
SHEET 3 AB9 4 TYR G 257 GLN G 262 -1 O THR G 258 N GLN G 218
SHEET 4 AB9 4 LEU G 272 ARG G 273 -1 O LEU G 272 N CYS G 259
SHEET 1 AC1 4 VAL H 9 SER H 11 0
SHEET 2 AC1 4 ASN H 21 VAL H 27 -1 O ASN H 24 N TYR H 10
SHEET 3 AC1 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 AC1 4 GLU H 50 HIS H 51 -1 N GLU H 50 O TYR H 67
SHEET 1 AC2 4 VAL H 9 SER H 11 0
SHEET 2 AC2 4 ASN H 21 VAL H 27 -1 O ASN H 24 N TYR H 10
SHEET 3 AC2 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 AC2 4 SER H 55 PHE H 56 -1 N SER H 55 O TYR H 63
SHEET 1 AC3 4 GLU H 44 ARG H 45 0
SHEET 2 AC3 4 GLU H 36 LYS H 41 -1 N LYS H 41 O GLU H 44
SHEET 3 AC3 4 TYR H 78 ASN H 83 -1 O ALA H 79 N LEU H 40
SHEET 4 AC3 4 LYS H 91 LYS H 94 -1 O VAL H 93 N CYS H 80
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.44
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.72
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.50
SSBOND 4 CYS D 101 CYS D 164 1555 1555 2.55
SSBOND 5 CYS D 203 CYS D 259 1555 1555 2.78
SSBOND 6 CYS E 25 CYS E 80 1555 1555 2.71
SSBOND 7 CYS G 101 CYS G 164 1555 1555 2.63
SSBOND 8 CYS G 203 CYS G 259 1555 1555 2.83
SSBOND 9 CYS H 25 CYS H 80 1555 1555 2.68
CISPEP 1 TYR A 209 PRO A 210 0 1.46
CISPEP 2 HIS B 31 PRO B 32 0 -0.50
CISPEP 3 SER C 5 PRO C 6 0 9.23
CISPEP 4 TYR D 209 PRO D 210 0 5.19
CISPEP 5 HIS E 31 PRO E 32 0 -1.01
CISPEP 6 SER F 5 PRO F 6 0 11.78
CISPEP 7 TYR G 209 PRO G 210 0 -0.99
CISPEP 8 HIS H 31 PRO H 32 0 -1.60
CISPEP 9 SER I 5 PRO I 6 0 12.88
SITE 1 AC1 1 VAL C 8
SITE 1 AC2 2 GLN D 156 VAL F 8
SITE 1 AC3 3 ASN E 83 HIS E 84 LEU E 87
CRYST1 155.500 150.198 105.829 90.00 120.53 90.00 C 1 2 1 12
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 0.006431 0.000000 0.003793 0.00000
SCALE2 0.000000 0.006658 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010970 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
