HEADER IMMUNE SYSTEM 16-JUN-13 4L8C
TITLE CRYSTAL STRUCTURE OF THE H2DB IN COMPLEX WITH THE NP-N3D PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-B ALPHA CHAIN;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: UNP RESIDUES 25-304;
COMPND 5 SYNONYM: HEAVY CHAIN H2DB, H-2D(B);
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 FRAGMENT: UNP RESIDUES 21-119;
COMPND 11 SYNONYM: B2M;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: NP-N3D PEPTIDE;
COMPND 15 CHAIN: I, J, K, L;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: H2-D1;
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: PET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: B2M;
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: PET;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES
KEYWDS INFLUENZA, VIRAL ESCAPE, T CELL IMMUNITY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ROSSJOHN,S.GRAS
REVDAT 4 20-SEP-23 4L8C 1 REMARK
REVDAT 3 15-NOV-17 4L8C 1 REMARK
REVDAT 2 04-DEC-13 4L8C 1 JRNL
REVDAT 1 16-OCT-13 4L8C 0
JRNL AUTH S.A.VALKENBURG,S.QUINONES-PARRA,S.GRAS,N.KOMADINA,
JRNL AUTH 2 J.MCVERNON,Z.WANG,H.HALIM,P.IANNELLO,C.COLE,K.LAURIE,
JRNL AUTH 3 A.KELSO,J.ROSSJOHN,P.C.DOHERTY,S.J.TURNER,K.KEDZIERSKA
JRNL TITL ACUTE EMERGENCE AND REVERSION OF INFLUENZA A VIRUS
JRNL TITL 2 QUASISPECIES WITHIN CD8(+) T CELL ANTIGENIC PEPTIDES.
JRNL REF NAT COMMUN V. 4 2663 2013
JRNL REFN ESSN 2041-1723
JRNL PMID 24173108
JRNL DOI 10.1038/NCOMMS3663
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 47090
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2382
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3457
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2410
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3274
REMARK 3 BIN R VALUE (WORKING SET) : 0.2369
REMARK 3 BIN FREE R VALUE : 0.3144
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.29
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 183
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 : 12517
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 95
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 76.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.86510
REMARK 3 B22 (A**2) : 6.27870
REMARK 3 B33 (A**2) : -10.14380
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.29390
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.337
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.362
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 : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12913 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17526 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4428 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 357 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1841 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12913 ; 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 : 1573 ; 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 : 13681 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.19
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.88
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 23.11
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 4L8C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-12
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 : MX2
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 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.12, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47116
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 138.505
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.60400
REMARK 200 R SYM FOR SHELL (I) : 0.60400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 4HUU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, PH 8.5, 0.2 M LITHIUM
REMARK 280 SULFATE, 25-30% PEG8000, 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 42.73200
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 4390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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: 4170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J
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: 4220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, K
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: 4
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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, L
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 PRO A 276
REMARK 465 PRO A 277
REMARK 465 PRO A 278
REMARK 465 SER A 279
REMARK 465 THR A 280
REMARK 465 ILE B 1
REMARK 465 GLN B 2
REMARK 465 PRO C 276
REMARK 465 PRO C 277
REMARK 465 PRO C 278
REMARK 465 SER C 279
REMARK 465 THR C 280
REMARK 465 ILE D 1
REMARK 465 GLN D 2
REMARK 465 PRO E 276
REMARK 465 PRO E 277
REMARK 465 PRO E 278
REMARK 465 SER E 279
REMARK 465 THR E 280
REMARK 465 ILE F 1
REMARK 465 PRO G 276
REMARK 465 PRO G 277
REMARK 465 PRO G 278
REMARK 465 SER G 279
REMARK 465 THR G 280
REMARK 465 ILE H 1
REMARK 465 GLN H 2
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 ASN A 42 79.38 70.35
REMARK 500 TRP A 51 1.09 -68.79
REMARK 500 GLN A 54 43.16 -69.88
REMARK 500 PRO A 57 -8.50 -55.80
REMARK 500 LEU A 110 -60.34 -99.92
REMARK 500 TYR A 123 -61.10 -121.50
REMARK 500 LEU A 224 73.02 -102.70
REMARK 500 LYS A 243 147.23 -175.91
REMARK 500 HIS A 263 135.19 -170.39
REMARK 500 GLU A 268 154.81 164.35
REMARK 500 TRP B 60 -9.94 72.65
REMARK 500 ARG C 35 137.04 -171.56
REMARK 500 GLN C 54 21.68 -71.42
REMARK 500 GLU C 128 -37.57 -33.93
REMARK 500 ASN C 176 -65.15 -28.56
REMARK 500 ASN C 220 -58.91 66.33
REMARK 500 GLU C 268 135.97 -174.49
REMARK 500 ASN D 21 -163.40 -161.21
REMARK 500 LYS D 48 84.32 66.67
REMARK 500 TRP D 60 -13.63 76.08
REMARK 500 SER E 105 -38.69 63.44
REMARK 500 TRP E 107 16.44 96.69
REMARK 500 PRO E 193 -70.78 -24.67
REMARK 500 ARG E 194 -54.19 77.13
REMARK 500 SER E 195 178.08 63.80
REMARK 500 ASN E 220 7.97 52.31
REMARK 500 ASP E 238 32.25 -91.83
REMARK 500 PRO E 267 32.10 -80.30
REMARK 500 GLU E 268 146.46 135.27
REMARK 500 HIS F 31 129.43 -170.37
REMARK 500 LYS F 45 123.78 -38.41
REMARK 500 TRP F 60 -7.03 87.86
REMARK 500 TRP G 60 -3.33 -57.93
REMARK 500 LEU G 110 -60.30 -90.49
REMARK 500 TYR G 123 -69.33 -128.50
REMARK 500 SER G 150 3.97 -65.08
REMARK 500 ASN G 176 -49.95 -6.99
REMARK 500 ASP G 227 74.26 44.27
REMARK 500 LYS G 253 5.16 -64.28
REMARK 500 GLU G 268 142.18 84.81
REMARK 500 ARG G 273 -17.91 -144.29
REMARK 500 TRP G 274 144.11 -0.36
REMARK 500 ASN H 21 -168.07 -128.62
REMARK 500 TRP H 60 -8.22 77.39
REMARK 500 MET I 6 -95.87 -80.70
REMARK 500 GLU J 7 129.34 67.91
REMARK 500 MET K 6 -103.48 -90.23
REMARK 500 MET L 6 -105.19 -77.58
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HUU RELATED DB: PDB
REMARK 900 RELATED ID: 4HUV RELATED DB: PDB
REMARK 900 RELATED ID: 4HUW RELATED DB: PDB
REMARK 900 RELATED ID: 4HUX RELATED DB: PDB
REMARK 900 RELATED ID: 4HV8 RELATED DB: PDB
REMARK 900 RELATED ID: 4L8B RELATED DB: PDB
REMARK 900 RELATED ID: 4L8D RELATED DB: PDB
DBREF 4L8C A 1 280 UNP P01899 HA11_MOUSE 25 304
DBREF 4L8C B 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 4L8C C 1 280 UNP P01899 HA11_MOUSE 25 304
DBREF 4L8C D 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 4L8C E 1 280 UNP P01899 HA11_MOUSE 25 304
DBREF 4L8C F 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 4L8C G 1 280 UNP P01899 HA11_MOUSE 25 304
DBREF 4L8C H 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 4L8C I 1 9 PDB 4L8C 4L8C 1 9
DBREF 4L8C J 1 9 PDB 4L8C 4L8C 1 9
DBREF 4L8C K 1 9 PDB 4L8C 4L8C 1 9
DBREF 4L8C L 1 9 PDB 4L8C 4L8C 1 9
SEQRES 1 A 280 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 A 280 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 A 280 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 A 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 A 280 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 A 280 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 A 280 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 A 280 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 A 280 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 A 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 A 280 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 A 280 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 A 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 A 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 A 280 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 A 280 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 A 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 A 280 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 A 280 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 A 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 B 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 B 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 B 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 B 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 B 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 B 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS
SEQRES 8 B 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 C 280 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 C 280 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 C 280 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 C 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 C 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 C 280 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 C 280 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 C 280 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 C 280 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 C 280 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 C 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 C 280 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 C 280 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 C 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 C 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 C 280 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 C 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 C 280 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 C 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 C 280 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 C 280 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 C 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 D 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 D 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 D 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 D 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 D 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 D 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 D 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS
SEQRES 8 D 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 E 280 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 E 280 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 E 280 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 E 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 E 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 E 280 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 E 280 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 E 280 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 E 280 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 E 280 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 E 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 E 280 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 E 280 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 E 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 E 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 E 280 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 E 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 E 280 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 E 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 E 280 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 E 280 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 E 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 F 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 F 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 F 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 F 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 F 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 F 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 F 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS
SEQRES 8 F 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 G 280 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 G 280 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 G 280 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 G 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 G 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 G 280 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 G 280 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 G 280 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 G 280 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 G 280 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 G 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 G 280 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 G 280 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 G 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 G 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 G 280 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 G 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 G 280 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 G 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 G 280 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 G 280 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 G 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 H 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 H 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 H 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 H 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 H 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 H 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 H 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS
SEQRES 8 H 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 I 9 ALA SER ASP GLU ASN MET GLU THR MET
SEQRES 1 J 9 ALA SER ASP GLU ASN MET GLU THR MET
SEQRES 1 K 9 ALA SER ASP GLU ASN MET GLU THR MET
SEQRES 1 L 9 ALA SER ASP GLU ASN MET GLU THR MET
HET SO4 A 301 5
HET SO4 C 301 5
HET SO4 C 302 5
HET SO4 E 301 5
HET SO4 E 302 5
HETNAM SO4 SULFATE ION
FORMUL 13 SO4 5(O4 S 2-)
FORMUL 18 HOH *95(H2 O)
HELIX 1 1 ALA A 49 GLU A 53 5 5
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 ALA A 139 SER A 150 1 12
HELIX 4 4 GLY A 151 GLY A 162 1 12
HELIX 5 5 GLY A 162 GLY A 175 1 14
HELIX 6 6 GLY A 175 LEU A 180 1 6
HELIX 7 7 GLY A 252 GLN A 255 5 4
HELIX 8 8 ALA C 49 GLU C 55 5 7
HELIX 9 9 GLY C 56 TYR C 85 1 30
HELIX 10 10 ALA C 139 SER C 150 1 12
HELIX 11 11 GLY C 151 GLY C 162 1 12
HELIX 12 12 GLY C 162 GLY C 175 1 14
HELIX 13 13 GLY C 175 LEU C 180 1 6
HELIX 14 14 LYS C 253 GLN C 255 5 3
HELIX 15 15 ALA E 49 GLU E 53 5 5
HELIX 16 16 GLY E 56 TYR E 85 1 30
HELIX 17 17 ASP E 137 GLY E 151 1 15
HELIX 18 18 GLY E 151 GLY E 162 1 12
HELIX 19 19 GLY E 162 GLY E 175 1 14
HELIX 20 20 GLY E 175 ARG E 181 1 7
HELIX 21 21 ALA G 49 GLU G 53 5 5
HELIX 22 22 GLU G 58 TYR G 85 1 28
HELIX 23 23 ALA G 140 SER G 150 1 11
HELIX 24 24 GLY G 151 GLY G 162 1 12
HELIX 25 25 GLY G 162 ASN G 176 1 15
HELIX 26 26 GLY G 252 GLN G 255 5 4
SHEET 1 A 8 GLU A 46 PRO A 47 0
SHEET 2 A 8 LYS A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 A 8 ARG A 21 VAL A 28 -1 N GLY A 26 O VAL A 34
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N PHE A 8 O VAL A 25
SHEET 5 A 8 THR A 94 LEU A 103 -1 O LEU A 103 N HIS A 3
SHEET 6 A 8 LEU A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 A 8 ARG A 121 LEU A 126 -1 O ILE A 124 N PHE A 116
SHEET 8 A 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 B 4 HIS A 188 PRO A 193 0
SHEET 2 B 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 B 4 PHE A 241 PRO A 250 -1 O VAL A 249 N VAL A 199
SHEET 4 B 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 C 4 GLU A 222 GLU A 223 0
SHEET 2 C 4 THR A 214 LEU A 219 -1 N LEU A 219 O GLU A 222
SHEET 3 C 4 TYR A 257 TYR A 262 -1 O THR A 258 N GLN A 218
SHEET 4 C 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 D 4 GLN B 6 SER B 11 0
SHEET 2 D 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 D 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25
SHEET 4 D 4 GLU B 50 MET B 51 -1 N GLU B 50 O HIS B 67
SHEET 1 E 4 GLN B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25
SHEET 4 E 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 F 4 LYS B 44 LYS B 45 0
SHEET 2 F 4 ILE B 35 LYS B 41 -1 N LYS B 41 O LYS B 44
SHEET 3 F 4 TYR B 78 HIS B 84 -1 O ARG B 81 N GLN B 38
SHEET 4 F 4 LYS B 91 TYR B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 G 8 GLU C 46 PRO C 47 0
SHEET 2 G 8 LYS C 31 ASP C 37 -1 N ARG C 35 O GLU C 46
SHEET 3 G 8 ARG C 21 VAL C 28 -1 N SER C 24 O PHE C 36
SHEET 4 G 8 HIS C 3 VAL C 12 -1 N PHE C 8 O VAL C 25
SHEET 5 G 8 THR C 94 LEU C 103 -1 O GLN C 97 N GLU C 9
SHEET 6 G 8 LEU C 109 TYR C 118 -1 O ALA C 117 N GLN C 96
SHEET 7 G 8 ARG C 121 LEU C 126 -1 O TYR C 123 N PHE C 116
SHEET 8 G 8 TRP C 133 ALA C 135 -1 O THR C 134 N ALA C 125
SHEET 1 H 4 LYS C 186 ARG C 194 0
SHEET 2 H 4 GLU C 198 PHE C 208 -1 O THR C 200 N HIS C 192
SHEET 3 H 4 PHE C 241 PRO C 250 -1 O ALA C 245 N CYS C 203
SHEET 4 H 4 MET C 228 LEU C 230 -1 N GLU C 229 O SER C 246
SHEET 1 I 4 LYS C 186 ARG C 194 0
SHEET 2 I 4 GLU C 198 PHE C 208 -1 O THR C 200 N HIS C 192
SHEET 3 I 4 PHE C 241 PRO C 250 -1 O ALA C 245 N CYS C 203
SHEET 4 I 4 ARG C 234 PRO C 235 -1 N ARG C 234 O GLN C 242
SHEET 1 J 4 GLU C 222 GLU C 223 0
SHEET 2 J 4 THR C 214 LEU C 219 -1 N LEU C 219 O GLU C 222
SHEET 3 J 4 TYR C 257 TYR C 262 -1 O TYR C 262 N THR C 214
SHEET 4 J 4 LEU C 270 LEU C 272 -1 O LEU C 272 N CYS C 259
SHEET 1 K 4 GLN D 6 SER D 11 0
SHEET 2 K 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 K 4 PHE D 62 PHE D 70 -1 O ALA D 66 N CYS D 25
SHEET 4 K 4 GLU D 50 MET D 51 -1 N GLU D 50 O HIS D 67
SHEET 1 L 4 GLN D 6 SER D 11 0
SHEET 2 L 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 L 4 PHE D 62 PHE D 70 -1 O ALA D 66 N CYS D 25
SHEET 4 L 4 SER D 55 PHE D 56 -1 N SER D 55 O TYR D 63
SHEET 1 M 4 LYS D 44 LYS D 45 0
SHEET 2 M 4 GLU D 36 LYS D 41 -1 N LYS D 41 O LYS D 44
SHEET 3 M 4 TYR D 78 LYS D 83 -1 O ARG D 81 N GLN D 38
SHEET 4 M 4 LYS D 91 TYR D 94 -1 O VAL D 93 N CYS D 80
SHEET 1 N 8 GLU E 46 PRO E 47 0
SHEET 2 N 8 LYS E 31 ASP E 37 -1 N ARG E 35 O GLU E 46
SHEET 3 N 8 ARG E 21 VAL E 28 -1 N VAL E 28 O LYS E 31
SHEET 4 N 8 HIS E 3 VAL E 12 -1 N PHE E 8 O VAL E 25
SHEET 5 N 8 THR E 94 LEU E 103 -1 O LEU E 103 N HIS E 3
SHEET 6 N 8 LEU E 109 TYR E 118 -1 O ALA E 117 N GLN E 96
SHEET 7 N 8 ARG E 121 LEU E 126 -1 O LEU E 126 N LEU E 114
SHEET 8 N 8 TRP E 133 ALA E 135 -1 O THR E 134 N ALA E 125
SHEET 1 O 4 LYS E 186 HIS E 192 0
SHEET 2 O 4 GLU E 198 PHE E 208 -1 O TRP E 204 N HIS E 188
SHEET 3 O 4 PHE E 241 PRO E 250 -1 O ALA E 245 N CYS E 203
SHEET 4 O 4 MET E 228 LEU E 230 -1 N GLU E 229 O SER E 246
SHEET 1 P 4 LYS E 186 HIS E 192 0
SHEET 2 P 4 GLU E 198 PHE E 208 -1 O TRP E 204 N HIS E 188
SHEET 3 P 4 PHE E 241 PRO E 250 -1 O ALA E 245 N CYS E 203
SHEET 4 P 4 ARG E 234 PRO E 235 -1 N ARG E 234 O GLN E 242
SHEET 1 Q 4 GLU E 222 GLU E 223 0
SHEET 2 Q 4 THR E 214 LEU E 219 -1 N LEU E 219 O GLU E 222
SHEET 3 Q 4 TYR E 257 TYR E 262 -1 O THR E 258 N GLN E 218
SHEET 4 Q 4 LEU E 270 LEU E 272 -1 O LEU E 272 N CYS E 259
SHEET 1 R 4 GLN F 6 SER F 11 0
SHEET 2 R 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 R 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 R 4 GLU F 50 MET F 51 -1 N GLU F 50 O HIS F 67
SHEET 1 S 4 GLN F 6 SER F 11 0
SHEET 2 S 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 S 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 S 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 T 4 LYS F 44 LYS F 45 0
SHEET 2 T 4 GLU F 36 LYS F 41 -1 N LYS F 41 O LYS F 44
SHEET 3 T 4 TYR F 78 LYS F 83 -1 O ARG F 81 N GLN F 38
SHEET 4 T 4 LYS F 91 TYR F 94 -1 O VAL F 93 N CYS F 80
SHEET 1 U 8 GLU G 46 PRO G 47 0
SHEET 2 U 8 LYS G 31 ASP G 37 -1 N ARG G 35 O GLU G 46
SHEET 3 U 8 ARG G 21 VAL G 28 -1 N GLY G 26 O PHE G 33
SHEET 4 U 8 HIS G 3 SER G 13 -1 N ARG G 6 O TYR G 27
SHEET 5 U 8 HIS G 93 LEU G 103 -1 O LEU G 103 N HIS G 3
SHEET 6 U 8 LEU G 109 TYR G 118 -1 O ARG G 111 N ASP G 102
SHEET 7 U 8 ARG G 121 LEU G 126 -1 O ILE G 124 N PHE G 116
SHEET 8 U 8 TRP G 133 ALA G 135 -1 O THR G 134 N ALA G 125
SHEET 1 V 4 LYS G 186 PRO G 193 0
SHEET 2 V 4 GLU G 198 PHE G 208 -1 O THR G 200 N HIS G 192
SHEET 3 V 4 PHE G 241 PRO G 250 -1 O LYS G 243 N ALA G 205
SHEET 4 V 4 GLU G 229 LEU G 230 -1 N GLU G 229 O SER G 246
SHEET 1 W 4 LYS G 186 PRO G 193 0
SHEET 2 W 4 GLU G 198 PHE G 208 -1 O THR G 200 N HIS G 192
SHEET 3 W 4 PHE G 241 PRO G 250 -1 O LYS G 243 N ALA G 205
SHEET 4 W 4 ARG G 234 PRO G 235 -1 N ARG G 234 O GLN G 242
SHEET 1 X 4 GLU G 222 GLU G 223 0
SHEET 2 X 4 THR G 214 LEU G 219 -1 N LEU G 219 O GLU G 222
SHEET 3 X 4 TYR G 257 TYR G 262 -1 O THR G 258 N GLN G 218
SHEET 4 X 4 LEU G 270 LEU G 272 -1 O LEU G 272 N CYS G 259
SHEET 1 Y 4 GLN H 6 SER H 11 0
SHEET 2 Y 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 Y 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 Y 4 GLU H 50 MET H 51 -1 N GLU H 50 O HIS H 67
SHEET 1 Z 4 GLN H 6 SER H 11 0
SHEET 2 Z 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 Z 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 Z 4 SER H 55 PHE H 56 -1 N SER H 55 O TYR H 63
SHEET 1 AA 4 LYS H 44 LYS H 45 0
SHEET 2 AA 4 GLU H 36 LYS H 41 -1 N LYS H 41 O LYS H 44
SHEET 3 AA 4 TYR H 78 LYS H 83 -1 O ARG H 81 N GLN H 38
SHEET 4 AA 4 LYS H 91 TYR H 94 -1 O LYS H 91 N VAL H 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.81
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.47
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.45
SSBOND 4 CYS C 101 CYS C 164 1555 1555 2.75
SSBOND 5 CYS C 203 CYS C 259 1555 1555 2.37
SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.29
SSBOND 7 CYS E 101 CYS E 164 1555 1555 2.62
SSBOND 8 CYS E 203 CYS E 259 1555 1555 2.43
SSBOND 9 CYS F 25 CYS F 80 1555 1555 2.41
SSBOND 10 CYS G 101 CYS G 164 1555 1555 2.75
SSBOND 11 CYS G 203 CYS G 259 1555 1555 2.58
SSBOND 12 CYS H 25 CYS H 80 1555 1555 2.52
CISPEP 1 TYR A 209 PRO A 210 0 -2.28
CISPEP 2 HIS B 31 PRO B 32 0 2.34
CISPEP 3 TYR C 209 PRO C 210 0 2.68
CISPEP 4 HIS D 31 PRO D 32 0 3.97
CISPEP 5 TYR E 209 PRO E 210 0 -2.21
CISPEP 6 HIS F 31 PRO F 32 0 5.07
CISPEP 7 TYR G 209 PRO G 210 0 6.02
CISPEP 8 HIS H 31 PRO H 32 0 4.03
SITE 1 AC1 3 ARG A 111 TYR A 113 LYS B 58
SITE 1 AC2 2 GLN C 87 GLN G 87
SITE 1 AC3 3 ARG C 111 TYR C 113 LYS D 58
SITE 1 AC4 1 GLN E 87
SITE 1 AC5 2 ARG E 111 TYR E 113
CRYST1 81.567 85.464 138.506 90.00 90.18 90.00 P 1 21 1 8
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 0.012260 0.000000 0.000039 0.00000
SCALE2 0.000000 0.011701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007220 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
