HEADER IMMUNE SYSTEM 09-MAY-11 3RWI
TITLE RHESUS MACAQUE MHC CLASS I MOLECULE MAMU-B*17-GW10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 24-297;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: VIF GW10 PEPTIDE FROM VIRION INFECTIVITY FACTOR;
COMPND 12 CHAIN: C;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA;
SOURCE 3 ORGANISM_COMMON: RHESUS MACAQUE;
SOURCE 4 ORGANISM_TAXID: 9544;
SOURCE 5 GENE: MHCI-B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MACACA MULATTA;
SOURCE 10 ORGANISM_COMMON: RHESUS MACAQUE;
SOURCE 11 ORGANISM_TAXID: 9544;
SOURCE 12 GENE: B2M;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: SIMIAN IMMUNODEFICIENCY VIRUS;
SOURCE 18 ORGANISM_COMMON: SIV-CPZ;
SOURCE 19 ORGANISM_TAXID: 11723;
SOURCE 20 OTHER_DETAILS: SYNTHTIC PEPTIDE
KEYWDS ANTIGENIC PEPTIDES, T LYMPHOCYTES, IMMUNE RESPONSE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WU,F.GAO,J.LIU,J.X.QI,D.A.PRICE,G.F.GAO
REVDAT 1 21-MAR-12 3RWI 0
JRNL AUTH Y.WU,F.GAO,J.LIU,J.X.QI,E.GOSTICK,D.A.PRICE,G.F.GAO
JRNL TITL STRUCTURAL BASIS OF DIVERSE PEPTIDE ACCOMMODATION BY THE
JRNL TITL 2 RHESUS MACAQUE MHC CLASS I MOLECULE MAMU-B*17: INSIGHTS INTO
JRNL TITL 3 IMMUNE PROTECTION FROM SIMIAN IMMUNODEFICIENCY VIRUS
JRNL REF J.IMMUNOL. V. 187 6382 2011
JRNL REFN ISSN 0022-1767
JRNL PMID 22084443
JRNL DOI 10.4049/JIMMUNOL.1101726
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 32113
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1642
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 24.4007 - 4.3206 0.97 3175 191 0.1504 0.1570
REMARK 3 2 4.3206 - 3.4324 0.98 3169 153 0.1551 0.1790
REMARK 3 3 3.4324 - 2.9994 0.97 3119 146 0.1885 0.2361
REMARK 3 4 2.9994 - 2.7256 0.97 3071 187 0.1880 0.2464
REMARK 3 5 2.7256 - 2.5305 0.96 3033 164 0.1767 0.2067
REMARK 3 6 2.5305 - 2.3814 0.95 3045 156 0.1789 0.2236
REMARK 3 7 2.3814 - 2.2622 0.95 2962 189 0.1916 0.2526
REMARK 3 8 2.2622 - 2.1638 0.94 2973 159 0.1934 0.2706
REMARK 3 9 2.1638 - 2.0806 0.94 2985 156 0.1914 0.2451
REMARK 3 10 2.0806 - 2.0088 0.93 2939 141 0.2080 0.2757
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 52.17
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.60230
REMARK 3 B22 (A**2) : -0.77260
REMARK 3 B33 (A**2) : 0.17030
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.06330
REMARK 3 B23 (A**2) : 0.00000
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 : 0.010 3393
REMARK 3 ANGLE : 0.849 4432
REMARK 3 CHIRALITY : 0.062 434
REMARK 3 PLANARITY : 0.003 592
REMARK 3 DIHEDRAL : 12.926 1212
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5109 -0.1184 -20.6266
REMARK 3 T TENSOR
REMARK 3 T11: 0.0621 T22: 0.0692
REMARK 3 T33: 0.0304 T12: -0.0324
REMARK 3 T13: -0.0035 T23: 0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 1.0973 L22: 0.2416
REMARK 3 L33: 0.2059 L12: 0.0190
REMARK 3 L13: 0.2515 L23: -0.0805
REMARK 3 S TENSOR
REMARK 3 S11: -0.0538 S12: 0.2502 S13: 0.0975
REMARK 3 S21: 0.0031 S22: 0.0172 S23: 0.0197
REMARK 3 S31: -0.0283 S32: 0.0733 S33: 0.0347
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 3RWI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32167
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.009
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
REMARK 200 STARTING MODEL: 2BVO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 130 LIES ON A SPECIAL POSITION.
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 -123.93 49.14
REMARK 500 HIS A 114 99.57 -161.42
REMARK 500 GLN B 2 112.00 69.57
REMARK 500 TRP B 60 -4.68 79.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RWC RELATED DB: PDB
REMARK 900 RELATED ID: 3RWD RELATED DB: PDB
REMARK 900 RELATED ID: 3RWE RELATED DB: PDB
REMARK 900 RELATED ID: 3RWF RELATED DB: PDB
REMARK 900 RELATED ID: 3RWG RELATED DB: PDB
REMARK 900 RELATED ID: 3RWH RELATED DB: PDB
REMARK 900 RELATED ID: 3RWJ RELATED DB: PDB
DBREF 3RWI A 1 276 UNP Q9GJ77 Q9GJ77_MACMU 24 299
DBREF 3RWI B 1 99 UNP Q6V7J5 B2MG_MACMU 21 119
DBREF 3RWI C 1 10 UNP Q89490 Q89490_SIVCZ 372 381
SEQRES 1 A 276 GLY SER HIS SER MET LYS TYR PHE TYR THR SER VAL SER
SEQRES 2 A 276 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE SER VAL GLY
SEQRES 3 A 276 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 276 ALA GLU SER PRO ARG GLU GLU PRO ARG ALA PRO TRP VAL
SEQRES 5 A 276 GLU GLN GLU GLY PRO GLU TYR TRP GLU GLU ALA THR ARG
SEQRES 6 A 276 ARG ALA LYS GLU ALA ALA GLN THR HIS ARG GLU ASN LEU
SEQRES 7 A 276 ARG THR ALA LEU ARG TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 276 SER HIS THR ILE GLN LYS MET TYR GLY CYS ASP LEU GLY
SEQRES 9 A 276 PRO ASP GLY ARG LEU LEU ARG GLY TYR HIS GLN SER ALA
SEQRES 10 A 276 TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLY ASP LEU
SEQRES 11 A 276 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ASN THR
SEQRES 12 A 276 GLN ARG LYS TRP GLU GLY ASN ARG TYR ALA GLU ARG PHE
SEQRES 13 A 276 ARG ALA TYR LEU GLU GLY GLU CYS LEU GLU TRP LEU ARG
SEQRES 14 A 276 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG ALA
SEQRES 15 A 276 ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO VAL SER
SEQRES 16 A 276 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 276 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 276 GLU GLU GLN THR GLN ASP THR GLU PHE VAL GLU THR ARG
SEQRES 19 A 276 PRO GLY GLY ASP GLY THR PHE GLN LYS TRP GLY ALA VAL
SEQRES 20 A 276 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 276 VAL GLN HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 A 276 TRP GLU PRO
SEQRES 1 B 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO PRO GLU ASN GLY LYS PRO 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 LYS MET GLY 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 ASN GLU LYS ASP GLU TYR
SEQRES 7 B 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLY PRO ARG
SEQRES 8 B 99 THR VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 10 GLY SER HIS LEU GLU VAL GLN GLY TYR TRP
FORMUL 4 HOH *445(H2 O)
HELIX 1 1 ALA A 49 GLN A 54 1 6
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 ASP A 137 ASN A 150 1 14
HELIX 4 4 ARG A 151 GLY A 162 1 12
HELIX 5 5 GLY A 162 GLY A 175 1 14
HELIX 6 6 GLY A 175 GLN A 180 1 6
HELIX 7 7 GLU A 253 GLN A 255 5 3
SHEET 1 A 8 GLU A 46 PRO A 47 0
SHEET 2 A 8 THR 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 SER A 24 O PHE A 36
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N LYS A 6 O TYR A 27
SHEET 5 A 8 THR A 94 LEU A 103 -1 O LYS A 97 N TYR A 9
SHEET 6 A 8 LEU A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 A 8 LYS A 121 LEU A 126 -1 O TYR A 123 N SER 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 LYS A 186 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 GLY A 245 N CYS A 203
SHEET 4 B 4 THR A 228 PHE A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 C 4 LYS A 186 PRO A 193 0
SHEET 2 C 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 C 4 PHE A 241 PRO A 250 -1 O GLY A 245 N CYS A 203
SHEET 4 C 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 D 4 GLU A 222 GLN A 224 0
SHEET 2 D 4 THR A 214 ARG A 219 -1 N TRP A 217 O GLN A 224
SHEET 3 D 4 TYR A 257 GLN A 262 -1 O HIS A 260 N THR A 216
SHEET 4 D 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 E 4 LYS 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 THR B 68 N LEU B 23
SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 F 4 LYS B 6 SER B 11 0
SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 F 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23
SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 G 4 GLU B 44 LYS B 45 0
SHEET 2 G 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 G 4 ARG B 91 LYS B 94 -1 O ARG B 91 N VAL B 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.04
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.03
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
CISPEP 1 TYR A 209 PRO A 210 0 2.40
CISPEP 2 HIS B 31 PRO B 32 0 -0.04
CRYST1 68.456 45.051 82.057 90.00 95.99 90.00 P 1 2 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 0.014608 0.000000 0.001533 0.00000
SCALE2 0.000000 0.022197 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012254 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
