HEADER IMMUNE SYSTEM 25-JUN-01 1JGE
TITLE HLA-B*2705 BOUND TO NONA-PEPTIDE M9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, B-27 B*2705 ALPHA
COMPND 3 CHAIN;
COMPND 4 CHAIN: A;
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: PEPTIDE M9;
COMPND 12 CHAIN: C;
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-B OR HLAB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
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 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS MHC (MAJOR HISTOCOMPATIBILITY COMPLEX), HLA (HUMAN LEUKOCYTE
KEYWDS 2 ANTIGEN), IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HULSMEYER,R.C.HILLIG,A.VOLZ,M.RUHL,W.SCHRODER,W.SAENGER,A.ZIEGLER,
AUTHOR 2 B.UCHANSKA-ZIEGLER
REVDAT 5 16-AUG-23 1JGE 1 SEQADV
REVDAT 4 24-FEB-09 1JGE 1 VERSN
REVDAT 3 12-AUG-03 1JGE 1 DBREF
REVDAT 2 23-DEC-02 1JGE 1 JRNL REMARK MASTER
REVDAT 1 30-OCT-02 1JGE 0
JRNL AUTH M.HULSMEYER,R.C.HILLIG,A.VOLZ,M.RUHL,W.SCHRODER,W.SAENGER,
JRNL AUTH 2 A.ZIEGLER,B.UCHANSKA-ZIEGLER
JRNL TITL HLA-B27 SUBTYPES DIFFERENTIALLY ASSOCIATED WITH DISEASE
JRNL TITL 2 EXHIBIT SUBTLE STRUCTURAL ALTERATIONS
JRNL REF J.BIOL.CHEM. V. 277 47844 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12244049
JRNL DOI 10.1074/JBC.M206392200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.R.MADDEN,J.C.GORGA,J.L.STROMINGER,D.C.WILEY
REMARK 1 TITL THE STRUCTURE OF HLA-B27 REVEALS NONAMER SELF-PEPTIDES BOUND
REMARK 1 TITL 2 IN AN EXTENDED CONFORMATION
REMARK 1 REF NATURE V. 353 321 1991
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/353321A0
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.R.MADDEN,J.C.GORGA,J.L.STROMINGER,D.C.WILEY
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 A
REMARK 1 TITL 2 RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE
REMARK 1 TITL 3 BINDING TO MHC
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 70 1035 1992
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/0092-8674(92)90252-8
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 26887
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1369
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3153
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 462
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : -1.50000
REMARK 3 B33 (A**2) : 1.71000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.014 ; 0.021
REMARK 3 ANGLE DISTANCE (A) : 1.426 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.766 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.282 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.263 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.507 ; 4.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JGE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.964
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26918
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 19.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.18200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1HSA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TRIS-HCL, NACL; PEG 400 AS
REMARK 280 CRYO PROTECTANT, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 25.65000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.65000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.60000
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETEROTRIMERIC COMPLEX
REMARK 300 CONSISTING OF ONE HLA-B*2705 (HEAVY) CHAIN, ONE BETA-2-
REMARK 300 MICROGLOBULIN (LIGHT) CHAIN AND ONE NONAMERIC MODEL PEPTIDE M9.
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: 4160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 30 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 14 72.00 -152.97
REMARK 500 ASP A 29 -127.31 55.20
REMARK 500 HIS A 114 112.95 -166.71
REMARK 500 SER A 131 -16.42 -143.89
REMARK 500 ARG A 239 -25.78 89.92
REMARK 500 TRP B 60 -11.30 77.95
REMARK 500 ARG B 97 -9.49 -58.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HSA RELATED DB: PDB
REMARK 900 HLA-B*2705 IN COMPLEX WITH AN ENDOGENOUS MIXTURE OF NONAMERIC
REMARK 900 PEPTIDES
REMARK 900 RELATED ID: 1JGD RELATED DB: PDB
REMARK 900 HLA-B*2709 IN COMPLEX WITH DECA-PEPTIDE S10
DBREF 1JGE A 1 276 UNP P03989 1B27_HUMAN 25 300
DBREF 1JGE B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 1JGE C 1 9 PDB 1JGE 1JGE 1 9
SEQADV 1JGE MET B 0 UNP P61769 CLONING ARTIFACT
SEQRES 1 A 276 GLY SER HIS SER MET ARG TYR PHE HIS THR SER VAL SER
SEQRES 2 A 276 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE THR VAL GLY
SEQRES 3 A 276 TYR VAL ASP ASP THR LEU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 276 ALA ALA SER PRO ARG GLU GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 276 GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG GLU THR GLN
SEQRES 6 A 276 ILE CYS LYS ALA LYS ALA GLN THR ASP ARG GLU ASP LEU
SEQRES 7 A 276 ARG THR LEU LEU ARG TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 276 SER HIS THR LEU GLN ASN MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 276 PRO ASP GLY ARG LEU LEU ARG GLY TYR HIS GLN ASP ALA
SEQRES 10 A 276 TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 A 276 SER SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR
SEQRES 12 A 276 GLN ARG LYS TRP GLU ALA ALA ARG VAL ALA GLU GLN LEU
SEQRES 13 A 276 ARG ALA TYR LEU GLU GLY GLU CYS VAL 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 ILE 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 ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 276 PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA 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 LYS PRO LEU THR LEU ARG
SEQRES 22 A 276 TRP GLU PRO
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 9 GLY ARG PHE ALA ALA ALA ILE ALA LYS
FORMUL 4 HOH *462(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 ALA A 150 1 12
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 THR A 225 THR A 228 5 4
HELIX 8 8 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 O ARG A 35 N GLU A 46
SHEET 3 A 8 ARG A 21 VAL A 28 -1 N THR A 24 O PHE A 36
SHEET 4 A 8 HIS A 3 VAL A 12 -1 O ARG A 6 N TYR A 27
SHEET 5 A 8 THR A 94 VAL A 103 -1 O LEU A 95 N SER A 11
SHEET 6 A 8 LEU A 109 TYR A 118 -1 N LEU A 110 O ASP A 102
SHEET 7 A 8 LYS A 121 LEU A 126 -1 O LYS A 121 N TYR A 118
SHEET 8 A 8 TRP A 133 ALA A 135 -1 N THR A 134 O 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 THR A 200 N HIS A 192
SHEET 3 B 4 PHE A 241 PRO A 250 -1 N PHE A 241 O PHE A 208
SHEET 4 B 4 GLU A 229 LEU 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 THR A 200 N HIS A 192
SHEET 3 C 4 PHE A 241 PRO A 250 -1 N PHE A 241 O PHE A 208
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 ASP A 223 0
SHEET 2 D 4 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222
SHEET 3 D 4 TYR A 257 GLN A 262 -1 O THR A 258 N GLN A 218
SHEET 4 D 4 LEU A 270 LEU A 272 -1 N LEU A 270 O VAL A 261
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 N ASN B 24 O TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 N PHE B 62 O PHE B 30
SHEET 4 E 4 GLU B 50 HIS B 51 -1 O GLU B 50 N 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 N ASN B 24 O TYR B 10
SHEET 3 F 4 PHE B 62 PHE B 70 -1 N PHE B 62 O PHE B 30
SHEET 4 F 4 SER B 55 PHE B 56 -1 O SER B 55 N TYR B 63
SHEET 1 G 4 GLU B 44 ARG 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 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.07
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.01
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.04
CISPEP 1 TYR A 209 PRO A 210 0 0.81
CISPEP 2 HIS B 31 PRO B 32 0 -1.06
CRYST1 51.300 83.200 110.400 90.00 90.00 90.00 P 21 21 21 4
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 0.019484 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012020 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009059 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
