HEADER IMMUNE SYSTEM 30-JUL-14 4U6X
TITLE CRYSTAL STRUCTURE OF HLA-A*0201 IN COMPLEX WITH ALQDA, A 15 MER SELF-
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 25-300;
COMPND 5 SYNONYM: MHC CLASS I ANTIGEN A*2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: ALQDA PEPTIDE, ALQDAGDSSRKEYFI;
COMPND 13 CHAIN: P;
COMPND 14 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: PET;
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: PET;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 24 ORGANISM_TAXID: 32630;
SOURCE 25 OTHER_DETAILS: GL BIOCHEM
KEYWDS HLA A*0201, LIGANDOME, TCR, T CELL, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GRAS,E.CHABROL,J.ROSSJOHN
REVDAT 5 27-SEP-23 4U6X 1 REMARK LINK
REVDAT 4 22-NOV-17 4U6X 1 SOURCE JRNL REMARK
REVDAT 3 11-FEB-15 4U6X 1 JRNL
REVDAT 2 31-DEC-14 4U6X 1 JRNL
REVDAT 1 24-DEC-14 4U6X 0
JRNL AUTH C.HASSAN,E.CHABROL,L.JAHN,M.G.KESTER,A.H.DE RU,
JRNL AUTH 2 J.W.DRIJFHOUT,J.ROSSJOHN,J.H.FALKENBURG,M.H.HEEMSKERK,
JRNL AUTH 3 S.GRAS,P.A.VAN VEELEN
JRNL TITL NATURALLY PROCESSED NON-CANONICAL HLA-A*02:01 PRESENTED
JRNL TITL 2 PEPTIDES.
JRNL REF J.BIOL.CHEM. V. 290 2593 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 25505266
JRNL DOI 10.1074/JBC.M114.607028
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 46425
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2346
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 39.5425 - 4.3122 1.00 2661 127 0.1527 0.1792
REMARK 3 2 4.3122 - 3.4234 1.00 2632 128 0.1317 0.1565
REMARK 3 3 3.4234 - 2.9908 1.00 2628 134 0.1509 0.1642
REMARK 3 4 2.9908 - 2.7174 1.00 2590 151 0.1635 0.2190
REMARK 3 5 2.7174 - 2.5227 1.00 2623 127 0.1707 0.2013
REMARK 3 6 2.5227 - 2.3740 1.00 2593 143 0.1721 0.2355
REMARK 3 7 2.3740 - 2.2551 1.00 2601 138 0.1679 0.2093
REMARK 3 8 2.2551 - 2.1569 1.00 2570 156 0.1586 0.1839
REMARK 3 9 2.1569 - 2.0739 1.00 2593 129 0.1610 0.2298
REMARK 3 10 2.0739 - 2.0023 1.00 2587 147 0.1681 0.1951
REMARK 3 11 2.0023 - 1.9397 1.00 2592 135 0.1779 0.2250
REMARK 3 12 1.9397 - 1.8843 1.00 2564 140 0.1841 0.2212
REMARK 3 13 1.8843 - 1.8347 1.00 2587 138 0.1931 0.2285
REMARK 3 14 1.8347 - 1.7899 1.00 2618 142 0.2020 0.2670
REMARK 3 15 1.7899 - 1.7492 1.00 2558 138 0.2134 0.2879
REMARK 3 16 1.7492 - 1.7120 1.00 2540 136 0.2233 0.2897
REMARK 3 17 1.7120 - 1.6800 0.96 2542 137 0.2280 0.2785
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3592
REMARK 3 ANGLE : 1.085 4906
REMARK 3 CHIRALITY : 0.082 494
REMARK 3 PLANARITY : 0.004 660
REMARK 3 DIHEDRAL : 14.097 1353
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4U6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202921.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46457
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 51.218
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.69500
REMARK 200 R SYM FOR SHELL (I) : 0.69500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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 (%): 45.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-22.5% PEG 3350, HEPES PH 7.5, 0.1M
REMARK 280 MGCL2, EVAPORATION, TEMPERATURE 277K
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 39.53150
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: 5640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P
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 GLU A 275
REMARK 465 PRO A 276
REMARK 465 GLY P 6
REMARK 465 ASP P 7
REMARK 465 SER P 8
REMARK 465 SER P 9
REMARK 465 ARG P 10
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 OE1 GLU A 232 O HOH A 558 2.02
REMARK 500 NZ LYS A 68 O HOH A 401 2.03
REMARK 500 O HOH A 480 O HOH A 518 2.05
REMARK 500 O HOH A 403 O HOH A 485 2.06
REMARK 500 O HOH A 402 O HOH A 492 2.09
REMARK 500 O HOH B 215 O HOH B 264 2.09
REMARK 500 O HOH A 402 O HOH A 440 2.10
REMARK 500 OE1 GLN A 180 O HOH A 402 2.12
REMARK 500 O HOH B 201 O HOH B 216 2.12
REMARK 500 O HOH A 622 O HOH B 237 2.15
REMARK 500 O HOH B 211 O HOH B 217 2.15
REMARK 500 O LEU B 87 O HOH B 238 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 425 O HOH A 496 1655 2.02
REMARK 500 O HOH A 474 O HOH B 216 1455 2.17
REMARK 500 O HOH A 431 O HOH A 496 1655 2.18
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 17 134.71 -172.49
REMARK 500 ASP A 29 -127.20 50.96
REMARK 500 HIS A 114 108.47 -161.08
REMARK 500 HIS A 114 106.41 -161.08
REMARK 500 SER A 195 -177.13 -176.19
REMARK 500 LYS B 48 41.18 -97.54
REMARK 500 TRP B 60 -0.46 76.26
REMARK 500 ASP P 4 75.16 -105.04
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 CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG P 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4U6Y RELATED DB: PDB
DBREF 4U6X A 1 276 UNP P01892 1A02_HUMAN 25 300
DBREF 4U6X B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 4U6X P 1 15 PDB 4U6X 4U6X 1 15
SEQADV 4U6X MET B 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 276 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 276 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 276 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 276 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 276 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 276 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 276 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 276 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 276 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 276 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 276 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 276 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 A 276 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 276 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 276 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 276 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER 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 GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 276 VAL VAL PRO SER GLY GLN 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 P 15 ALA LEU GLN ASP ALA GLY ASP SER SER ARG LYS GLU TYR
SEQRES 2 P 15 PHE ILE
HET CL A 301 1
HET PEG A 302 17
HET PEG A 303 17
HET PEG A 304 17
HET CL A 305 1
HET CL A 306 1
HET MG B 101 1
HET CL B 102 1
HET MG P 101 1
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM MG MAGNESIUM ION
FORMUL 4 CL 4(CL 1-)
FORMUL 5 PEG 3(C4 H10 O3)
FORMUL 10 MG 2(MG 2+)
FORMUL 13 HOH *359(H2 O)
HELIX 1 AA1 ALA A 49 GLU A 55 5 7
HELIX 2 AA2 GLY A 56 TYR A 85 1 30
HELIX 3 AA3 ASP A 137 ALA A 150 1 14
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 GLN A 253 GLN A 255 5 3
SHEET 1 AA1 8 GLU A 46 PRO A 47 0
SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 AA1 8 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 PHE A 8 O VAL A 25
SHEET 5 AA1 8 THR A 94 VAL A 103 -1 O ARG A 97 N PHE A 9
SHEET 6 AA1 8 PHE A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 AA1 8 LYS A 121 LEU A 126 -1 O ILE A 124 N TYR 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 ALA A 193 0
SHEET 2 AA2 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA2 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
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 ALA A 193 0
SHEET 2 AA3 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA3 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
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 ASP A 223 0
SHEET 2 AA4 4 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222
SHEET 3 AA4 4 TYR A 257 GLN A 262 -1 O HIS A 260 N THR A 216
SHEET 4 AA4 4 LEU A 270 ARG A 273 -1 O LEU A 272 N CYS A 259
SHEET 1 AA5 4 LYS B 6 SER B 11 0
SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23
SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 AA6 4 LYS B 6 SER B 11 0
SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23
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 LYS B 94 -1 O LYS B 91 N VAL B 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.05
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.06
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.01
LINK O HOH A 597 MG MG P 101 1555 1555 2.12
LINK OH TYR B 66 MG MG B 101 1555 1555 2.99
CISPEP 1 TYR A 209 PRO A 210 0 0.56
CISPEP 2 HIS B 31 PRO B 32 0 0.08
SITE 1 AC1 1 ARG A 181
SITE 1 AC2 4 ASP A 29 ASP A 30 PHE A 241 TYR B 63
SITE 1 AC3 2 GLU A 166 ARG A 170
SITE 1 AC4 3 HIS A 188 MET A 189 ARG A 273
SITE 1 AC5 2 LYS A 127 GLU A 128
SITE 1 AC6 1 SER A 105
SITE 1 AC7 3 ILE B 35 VAL B 37 TYR B 66
SITE 1 AC8 3 HOH A 597 ASP P 4 HOH P 206
CRYST1 51.043 79.063 54.903 90.00 111.11 90.00 P 1 21 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 0.019591 0.000000 0.007564 0.00000
SCALE2 0.000000 0.012648 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019524 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
