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1EEY.pdb
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HEADER IMMUNE SYSTEM 04-FEB-00 1EEY
TITLE CRYSTAL STRUCTURE DETERMINATION OF HLA A2 COMPLEXED TO
TITLE 2 PEPTIDE GP2 WITH THE SUBSTITUTION (I2L/V5L/L9V)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA-A2.1 MHC CLASS I (HEAVY CHAIN);
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: RESIDUES 1-275 OF EXTRACELLULAR PORTION;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN (LIGHT CHAIN);
COMPND 8 CHAIN: B, E;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: GP2 PEPTIDE;
COMPND 12 CHAIN: C, F;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 OTHER_DETAILS: THE PEPTIDE WAS SYNTHESIZED AT THE PEPTIDE
SOURCE 16 SYNTHESIS FACILITY OF UNIVERSITY OF NORTH CAROLINA AT
SOURCE 17 CHAPEL HILL.
KEYWDS MAJOR HISTICOMPATIBILITY COMPLEX, PEPTIDE BINDING,
KEYWDS 2 CRYSTALLOGRAPHY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.SHARMA,J.J.KUHNS,E.J.COLLINS
REVDAT 3 24-FEB-09 1EEY 1 VERSN
REVDAT 2 29-MAR-05 1EEY 1 JRNL
REVDAT 1 10-JUN-03 1EEY 0
JRNL AUTH A.K.SHARMA,J.J.KUHNS,S.YAN,R.H.FRIEDLINE,B.LONG,
JRNL AUTH 2 R.TISCH,E.J.COLLINS
JRNL TITL CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX ANCHOR
JRNL TITL 2 SUBSTITUTIONS ALTER THE CONFORMATION OF T CELL
JRNL TITL 3 RECEPTOR CONTACTS.
JRNL REF J.BIOL.CHEM. V. 276 21443 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11287414
JRNL DOI 10.1074/JBC.M010791200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.J.KUHNS,M.A.BATALIA,S.YAN,E.J.COLLINS
REMARK 1 TITL POOR BINDING OF HER-2/NEU EPITOPE (GP2) TO
REMARK 1 TITL 2 HLA-A2.1 IS DUE TO A LACK OF INTERACTIONS WITH THE
REMARK 1 TITL 3 CENTER OF THE PEPTIDE
REMARK 1 REF J.BIOL.CHEM. V. 274 36422 1999
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.274.51.36422
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1060563.400
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 38096
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 SET) : 0.248
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1907
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5027
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 254
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6292
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.99000
REMARK 3 B22 (A**2) : -3.63000
REMARK 3 B33 (A**2) : -3.36000
REMARK 3 B12 (A**2) : 1.38000
REMARK 3 B13 (A**2) : 1.11000
REMARK 3 B23 (A**2) : 0.09000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 28.69
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD FUNCTION
REMARK 4
REMARK 4 1EEY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-00.
REMARK 100 THE RCSB ID CODE IS RCSB010510.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38096
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.18000
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 25 MM MES, PH6.5.,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: HLA A2 HEAVY CHAIN NONCOVALENTLY ASSOCIATED TO A BETA-2-
REMARK 300 MICROGLOBULIN SUBUNIT (LIGHT CHAIN). HEAVY CHAIN IS MADE OF
REMARK 300 THREE SUBUNITS ALPHA1, ALPHA 2 AND ALPHA 3. PEPTIDE BINDS TO THE
REMARK 300 GROOVE FORMED BY THE ALPHA1 AND ALPHA2 DOMAINS.
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: 4250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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: 4210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 400
REMARK 400 COMPOUND
REMARK 400 HLA A2 heavy chain noncovalently associated to a
REMARK 400 beta-2-microglobulin subunit (light chain). Heavy chain is
REMARK 400 made of three subunits alpha1, alpha 2 and alpha 3. Peptide
REMARK 400 binds to the groove formed by the alpha1 and alpha2 domains.
REMARK 410
REMARK 410 IMGT/3Dstructure-DB annotations
REMARK 410 (http://www.imgt.org)
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1 HLA-A*0201
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Homo sapiens (human)
REMARK 410 Chain ID
REMARK 410 1eey_A,1eey_B
REMARK 410
REMARK 410 ligand(s)
REMARK 410 Receptor tyrosine-protein kinase erbB-2 peptide 654-662 (P04626),
REMARK 410 I2>L, L5>V, L9>V
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Homo sapiens (human)
REMARK 410 Chain ID
REMARK 410 1eey_C
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1 HLA-A*0201
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Homo sapiens (human)
REMARK 410 Chain ID
REMARK 410 1eey_D,1eey_E
REMARK 410
REMARK 410 ligand(s)
REMARK 410 Receptor tyrosine-protein kinase erbB-2 peptide 654-662 (P04626),
REMARK 410 I2>L, L5>V, L9>V
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Homo sapiens (human)
REMARK 410 Chain ID
REMARK 410 1eey_F
REMARK 410
REMARK 410
REMARK 410 Chain ID 1eey_A (1EEYA)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDGETRK
REMARK 410 ][ G-ALPHA
REMARK 410 VKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDGKDYIALKEDLRS
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHE
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 ATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGQEQRYTCHVQHE
REMARK 410 ]
REMARK 410 GLPKPLTLRWE
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Homo sapiens HLA-A*0201
REMARK 410 G-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 G-DOMAIN IMGT gene and allele HLA-A*0296 (100%), Homo
REMARK 410 G-DOMAIN IMGT gene and allele sapiens HLA-A*9221 (100%)
REMARK 410 G-DOMAIN ..........GSHSMRY.FFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAA
REMARK 410 G-DOMAIN SQRMEPRA.......PWIEQEGPEYWDGETRKVKAHSQTHRVDLGTLRGYYN
REMARK 410 G-DOMAIN QSEA
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Homo sapiens HLA-A*0201
REMARK 410 G-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 G-DOMAIN IMGT gene and allele HLA-A*0296 (100%), Homo
REMARK 410 G-DOMAIN IMGT gene and allele sapiens HLA-A*9221 (100%)
REMARK 410 G-DOMAIN ..........GSHTVQRMYGCDVGSDWRFLRGYHQYAYDGKDYIALKED..L
REMARK 410 G-DOMAIN RSWTAAD.......MAAQTTKHKWEAA.HVAEQLRAYLEGTCVEWLRRYLEN
REMARK 410 G-DOMAIN GKETLQRT
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Homo sapiens HLA-A*0201
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele HLA-A*0296 (100%), Homo
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele sapiens HLA-A*9221 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DAPKTHMTHHAVSD......HEATLRCWALSFYP..AEITLTWQR
REMARK 410 C-LIKE-DOMAIN DGEDQTQ..DTELVETRPAGD......GTFQKWAAVVVPSG.....QEQRYT
REMARK 410 C-LIKE-DOMAIN CHVQHEG..LPKPLTLRW
REMARK 410
REMARK 410 Chain ID 1eey_B (1EEYB)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (2-100) [D1]
REMARK 410 MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLL
REMARK 410 ]
REMARK 410 YYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Homo sapiens B2M*01
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele B2M*02 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQRTPKIQVYSRHPAEN....GKSNFLNCYVSGFHP..SDIEVDLLK
REMARK 410 C-LIKE-DOMAIN NGERIE...KVEHSDLSFSKD......WSFYLLYYTEFTPTE.....KDEYA
REMARK 410 C-LIKE-DOMAIN CRVNHVT..LSQPKIVKWDRDM
REMARK 410
REMARK 410 Chain ID 1eey_D (1EEYD)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDGETRK
REMARK 410 ][ G-ALPHA
REMARK 410 VKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDGKDYIALKEDLRS
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHE
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 ATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGQEQRYTCHVQHE
REMARK 410 ]
REMARK 410 GLPKPLTLRWE
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Homo sapiens HLA-A*0201
REMARK 410 G-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 G-DOMAIN IMGT gene and allele HLA-A*0296 (100%), Homo
REMARK 410 G-DOMAIN IMGT gene and allele sapiens HLA-A*9221 (100%)
REMARK 410 G-DOMAIN ..........GSHSMRY.FFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAA
REMARK 410 G-DOMAIN SQRMEPRA.......PWIEQEGPEYWDGETRKVKAHSQTHRVDLGTLRGYYN
REMARK 410 G-DOMAIN QSEA
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Homo sapiens HLA-A*0201
REMARK 410 G-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 G-DOMAIN IMGT gene and allele HLA-A*0296 (100%), Homo
REMARK 410 G-DOMAIN IMGT gene and allele sapiens HLA-A*9221 (100%)
REMARK 410 G-DOMAIN ..........GSHTVQRMYGCDVGSDWRFLRGYHQYAYDGKDYIALKED..L
REMARK 410 G-DOMAIN RSWTAAD.......MAAQTTKHKWEAA.HVAEQLRAYLEGTCVEWLRRYLEN
REMARK 410 G-DOMAIN GKETLQRT
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Homo sapiens HLA-A*0201
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele HLA-A*0296 (100%), Homo
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele sapiens HLA-A*9221 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DAPKTHMTHHAVSD......HEATLRCWALSFYP..AEITLTWQR
REMARK 410 C-LIKE-DOMAIN DGEDQTQ..DTELVETRPAGD......GTFQKWAAVVVPSG.....QEQRYT
REMARK 410 C-LIKE-DOMAIN CHVQHEG..LPKPLTLRW
REMARK 410
REMARK 410 Chain ID 1eey_E (1EEYE)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (2-100) [D1]
REMARK 410 MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLL
REMARK 410 ]
REMARK 410 YYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Homo sapiens B2M*01
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele B2M*02 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQRTPKIQVYSRHPAEN....GKSNFLNCYVSGFHP..SDIEVDLLK
REMARK 410 C-LIKE-DOMAIN NGERIE...KVEHSDLSFSKD......WSFYLLYYTEFTPTE.....KDEYA
REMARK 410 C-LIKE-DOMAIN CRVNHVT..LSQPKIVKWDRDM
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 -122.77 57.28
REMARK 500 TRP A 107 15.43 59.52
REMARK 500 HIS A 114 96.07 -163.55
REMARK 500 ASP A 137 -157.75 -137.95
REMARK 500 THR A 178 -70.82 -88.85
REMARK 500 LYS A 243 146.27 -176.14
REMARK 500 HIS B 31 134.19 -174.11
REMARK 500 PRO B 32 -178.62 -65.81
REMARK 500 TRP B 60 -6.37 73.43
REMARK 500 ASP D 29 -124.17 56.06
REMARK 500 TRP D 107 16.44 59.16
REMARK 500 HIS D 114 96.68 -161.66
REMARK 500 TYR D 123 -60.90 -120.31
REMARK 500 ASP D 137 -157.90 -137.08
REMARK 500 THR D 178 -71.51 -88.49
REMARK 500 HIS D 197 12.72 -152.19
REMARK 500 GLN D 224 52.44 -103.81
REMARK 500 HIS E 31 133.81 -175.36
REMARK 500 PRO E 32 -179.19 -65.54
REMARK 500 TRP E 60 -5.16 72.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH D 309
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QR1 RELATED DB: PDB
REMARK 900 1QR1 CONTAINS HLA-A2.1 COMPLEXED TO GP2 PEPTIDE
REMARK 900 RELATED ID: 1EEZ RELATED DB: PDB
REMARK 900 1EEZ CONTAINS HLA-A2.1 COMPLEXED TO GP2 PEPTIDE (I2L/V5L
REMARK 900 VARIANT)
DBREF 1EEY A 1 275 UNP P01892 1A02_HUMAN 1 275
DBREF 1EEY D 1 275 UNP P01892 1A02_HUMAN 1 275
DBREF 1EEY B 0 99 UNP P01884 B2MG_HUMAN 20 119
DBREF 1EEY E 0 99 UNP P01884 B2MG_HUMAN 20 119
DBREF 1EEY C 1 9 PDB 1EEY 1EEY 1 9
DBREF 1EEY F 1 9 PDB 1EEY 1EEY 1 9
SEQADV 1EEY MET B 1 UNP P01884 ALA 20 INITIATING MET
SEQADV 1EEY MET E 1 UNP P01884 ALA 20 INITIATING MET
SEQRES 1 A 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 275 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 A 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 A 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 275 TRP GLU
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 ILE LEU SER ALA LEU VAL GLY ILE VAL
SEQRES 1 D 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 D 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 D 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 D 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 D 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 D 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 D 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 D 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 D 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 D 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 D 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 D 275 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 D 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 D 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 D 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 D 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 D 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 D 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 D 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 D 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 D 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 D 275 TRP GLU
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 9 ILE LEU SER ALA LEU VAL GLY ILE VAL
FORMUL 7 HOH *143(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 ASP A 1049 ALA A 1061A 1 14
HELIX 4 4 HIS A 1062 GLY A 1072A 1 12
HELIX 5 5 GLY A 1072A GLY A 1085 1 14
HELIX 6 6 GLY A 1085 GLN A 1090 1 6
HELIX 7 7 THR A 2045D THR A 2078 5 4
HELIX 8 8 GLN A 2098 GLN A 2100 5 3
HELIX 9 9 ALA D 49 GLU D 53 5 5
HELIX 10 10 GLY D 56 TYR D 85 1 30
HELIX 11 11 ASP D 1049 ALA D 1061A 1 14
HELIX 12 12 HIS D 1062 GLY D 1072A 1 12
HELIX 13 13 GLY D 1072A GLY D 1085 1 14
HELIX 14 14 GLY D 1085 GLN D 1090 1 6
HELIX 15 15 THR D 2045D THR D 2078 5 4
HELIX 16 16 GLN D 2098 GLN D 2100 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 ALA 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 A1004 VAL A1013 -1 O VAL A1005 N SER A 11
SHEET 6 A 8 PHE A1019 TYR A1028 -1 N LEU A1020 O ASP A1012
SHEET 7 A 8 LYS A1031 LEU A1036 -1 O LYS A1031 N TYR A1028
SHEET 8 A 8 TRP A1045 ALA A1047 -1 N THR A1046 O ALA A1035
SHEET 1 B 4 LYS A2003 ALA A2010 0
SHEET 2 B 4 GLU A2018 PHE A2028 -1 N THR A2020 O HIS A2009
SHEET 3 B 4 PHE A2085B PRO A2092 -1 N PHE A2085B O PHE A2028
SHEET 4 B 4 GLU A2079 LEU A2080 -1 N GLU A2079 O ALA A2088
SHEET 1 C 4 LYS A2003 ALA A2010 0
SHEET 2 C 4 GLU A2018 PHE A2028 -1 N THR A2020 O HIS A2009
SHEET 3 C 4 PHE A2085B PRO A2092 -1 N PHE A2085B O PHE A2028
SHEET 4 C 4 ARG A2084 PRO A2084A-1 N ARG A2084 O GLN A2085A
SHEET 1 D 4 GLU A2045A ASP A2045B 0
SHEET 2 D 4 THR A2038 ARG A2043 -1 N ARG A2043 O GLU A2045A
SHEET 3 D 4 TYR A2102 GLN A2107 -1 O THR A2103 N GLN A2042
SHEET 4 D 4 LEU A2117 LEU A2119 -1 O LEU A2117 N VAL A2106
SHEET 1 E 4 LYS B1003 SER B1008 0
SHEET 2 E 4 ASN B1019 PHE B1028 -1 N ASN B1022 O TYR B1007
SHEET 3 E 4 PHE B1085B PHE B1091 -1 N PHE B1085B O PHE B1028
SHEET 4 E 4 GLU B1079 HIS B1080 -1 O GLU B1079 N TYR B1088
SHEET 1 F 4 LYS B1003 SER B1008 0
SHEET 2 F 4 ASN B1019 PHE B1028 -1 N ASN B1022 O TYR B1007
SHEET 3 F 4 PHE B1085B PHE B1091 -1 N PHE B1085B O PHE B1028
SHEET 4 F 4 SER B1084 PHE B1084A-1 O SER B1084 N TYR B1085A
SHEET 1 G 4 GLU B1045A ARG B1045B 0
SHEET 2 G 4 GLU B1038 LYS B1043 -1 N LYS B1043 O GLU B1045A
SHEET 3 G 4 TYR B1102 ASN B1107 -1 O ALA B1103 N LEU B1042
SHEET 4 G 4 LYS B1117 LYS B1120 -1 O LYS B1117 N VAL B1106
SHEET 1 H 8 GLU D 46 PRO D 47 0
SHEET 2 H 8 THR D 31 ASP D 37 -1 O ARG D 35 N GLU D 46
SHEET 3 H 8 ARG D 21 VAL D 28 -1 N ALA D 24 O PHE D 36
SHEET 4 H 8 HIS D 3 VAL D 12 -1 O ARG D 6 N TYR D 27
SHEET 5 H 8 THR D1004 VAL D1013 -1 O VAL D1005 N SER D 11
SHEET 6 H 8 PHE D1019 TYR D1028 -1 N LEU D1020 O ASP D1012
SHEET 7 H 8 LYS D1031 LEU D1036 -1 O LYS D1031 N TYR D1028
SHEET 8 H 8 TRP D1045 ALA D1047 -1 N THR D1046 O ALA D1035
SHEET 1 I 4 LYS D2003 SER D2012 0
SHEET 2 I 4 GLU D2018 PHE D2028 -1 O GLU D2018 N SER D2012
SHEET 3 I 4 PHE D2085B PRO D2092 -1 N PHE D2085B O PHE D2028
SHEET 4 I 4 GLU D2079 LEU D2080 -1 N GLU D2079 O ALA D2088
SHEET 1 J 4 LYS D2003 SER D2012 0
SHEET 2 J 4 GLU D2018 PHE D2028 -1 O GLU D2018 N SER D2012
SHEET 3 J 4 PHE D2085B PRO D2092 -1 N PHE D2085B O PHE D2028
SHEET 4 J 4 ARG D2084 PRO D2084A-1 N ARG D2084 O GLN D2085A
SHEET 1 K 4 GLU D2045A ASP D2045B 0
SHEET 2 K 4 THR D2038 ARG D2043 -1 O ARG D2043 N GLU D2045A
SHEET 3 K 4 TYR D2102 GLN D2107 -1 N THR D2103 O GLN D2042
SHEET 4 K 4 LEU D2117 ARG D2120 -1 N LEU D2117 O VAL D2106
SHEET 1 L 4 LYS E1003 SER E1008 0
SHEET 2 L 4 ASN E1019 PHE E1028 -1 N ASN E1022 O TYR E1007
SHEET 3 L 4 PHE E1085B PHE E1091 -1 N PHE E1085B O PHE E1028
SHEET 4 L 4 GLU E1079 HIS E1080 -1 O GLU E1079 N TYR E1088
SHEET 1 M 4 LYS E1003 SER E1008 0
SHEET 2 M 4 ASN E1019 PHE E1028 -1 N ASN E1022 O TYR E1007
SHEET 3 M 4 PHE E1085B PHE E1091 -1 N PHE E1085B O PHE E1028
SHEET 4 M 4 SER E1084 PHE E1084A-1 O SER E1084 N TYR E1085A
SHEET 1 N 4 GLU E1045A ARG E1045B 0
SHEET 2 N 4 GLU E1038 LYS E1043 -1 N LYS E1043 O GLU E1045A
SHEET 3 N 4 TYR E1102 ASN E1107 -1 O ALA E1103 N LEU E1042
SHEET 4 N 4 LYS E1117 LYS E1120 -1 O LYS E1117 N VAL E1106
SSBOND 1 CYS A 1011 CYS A 1074 1555 1555
SSBOND 2 CYS A 2023 CYS A 2104 1555 1555
SSBOND 3 CYS B 1023 CYS B 1104 1555 1555
SSBOND 4 CYS D 1011 CYS D 1074 1555 1555
SSBOND 5 CYS D 2023 CYS D 2104 1555 1555
SSBOND 6 CYS E 1023 CYS E 1104 1555 1555
CISPEP 1 TYR A 2029 PRO A 2030 0 0.12
CISPEP 2 HIS B 1029 PRO B 1030 0 -0.05
CISPEP 3 TYR D 2029 PRO D 2030 0 -0.15
CISPEP 4 HIS E 1029 PRO E 1030 0 0.06
CRYST1 49.950 62.930 74.650 82.07 76.50 78.04 P 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 0.020020 -0.004241 -0.004427 0.00000
SCALE2 0.000000 0.016243 -0.001537 0.00000
SCALE3 0.000000 0.000000 0.013838 0.00000
ATOM 1 N GLY A 1 -18.295 -14.326 -7.314 1.00 20.92 N
ATOM 2 CA GLY A 1 -18.444 -13.675 -5.984 1.00 20.68 C
ATOM 3 C GLY A 1 -17.632 -12.398 -5.875 1.00 20.54 C
ATOM 4 O GLY A 1 -17.103 -11.915 -6.872 1.00 20.66 O
ATOM 5 N SER A 2 -17.537 -11.852 -4.663 1.00 20.29 N
ATOM 6 CA SER A 2 -16.780 -10.625 -4.424 1.00 19.96 C
ATOM 7 C SER A 2 -15.282 -10.871 -4.451 1.00 19.64 C
ATOM 8 O SER A 2 -14.823 -11.992 -4.217 1.00 19.66 O
ATOM 9 CB SER A 2 -17.159 -10.012 -3.078 1.00 20.06 C
ATOM 10 OG SER A 2 -18.384 -9.307 -3.185 1.00 20.60 O
ATOM 11 N HIS A 3 -14.524 -9.807 -4.715 1.00 18.87 N
ATOM 12 CA HIS A 3 -13.077 -9.902 -4.805 1.00 18.07 C
ATOM 13 C HIS A 3 -12.431 -8.636 -4.274 1.00 17.50 C
ATOM 14 O HIS A 3 -13.082 -7.605 -4.164 1.00 17.11 O
ATOM 15 CB HIS A 3 -12.668 -10.113 -6.268 1.00 17.92 C
ATOM 16 CG HIS A 3 -13.095 -11.436 -6.824 1.00 18.21 C
ATOM 17 ND1 HIS A 3 -12.437 -12.613 -6.533 1.00 18.34 N
ATOM 18 CD2 HIS A 3 -14.143 -11.777 -7.612 1.00 18.27 C
ATOM 19 CE1 HIS A 3 -13.061 -13.621 -7.116 1.00 18.26 C
ATOM 20 NE2 HIS A 3 -14.099 -13.141 -7.777 1.00 18.48 N
ATOM 21 N SER A 4 -11.142 -8.722 -3.961 1.00 16.81 N
ATOM 22 CA SER A 4 -10.417 -7.573 -3.457 1.00 16.54 C
ATOM 23 C SER A 4 -8.938 -7.664 -3.805 1.00 16.42 C
ATOM 24 O SER A 4 -8.413 -8.751 -4.095 1.00 16.42 O
ATOM 25 CB SER A 4 -10.554 -7.484 -1.933 1.00 16.49 C
ATOM 26 OG SER A 4 -9.858 -8.547 -1.289 1.00 16.62 O
ATOM 27 N MET A 5 -8.283 -6.509 -3.790 1.00 15.86 N
ATOM 28 CA MET A 5 -6.843 -6.418 -4.013 1.00 15.61 C
ATOM 29 C MET A 5 -6.299 -5.482 -2.950 1.00 15.25 C
ATOM 30 O MET A 5 -6.819 -4.381 -2.770 1.00 15.22 O
ATOM 31 CB MET A 5 -6.489 -5.831 -5.376 1.00 15.50 C
ATOM 32 CG MET A 5 -4.984 -5.586 -5.486 1.00 15.89 C
ATOM 33 SD MET A 5 -4.347 -5.107 -7.106 1.00 16.28 S
ATOM 34 CE MET A 5 -4.789 -3.363 -7.158 1.00 15.80 C
ATOM 35 N ARG A 6 -5.274 -5.903 -2.226 1.00 15.01 N
ATOM 36 CA ARG A 6 -4.715 -5.017 -1.220 1.00 14.92 C
ATOM 37 C ARG A 6 -3.233 -5.163 -0.989 1.00 14.39 C
ATOM 38 O ARG A 6 -2.669 -6.253 -1.093 1.00 14.46 O
ATOM 39 CB ARG A 6 -5.471 -5.141 0.110 1.00 15.78 C
ATOM 40 CG ARG A 6 -6.181 -6.458 0.352 1.00 16.87 C
ATOM 41 CD ARG A 6 -7.458 -6.208 1.160 1.00 17.71 C
ATOM 42 NE ARG A 6 -8.191 -5.112 0.537 1.00 19.21 N
ATOM 43 CZ ARG A 6 -9.461 -4.800 0.765 1.00 19.45 C
ATOM 44 NH1 ARG A 6 -10.188 -5.505 1.623 1.00 19.78 N
ATOM 45 NH2 ARG A 6 -10.003 -3.777 0.113 1.00 19.46 N
ATOM 46 N TYR A 7 -2.611 -4.034 -0.680 1.00 13.68 N
ATOM 47 CA TYR A 7 -1.189 -3.975 -0.418 1.00 13.16 C
ATOM 48 C TYR A 7 -0.950 -3.700 1.064 1.00 12.93 C
ATOM 49 O TYR A 7 -1.576 -2.817 1.656 1.00 12.78 O
ATOM 50 CB TYR A 7 -0.545 -2.889 -1.296 1.00 12.70 C
ATOM 51 CG TYR A 7 -0.435 -3.268 -2.766 1.00 12.35 C
ATOM 52 CD1 TYR A 7 0.613 -4.068 -3.233 1.00 12.41 C
ATOM 53 CD2 TYR A 7 -1.381 -2.833 -3.689 1.00 12.59 C
ATOM 54 CE1 TYR A 7 0.712 -4.419 -4.590 1.00 11.83 C
ATOM 55 CE2 TYR A 7 -1.291 -3.173 -5.041 1.00 12.04 C
ATOM 56 CZ TYR A 7 -0.243 -3.962 -5.483 1.00 12.05 C
ATOM 57 OH TYR A 7 -0.155 -4.253 -6.827 1.00 11.53 O
ATOM 58 N PHE A 8 -0.051 -4.481 1.654 1.00 12.93 N
ATOM 59 CA PHE A 8 0.296 -4.370 3.063 1.00 12.83 C
ATOM 60 C PHE A 8 1.746 -3.929 3.180 1.00 12.96 C
ATOM 61 O PHE A 8 2.636 -4.530 2.578 1.00 12.92 O
ATOM 62 CB PHE A 8 0.092 -5.726 3.749 1.00 12.68 C
ATOM 63 CG PHE A 8 -1.320 -6.221 3.691 1.00 12.65 C
ATOM 64 CD1 PHE A 8 -2.207 -5.959 4.727 1.00 12.68 C
ATOM 65 CD2 PHE A 8 -1.769 -6.940 2.596 1.00 12.80 C
ATOM 66 CE1 PHE A 8 -3.519 -6.408 4.670 1.00 12.50 C
ATOM 67 CE2 PHE A 8 -3.083 -7.396 2.528 1.00 13.03 C
ATOM 68 CZ PHE A 8 -3.960 -7.126 3.571 1.00 12.81 C
ATOM 69 N PHE A 9 1.978 -2.878 3.961 1.00 13.27 N
ATOM 70 CA PHE A 9 3.317 -2.338 4.147 1.00 13.62 C
ATOM 71 C PHE A 9 3.692 -2.255 5.618 1.00 13.87 C
ATOM 72 O PHE A 9 2.949 -1.684 6.423 1.00 13.89 O
ATOM 73 CB PHE A 9 3.401 -0.938 3.537 1.00 13.67 C
ATOM 74 CG PHE A 9 2.906 -0.861 2.123 1.00 13.73 C
ATOM 75 CD1 PHE A 9 3.762 -1.102 1.057 1.00 13.90 C
ATOM 76 CD2 PHE A 9 1.579 -0.541 1.858 1.00 13.81 C
ATOM 77 CE1 PHE A 9 3.305 -1.021 -0.260 1.00 14.02 C
ATOM 78 CE2 PHE A 9 1.106 -0.457 0.550 1.00 14.02 C
ATOM 79 CZ PHE A 9 1.970 -0.696 -0.515 1.00 13.99 C
ATOM 80 N THR A 10 4.846 -2.818 5.961 1.00 14.14 N
ATOM 81 CA THR A 10 5.336 -2.790 7.336 1.00 14.66 C
ATOM 82 C THR A 10 6.721 -2.178 7.369 1.00 15.06 C
ATOM 83 O THR A 10 7.623 -2.618 6.655 1.00 15.00 O
ATOM 84 CB THR A 10 5.452 -4.191 7.938 1.00 14.54 C
ATOM 85 OG1 THR A 10 4.219 -4.894 7.764 1.00 14.50 O
ATOM 86 CG2 THR A 10 5.777 -4.096 9.418 1.00 14.52 C
ATOM 87 N SER A 11 6.885 -1.169 8.209 1.00 15.76 N
ATOM 88 CA SER A 11 8.157 -0.485 8.356 1.00 16.71 C
ATOM 89 C SER A 11 8.553 -0.561 9.825 1.00 16.92 C
ATOM 90 O SER A 11 7.759 -0.249 10.699 1.00 16.82 O
ATOM 91 CB SER A 11 8.004 0.974 7.917 1.00 17.14 C
ATOM 92 OG SER A 11 9.182 1.720 8.179 1.00 18.48 O
ATOM 93 N VAL A 12 9.779 -0.987 10.099 1.00 17.57 N
ATOM 94 CA VAL A 12 10.244 -1.107 11.476 1.00 18.28 C
ATOM 95 C VAL A 12 11.613 -0.471 11.653 1.00 19.08 C
ATOM 96 O VAL A 12 12.581 -0.901 11.029 1.00 19.38 O
ATOM 97 CB VAL A 12 10.352 -2.588 11.899 1.00 18.08 C
ATOM 98 CG1 VAL A 12 10.826 -2.687 13.347 1.00 17.98 C
ATOM 99 CG2 VAL A 12 9.022 -3.286 11.722 1.00 17.75 C
ATOM 100 N SER A 13 11.705 0.536 12.515 1.00 20.01 N
ATOM 101 CA SER A 13 12.981 1.210 12.746 1.00 21.10 C
ATOM 102 C SER A 13 13.954 0.306 13.494 1.00 22.18 C
ATOM 103 O SER A 13 13.554 -0.525 14.318 1.00 22.15 O
ATOM 104 CB SER A 13 12.770 2.509 13.533 1.00 20.80 C
ATOM 105 OG SER A 13 12.093 2.269 14.755 1.00 20.29 O
ATOM 106 N ARG A 14 15.236 0.475 13.197 1.00 23.46 N
ATOM 107 CA ARG A 14 16.292 -0.308 13.818 1.00 24.71 C
ATOM 108 C ARG A 14 17.394 0.625 14.306 1.00 25.44 C
ATOM 109 O ARG A 14 18.452 0.744 13.686 1.00 25.71 O
ATOM 110 CB ARG A 14 16.848 -1.318 12.807 1.00 24.98 C
ATOM 111 CG ARG A 14 15.814 -2.345 12.402 1.00 25.52 C
ATOM 112 CD ARG A 14 16.388 -3.435 11.520 1.00 25.80 C
ATOM 113 NE ARG A 14 16.667 -2.972 10.163 1.00 26.30 N
ATOM 114 CZ ARG A 14 16.766 -3.781 9.111 1.00 26.24 C
ATOM 115 NH1 ARG A 14 16.610 -5.089 9.267 1.00 26.20 N
ATOM 116 NH2 ARG A 14 17.005 -3.284 7.906 1.00 26.26 N
ATOM 117 N PRO A 15 17.145 1.310 15.428 1.00 26.20 N
ATOM 118 CA PRO A 15 18.063 2.258 16.066 1.00 26.63 C
ATOM 119 C PRO A 15 19.482 1.720 16.243 1.00 27.27 C
ATOM 120 O PRO A 15 19.699 0.700 16.902 1.00 27.08 O
ATOM 121 CB PRO A 15 17.386 2.537 17.400 1.00 26.73 C
ATOM 122 CG PRO A 15 15.919 2.444 17.040 1.00 26.58 C
ATOM 123 CD PRO A 15 15.888 1.202 16.195 1.00 26.40 C
ATOM 124 N GLY A 16 20.443 2.420 15.648 1.00 27.91 N
ATOM 125 CA GLY A 16 21.832 2.016 15.754 1.00 28.69 C
ATOM 126 C GLY A 16 22.154 0.743 15.002 1.00 29.08 C
ATOM 127 O GLY A 16 23.287 0.276 15.045 1.00 29.27 O
ATOM 128 N ARG A 17 21.166 0.180 14.312 1.00 29.41 N
ATOM 129 CA ARG A 17 21.374 -1.055 13.564 1.00 29.68 C
ATOM 130 C ARG A 17 21.192 -0.831 12.069 1.00 29.32 C
ATOM 131 O ARG A 17 20.879 -1.755 11.322 1.00 29.40 O
ATOM 132 CB ARG A 17 20.411 -2.145 14.061 1.00 30.37 C
ATOM 133 CG ARG A 17 20.584 -2.486 15.543 1.00 31.49 C
ATOM 134 CD ARG A 17 19.679 -3.643 15.983 1.00 32.34 C
ATOM 135 NE ARG A 17 18.266 -3.270 16.110 1.00 33.07 N
ATOM 136 CZ ARG A 17 17.783 -2.413 17.011 1.00 33.43 C
ATOM 137 NH1 ARG A 17 18.596 -1.820 17.881 1.00 33.46 N
ATOM 138 NH2 ARG A 17 16.479 -2.156 17.055 1.00 33.60 N
ATOM 139 N GLY A 18 21.379 0.412 11.642 1.00 29.07 N
ATOM 140 CA GLY A 18 21.251 0.736 10.235 1.00 28.68 C
ATOM 141 C GLY A 18 19.876 1.156 9.753 1.00 28.30 C
ATOM 142 O GLY A 18 19.077 1.723 10.492 1.00 28.53 O
ATOM 143 N GLU A 19 19.613 0.860 8.489 1.00 27.89 N
ATOM 144 CA GLU A 19 18.361 1.194 7.827 1.00 27.28 C
ATOM 145 C GLU A 19 17.136 0.502 8.418 1.00 26.38 C
ATOM 146 O GLU A 19 17.232 -0.591 8.981 1.00 26.29 O
ATOM 147 CB GLU A 19 18.466 0.820 6.348 1.00 28.03 C
ATOM 148 CG GLU A 19 17.836 1.822 5.418 1.00 29.14 C
ATOM 149 CD GLU A 19 18.553 3.145 5.471 1.00 29.85 C
ATOM 150 OE1 GLU A 19 19.778 3.150 5.242 1.00 30.46 O
ATOM 151 OE2 GLU A 19 17.901 4.178 5.742 1.00 30.49 O
ATOM 152 N PRO A 20 15.961 1.140 8.301 1.00 25.43 N
ATOM 153 CA PRO A 20 14.709 0.578 8.812 1.00 24.45 C
ATOM 154 C PRO A 20 14.294 -0.604 7.943 1.00 23.57 C
ATOM 155 O PRO A 20 14.513 -0.596 6.733 1.00 23.27 O
ATOM 156 CB PRO A 20 13.729 1.736 8.677 1.00 24.73 C
ATOM 157 CG PRO A 20 14.600 2.932 8.815 1.00 25.13 C
ATOM 158 CD PRO A 20 15.790 2.566 7.979 1.00 25.37 C
ATOM 159 N ARG A 21 13.696 -1.618 8.554 1.00 22.67 N
ATOM 160 CA ARG A 21 13.244 -2.785 7.802 1.00 21.81 C
ATOM 161 C ARG A 21 11.941 -2.413 7.102 1.00 20.73 C
ATOM 162 O ARG A 21 11.065 -1.811 7.710 1.00 20.71 O
ATOM 163 CB ARG A 21 12.990 -3.967 8.744 1.00 22.31 C
ATOM 164 CG ARG A 21 12.528 -5.237 8.044 1.00 22.93 C
ATOM 165 CD ARG A 21 13.605 -5.770 7.124 1.00 23.61 C
ATOM 166 NE ARG A 21 13.227 -7.028 6.488 1.00 24.16 N
ATOM 167 CZ ARG A 21 13.219 -8.211 7.093 1.00 24.59 C
ATOM 168 NH1 ARG A 21 13.573 -8.317 8.368 1.00 24.80 N
ATOM 169 NH2 ARG A 21 12.859 -9.296 6.414 1.00 24.75 N
ATOM 170 N PHE A 22 11.820 -2.771 5.829 1.00 19.49 N
ATOM 171 CA PHE A 22 10.619 -2.469 5.068 1.00 18.07 C
ATOM 172 C PHE A 22 10.134 -3.692 4.293 1.00 17.29 C
ATOM 173 O PHE A 22 10.895 -4.306 3.551 1.00 17.14 O
ATOM 174 CB PHE A 22 10.886 -1.328 4.088 1.00 18.04 C
ATOM 175 CG PHE A 22 9.668 -0.907 3.318 1.00 17.75 C
ATOM 176 CD1 PHE A 22 8.644 -0.212 3.947 1.00 17.57 C
ATOM 177 CD2 PHE A 22 9.527 -1.241 1.977 1.00 17.52 C
ATOM 178 CE1 PHE A 22 7.492 0.143 3.248 1.00 17.64 C
ATOM 179 CE2 PHE A 22 8.385 -0.892 1.268 1.00 17.43 C
ATOM 180 CZ PHE A 22 7.362 -0.199 1.903 1.00 17.60 C
ATOM 181 N ILE A 23 8.865 -4.042 4.463 1.00 16.28 N
ATOM 182 CA ILE A 23 8.306 -5.185 3.760 1.00 15.41 C
ATOM 183 C ILE A 23 6.947 -4.874 3.166 1.00 14.86 C
ATOM 184 O ILE A 23 6.061 -4.350 3.843 1.00 14.98 O
ATOM 185 CB ILE A 23 8.160 -6.407 4.687 1.00 15.25 C
ATOM 186 CG1 ILE A 23 9.496 -6.690 5.378 1.00 15.16 C
ATOM 187 CG2 ILE A 23 7.738 -7.610 3.877 1.00 15.13 C
ATOM 188 CD1 ILE A 23 9.471 -7.867 6.329 1.00 15.38 C
ATOM 189 N ALA A 24 6.786 -5.200 1.892 1.00 14.06 N
ATOM 190 CA ALA A 24 5.532 -4.969 1.211 1.00 13.25 C
ATOM 191 C ALA A 24 5.074 -6.259 0.554 1.00 12.80 C
ATOM 192 O ALA A 24 5.889 -7.039 0.052 1.00 12.42 O
ATOM 193 CB ALA A 24 5.699 -3.869 0.154 1.00 13.45 C
ATOM 194 N VAL A 25 3.766 -6.489 0.579 1.00 12.22 N
ATOM 195 CA VAL A 25 3.184 -7.672 -0.044 1.00 11.82 C
ATOM 196 C VAL A 25 1.858 -7.273 -0.652 1.00 11.61 C
ATOM 197 O VAL A 25 1.186 -6.368 -0.154 1.00 11.24 O
ATOM 198 CB VAL A 25 2.943 -8.820 0.957 1.00 11.61 C
ATOM 199 CG1 VAL A 25 4.266 -9.316 1.499 1.00 11.84 C
ATOM 200 CG2 VAL A 25 2.031 -8.358 2.080 1.00 11.78 C
ATOM 201 N GLY A 26 1.506 -7.935 -1.749 1.00 11.63 N
ATOM 202 CA GLY A 26 0.255 -7.649 -2.424 1.00 11.45 C
ATOM 203 C GLY A 26 -0.577 -8.908 -2.474 1.00 11.33 C
ATOM 204 O GLY A 26 -0.037 -9.997 -2.613 1.00 11.48 O
ATOM 205 N TYR A 27 -1.888 -8.761 -2.359 1.00 11.20 N
ATOM 206 CA TYR A 27 -2.790 -9.898 -2.388 1.00 11.37 C
ATOM 207 C TYR A 27 -3.982 -9.628 -3.279 1.00 11.66 C
ATOM 208 O TYR A 27 -4.407 -8.482 -3.435 1.00 11.73 O
ATOM 209 CB TYR A 27 -3.377 -10.190 -0.996 1.00 11.14 C
ATOM 210 CG TYR A 27 -2.465 -10.877 -0.013 1.00 11.17 C
ATOM 211 CD1 TYR A 27 -1.484 -10.164 0.668 1.00 11.21 C
ATOM 212 CD2 TYR A 27 -2.588 -12.245 0.246 1.00 11.17 C
ATOM 213 CE1 TYR A 27 -0.647 -10.786 1.586 1.00 11.07 C
ATOM 214 CE2 TYR A 27 -1.745 -12.884 1.167 1.00 11.18 C
ATOM 215 CZ TYR A 27 -0.782 -12.142 1.828 1.00 11.40 C
ATOM 216 OH TYR A 27 0.056 -12.747 2.729 1.00 11.84 O
ATOM 217 N VAL A 28 -4.502 -10.692 -3.874 1.00 11.63 N
ATOM 218 CA VAL A 28 -5.737 -10.610 -4.630 1.00 11.84 C
ATOM 219 C VAL A 28 -6.512 -11.629 -3.811 1.00 12.34 C
ATOM 220 O VAL A 28 -6.160 -12.812 -3.783 1.00 12.56 O
ATOM 221 CB VAL A 28 -5.635 -11.101 -6.091 1.00 11.62 C
ATOM 222 CG1 VAL A 28 -7.037 -11.228 -6.676 1.00 11.01 C
ATOM 223 CG2 VAL A 28 -4.821 -10.105 -6.927 1.00 11.50 C
ATOM 224 N ASP A 29 -7.548 -11.164 -3.131 1.00 12.83 N
ATOM 225 CA ASP A 29 -8.338 -12.022 -2.270 1.00 13.15 C
ATOM 226 C ASP A 29 -7.354 -12.619 -1.258 1.00 13.30 C
ATOM 227 O ASP A 29 -6.662 -11.868 -0.570 1.00 12.88 O
ATOM 228 CB ASP A 29 -9.055 -13.100 -3.087 1.00 13.75 C
ATOM 229 CG ASP A 29 -10.063 -12.510 -4.078 1.00 14.33 C
ATOM 230 OD1 ASP A 29 -10.667 -11.452 -3.781 1.00 14.54 O
ATOM 231 OD2 ASP A 29 -10.272 -13.109 -5.155 1.00 14.93 O
ATOM 232 N ASP A 30 -7.263 -13.946 -1.178 1.00 13.73 N
ATOM 233 CA ASP A 30 -6.362 -14.585 -0.213 1.00 13.80 C
ATOM 234 C ASP A 30 -5.084 -15.156 -0.847 1.00 14.02 C
ATOM 235 O ASP A 30 -4.368 -15.975 -0.245 1.00 13.92 O
ATOM 236 CB ASP A 30 -7.111 -15.690 0.545 1.00 14.40 C
ATOM 237 CG ASP A 30 -8.367 -15.171 1.262 1.00 14.79 C
ATOM 238 OD1 ASP A 30 -8.265 -14.159 1.984 1.00 14.95 O
ATOM 239 OD2 ASP A 30 -9.454 -15.778 1.108 1.00 15.09 O
ATOM 240 N THR A 31 -4.779 -14.713 -2.059 1.00 13.88 N
ATOM 241 CA THR A 31 -3.571 -15.193 -2.734 1.00 13.93 C
ATOM 242 C THR A 31 -2.559 -14.053 -2.863 1.00 13.86 C
ATOM 243 O THR A 31 -2.870 -13.008 -3.439 1.00 13.90 O
ATOM 244 CB THR A 31 -3.901 -15.722 -4.144 1.00 13.89 C
ATOM 245 OG1 THR A 31 -4.912 -16.733 -4.047 1.00 14.51 O
ATOM 246 CG2 THR A 31 -2.658 -16.306 -4.799 1.00 13.89 C
ATOM 247 N GLN A 32 -1.368 -14.246 -2.303 1.00 13.63 N
ATOM 248 CA GLN A 32 -0.311 -13.245 -2.381 1.00 13.85 C
ATOM 249 C GLN A 32 0.295 -13.339 -3.780 1.00 13.95 C
ATOM 250 O GLN A 32 0.456 -14.443 -4.304 1.00 13.52 O
ATOM 251 CB GLN A 32 0.787 -13.536 -1.356 1.00 14.14 C
ATOM 252 CG GLN A 32 1.708 -12.354 -1.103 1.00 14.25 C
ATOM 253 CD GLN A 32 3.047 -12.752 -0.518 1.00 14.53 C
ATOM 254 OE1 GLN A 32 3.149 -13.725 0.229 1.00 15.27 O
ATOM 255 NE2 GLN A 32 4.079 -11.986 -0.833 1.00 14.22 N
ATOM 256 N PHE A 33 0.626 -12.201 -4.395 1.00 14.00 N
ATOM 257 CA PHE A 33 1.215 -12.251 -5.737 1.00 14.47 C
ATOM 258 C PHE A 33 2.538 -11.506 -5.929 1.00 14.69 C
ATOM 259 O PHE A 33 3.239 -11.758 -6.906 1.00 14.88 O
ATOM 260 CB PHE A 33 0.205 -11.810 -6.814 1.00 13.96 C
ATOM 261 CG PHE A 33 -0.188 -10.363 -6.741 1.00 14.00 C
ATOM 262 CD1 PHE A 33 -1.006 -9.896 -5.713 1.00 13.72 C
ATOM 263 CD2 PHE A 33 0.226 -9.468 -7.730 1.00 13.97 C
ATOM 264 CE1 PHE A 33 -1.415 -8.559 -5.671 1.00 13.98 C
ATOM 265 CE2 PHE A 33 -0.177 -8.119 -7.700 1.00 14.10 C
ATOM 266 CZ PHE A 33 -1.003 -7.664 -6.666 1.00 13.89 C
ATOM 267 N VAL A 34 2.877 -10.593 -5.020 1.00 15.03 N
ATOM 268 CA VAL A 34 4.156 -9.880 -5.094 1.00 15.51 C
ATOM 269 C VAL A 34 4.700 -9.587 -3.699 1.00 16.03 C
ATOM 270 O VAL A 34 3.974 -9.663 -2.707 1.00 16.07 O
ATOM 271 CB VAL A 34 4.055 -8.510 -5.840 1.00 15.44 C
ATOM 272 CG1 VAL A 34 3.715 -8.725 -7.303 1.00 14.99 C
ATOM 273 CG2 VAL A 34 3.029 -7.615 -5.159 1.00 14.69 C
ATOM 274 N ARG A 35 5.981 -9.252 -3.628 1.00 16.79 N
ATOM 275 CA ARG A 35 6.605 -8.916 -2.359 1.00 17.73 C
ATOM 276 C ARG A 35 7.841 -8.066 -2.604 1.00 18.05 C
ATOM 277 O ARG A 35 8.390 -8.037 -3.709 1.00 18.15 O
ATOM 278 CB ARG A 35 7.053 -10.167 -1.603 1.00 18.27 C
ATOM 279 CG ARG A 35 8.389 -10.723 -2.127 1.00 19.55 C
ATOM 280 CD ARG A 35 8.998 -11.763 -1.196 1.00 20.36 C
ATOM 281 NE ARG A 35 10.154 -12.403 -1.812 1.00 21.47 N
ATOM 282 CZ ARG A 35 10.677 -13.556 -1.407 1.00 21.93 C
ATOM 283 NH1 ARG A 35 10.150 -14.197 -0.371 1.00 22.15 N
ATOM 284 NH2 ARG A 35 11.701 -14.090 -2.063 1.00 22.09 N
ATOM 285 N PHE A 36 8.266 -7.379 -1.556 1.00 18.26 N
ATOM 286 CA PHE A 36 9.470 -6.576 -1.590 1.00 18.87 C
ATOM 287 C PHE A 36 10.029 -6.633 -0.185 1.00 19.27 C
ATOM 288 O PHE A 36 9.304 -6.385 0.787 1.00 19.32 O
ATOM 289 CB PHE A 36 9.195 -5.115 -1.940 1.00 18.75 C
ATOM 290 CG PHE A 36 10.432 -4.255 -1.912 1.00 18.81 C
ATOM 291 CD1 PHE A 36 11.374 -4.329 -2.934 1.00 19.02 C
ATOM 292 CD2 PHE A 36 10.688 -3.416 -0.835 1.00 18.97 C
ATOM 293 CE1 PHE A 36 12.557 -3.581 -2.882 1.00 18.88 C
ATOM 294 CE2 PHE A 36 11.871 -2.662 -0.770 1.00 18.93 C
ATOM 295 CZ PHE A 36 12.804 -2.748 -1.795 1.00 18.96 C
ATOM 296 N ASP A 37 11.307 -6.968 -0.071 1.00 19.73 N
ATOM 297 CA ASP A 37 11.948 -7.032 1.238 1.00 20.22 C
ATOM 298 C ASP A 37 13.204 -6.189 1.204 1.00 20.59 C
ATOM 299 O ASP A 37 14.164 -6.533 0.519 1.00 20.62 O
ATOM 300 CB ASP A 37 12.318 -8.469 1.600 1.00 20.08 C
ATOM 301 CG ASP A 37 12.796 -8.600 3.036 1.00 20.24 C
ATOM 302 OD1 ASP A 37 13.436 -7.661 3.551 1.00 19.75 O
ATOM 303 OD2 ASP A 37 12.538 -9.654 3.649 1.00 20.81 O
ATOM 304 N SER A 38 13.191 -5.087 1.950 1.00 21.06 N
ATOM 305 CA SER A 38 14.327 -4.180 2.013 1.00 21.67 C
ATOM 306 C SER A 38 15.639 -4.889 2.356 1.00 22.00 C
ATOM 307 O SER A 38 16.713 -4.425 1.974 1.00 22.08 O
ATOM 308 CB SER A 38 14.072 -3.084 3.047 1.00 21.71 C
ATOM 309 OG SER A 38 14.014 -3.626 4.356 1.00 22.28 O
ATOM 310 N ASP A 39 15.556 -6.003 3.077 1.00 22.32 N
ATOM 311 CA ASP A 39 16.762 -6.742 3.460 1.00 22.76 C
ATOM 312 C ASP A 39 17.158 -7.816 2.450 1.00 22.85 C
ATOM 313 O ASP A 39 18.193 -8.468 2.606 1.00 23.20 O
ATOM 314 CB ASP A 39 16.581 -7.378 4.842 1.00 22.76 C
ATOM 315 CG ASP A 39 16.698 -6.363 5.978 1.00 23.19 C
ATOM 316 OD1 ASP A 39 16.512 -5.148 5.740 1.00 23.16 O
ATOM 317 OD2 ASP A 39 16.968 -6.783 7.125 1.00 23.34 O
ATOM 318 N ALA A 40 16.350 -7.998 1.410 1.00 22.69 N
ATOM 319 CA ALA A 40 16.654 -9.007 0.405 1.00 22.66 C
ATOM 320 C ALA A 40 17.738 -8.520 -0.558 1.00 22.68 C
ATOM 321 O ALA A 40 17.977 -7.320 -0.699 1.00 22.46 O
ATOM 322 CB ALA A 40 15.396 -9.391 -0.355 1.00 22.64 C
ATOM 323 N ALA A 41 18.388 -9.466 -1.225 1.00 22.67 N
ATOM 324 CA ALA A 41 19.474 -9.146 -2.144 1.00 22.64 C
ATOM 325 C ALA A 41 19.086 -8.472 -3.459 1.00 22.48 C
ATOM 326 O ALA A 41 19.810 -7.599 -3.937 1.00 22.58 O
ATOM 327 CB ALA A 41 20.283 -10.418 -2.438 1.00 22.56 C
ATOM 328 N SER A 42 17.959 -8.870 -4.043 1.00 22.19 N
ATOM 329 CA SER A 42 17.523 -8.319 -5.331 1.00 21.89 C
ATOM 330 C SER A 42 17.157 -6.836 -5.334 1.00 21.55 C
ATOM 331 O SER A 42 17.416 -6.117 -6.312 1.00 21.68 O
ATOM 332 CB SER A 42 16.324 -9.104 -5.853 1.00 21.99 C
ATOM 333 OG SER A 42 15.162 -8.790 -5.091 1.00 22.61 O
ATOM 334 N GLN A 43 16.541 -6.379 -4.252 1.00 20.96 N