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1DUZ.pdb
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HEADER IMMUNE SYSTEM 19-JAN-00 1DUZ
TITLE HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A 0201) IN
TITLE 2 COMPLEX WITH A NONAMERIC PEPTIDE FROM HTLV-1 TAX PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA-A*0201;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: HEAVY CHAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2 MICROGLOBULIN;
COMPND 8 CHAIN: B, E;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: HTLV-1 OCTAMERIC TAX PEPTIDE;
COMPND 12 CHAIN: C, F;
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 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: PEPTIDE WAS OBTAINED THROUGH STANDARD SOLID-
SOURCE 16 PHASE PEPTIDE SYNTHESIS
KEYWDS IMMUNOGLOBULIN FOLD, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.KHAN,B.M.BAKER,P.GHOSH,W.E.BIDDISON,D.C.WILEY
REVDAT 3 24-FEB-09 1DUZ 1 VERSN
REVDAT 2 30-AUG-00 1DUZ 1 JRNL DBREF SEQADV
REVDAT 1 04-FEB-00 1DUZ 0
JRNL AUTH A.R.KHAN,B.M.BAKER,P.GHOSH,W.E.BIDDISON,D.C.WILEY
JRNL TITL THE STRUCTURE AND STABILITY OF AN
JRNL TITL 2 HLA-A*0201/OCTAMERIC TAX PEPTIDE COMPLEX WITH AN
JRNL TITL 3 EMPTY CONSERVED PEPTIDE-N-TERMINAL BINDING SITE.
JRNL REF J.IMMUNOL. V. 164 6398 2000
JRNL REFN ISSN 0022-1767
JRNL PMID 10843695
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.R.MADDEN,D.N.GARBOCZI,D.C.WILEY
REMARK 1 TITL THE ANTIGENIC IDENTITY OF PEPTIDE-MHC COMPLEXES: A
REMARK 1 TITL 2 COMPARISON OF THE CONFORMATIONS OF FIVE VIRAL
REMARK 1 TITL 3 PEPTIDES PRESENTED BY HLA-A2
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 75 693 1993
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/0092-8674(93)90490-H
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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 AND HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.3
REMARK 3 NUMBER OF REFLECTIONS : 72184
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 7033
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 608
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.40
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.030
REMARK 3 BOND ANGLES (DEGREES) : 2.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CRYSTALLOGRAPHICALLY RESTRAINED
REMARK 3 LEAST-SQUARES REFINEMENT USING CNS
REMARK 4
REMARK 4 1DUZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-00.
REMARK 100 THE RCSB ID CODE IS RCSB010393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-96
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 : ELLIOTT GX-13
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 : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 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: 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 (%): 51.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-20% POLYETHYLENE GLYCOL 6000, 25
REMARK 280 MM MES BUFFER, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 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: 4420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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: 4500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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 1duz_D,1duz_E
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 1duz_A,1duz_B
REMARK 410
REMARK 410 ligand(s)
REMARK 410 Tax peptide 11-19 (Q82235)
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Human T-cell leukemia virus type I
REMARK 410 Chain ID
REMARK 410 1duz_F
REMARK 410
REMARK 410 ligand(s)
REMARK 410 Tax peptide 11-19 (Q82235)
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Human T-cell leukemia virus type I
REMARK 410 Chain ID
REMARK 410 1duz_C
REMARK 410
REMARK 410
REMARK 410 Chain ID 1duz_D (1DUZD)
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 1duz_E (1DUZE)
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 1duz_A (1DUZA)
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 1duz_B (1DUZB)
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: 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 O ASP B 96 N ASP B 98 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 147 CB TRP A 147 CG 0.124
REMARK 500 TYR A 159 CD1 TYR A 159 CE1 0.104
REMARK 500 GLU A 173 CG GLU A 173 CD 0.091
REMARK 500 TYR B 26 CD1 TYR B 26 CE1 0.109
REMARK 500 VAL B 37 CB VAL B 37 CG1 0.133
REMARK 500 GLU B 44 CG GLU B 44 CD 0.095
REMARK 500 TYR C 8 CD1 TYR C 8 CE1 0.091
REMARK 500 GLY D 1 N GLY D 1 CA 0.100
REMARK 500 THR D 190 CB THR D 190 CG2 -0.199
REMARK 500 PHE D 241 CE2 PHE D 241 CD2 0.123
REMARK 500 VAL E 9 CB VAL E 9 CG2 0.147
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 5 CA - CB - CG ANGL. DEV. = 13.1 DEGREES
REMARK 500 MET A 5 CG - SD - CE ANGL. DEV. = -18.4 DEGREES
REMARK 500 ARG A 14 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 61 CB - CG - OD1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 220 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 256 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 256 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 273 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 97 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP D 30 CB - CG - OD1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP D 39 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG D 108 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG D 108 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG D 111 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG D 111 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 LYS D 144 CD - CE - NZ ANGL. DEV. = 17.0 DEGREES
REMARK 500 ARG D 157 CG - CD - NE ANGL. DEV. = -17.1 DEGREES
REMARK 500 ARG D 157 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG D 169 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG D 169 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG D 219 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D 256 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP E 34 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG E 45 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG E 45 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 LYS E 48 CD - CE - NZ ANGL. DEV. = -21.3 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 PRO A 15 116.25 -36.89
REMARK 500 ARG A 17 35.00 -69.74
REMARK 500 ASP A 29 -125.38 48.31
REMARK 500 HIS A 114 111.05 -160.77
REMARK 500 THR A 178 -75.85 -78.30
REMARK 500 ASN B 21 -166.44 -162.15
REMARK 500 PRO B 32 -179.71 -67.97
REMARK 500 TRP B 60 -7.33 80.63
REMARK 500 ARG B 97 -13.55 -36.84
REMARK 500 ASP D 29 -130.20 48.26
REMARK 500 TRP D 107 18.05 59.24
REMARK 500 HIS D 114 99.32 -163.09
REMARK 500 THR D 178 -68.23 -93.43
REMARK 500 SER D 195 -172.99 176.95
REMARK 500 SER D 207 49.11 38.78
REMARK 500 TRP E 60 -7.77 74.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR D 123 0.06 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 632 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH D 716 DISTANCE = 7.36 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HHK RELATED DB: PDB
REMARK 900 2.5 ANGSTROMS RESOLUTION STRUCTURE
REMARK 900 RELATED ID: 1DUY RELATED DB: PDB
DBREF 1DUZ A 1 275 UNP P01892 1A02_HUMAN 25 299
DBREF 1DUZ B 0 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 1DUZ D 1 275 UNP P01892 1A02_HUMAN 25 299
DBREF 1DUZ E 0 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 1DUZ C 1 9 PDB 1DUZ 1DUZ 1 9
DBREF 1DUZ F 1 9 PDB 1DUZ 1DUZ 1 9
SEQADV 1DUZ MET B 1 UNP P61769 ALA 11 CONFLICT
SEQADV 1DUZ MET E 1 UNP P61769 ALA 11 CONFLICT
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 LEU LEU PHE GLY TYR PRO VAL TYR 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 LEU LEU PHE GLY TYR PRO VAL TYR VAL
FORMUL 7 HOH *608(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 1051 ALA A 1061A 1 12
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 N VAL A1005 O 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 O GLU A2079 N 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 O ARG A2043 N 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 N LEU A2117 O 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 N GLU B1079 O 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 N VAL D1005 O 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 ALA D2010 0
SHEET 2 I 4 GLU D2018 PHE D2028 -1 N THR D2020 O HIS D2009
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 ALA D2010 0
SHEET 2 J 4 GLU D2018 PHE D2028 -1 N THR D2020 O HIS D2009
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 LEU D2119 -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 N GLU E1079 O 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 N LYS E1117 O 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 -0.13
CISPEP 2 HIS B 1029 PRO B 1030 0 -0.50
CISPEP 3 TYR D 2029 PRO D 2030 0 0.76
CISPEP 4 HIS E 1029 PRO E 1030 0 -0.22
CRYST1 50.560 63.790 75.080 81.58 75.66 77.38 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 0.019778 -0.004428 -0.004646 0.00000
SCALE2 0.000000 0.016065 -0.001576 0.00000
SCALE3 0.000000 0.000000 0.013813 0.00000
ATOM 1 N GLY A 1 14.752 -6.145 13.692 1.00 25.90 N
ATOM 2 CA GLY A 1 15.556 -5.512 12.629 1.00 26.24 C
ATOM 3 C GLY A 1 15.173 -4.015 12.551 1.00 25.34 C
ATOM 4 O GLY A 1 14.683 -3.476 13.556 1.00 26.37 O
ATOM 5 N SER A 2 15.385 -3.415 11.390 1.00 24.50 N
ATOM 6 CA SER A 2 15.117 -1.999 11.027 1.00 23.82 C
ATOM 7 C SER A 2 13.621 -1.646 10.953 1.00 21.82 C
ATOM 8 O SER A 2 12.801 -2.540 10.698 1.00 20.40 O
ATOM 9 CB SER A 2 15.721 -1.709 9.635 1.00 24.56 C
ATOM 10 OG SER A 2 17.138 -1.917 9.705 1.00 29.71 O
ATOM 11 N HIS A 3 13.271 -0.356 11.200 1.00 20.13 N
ATOM 12 CA HIS A 3 11.821 0.031 11.153 1.00 18.92 C
ATOM 13 C HIS A 3 11.657 1.450 10.570 1.00 18.05 C
ATOM 14 O HIS A 3 12.661 2.139 10.422 1.00 17.09 O
ATOM 15 CB HIS A 3 11.225 0.000 12.561 1.00 18.31 C
ATOM 16 CG HIS A 3 11.161 -1.410 13.108 1.00 17.87 C
ATOM 17 ND1 HIS A 3 10.185 -2.297 12.725 1.00 18.42 N
ATOM 18 CD2 HIS A 3 11.937 -2.071 13.989 1.00 19.01 C
ATOM 19 CE1 HIS A 3 10.362 -3.467 13.333 1.00 19.54 C
ATOM 20 NE2 HIS A 3 11.415 -3.344 14.121 1.00 19.01 N
ATOM 21 N SER A 4 10.440 1.783 10.052 1.00 16.94 N
ATOM 22 CA SER A 4 10.259 3.123 9.561 1.00 17.04 C
ATOM 23 C SER A 4 8.878 3.631 9.966 1.00 16.18 C
ATOM 24 O SER A 4 8.046 2.858 10.268 1.00 15.59 O
ATOM 25 CB SER A 4 10.276 3.126 8.026 1.00 16.67 C
ATOM 26 OG SER A 4 9.273 2.229 7.524 1.00 17.32 O
ATOM 27 N MET A 5 8.700 4.945 9.926 1.00 16.37 N
ATOM 28 CA MET A 5 7.420 5.604 10.156 1.00 17.35 C
ATOM 29 C MET A 5 7.223 6.519 8.917 1.00 17.08 C
ATOM 30 O MET A 5 8.172 7.224 8.460 1.00 17.55 O
ATOM 31 CB MET A 5 7.487 6.522 11.396 1.00 18.89 C
ATOM 32 CG MET A 5 7.026 6.177 12.793 1.00 23.71 C
ATOM 33 SD MET A 5 5.662 7.509 13.181 1.00 23.68 S
ATOM 34 CE MET A 5 5.343 7.313 11.482 1.00 22.38 C
ATOM 35 N ARG A 6 6.039 6.530 8.293 1.00 16.73 N
ATOM 36 CA ARG A 6 5.872 7.414 7.112 1.00 15.93 C
ATOM 37 C ARG A 6 4.437 8.026 7.140 1.00 16.07 C
ATOM 38 O ARG A 6 3.517 7.283 7.417 1.00 15.20 O
ATOM 39 CB ARG A 6 5.904 6.633 5.801 1.00 17.04 C
ATOM 40 CG ARG A 6 7.218 6.055 5.363 1.00 18.71 C
ATOM 41 CD ARG A 6 8.164 7.111 4.857 1.00 20.48 C
ATOM 42 NE ARG A 6 9.395 6.466 4.409 1.00 22.10 N
ATOM 43 CZ ARG A 6 10.423 6.075 5.178 1.00 23.42 C
ATOM 44 NH1 ARG A 6 10.451 6.265 6.496 1.00 23.22 N
ATOM 45 NH2 ARG A 6 11.413 5.400 4.609 1.00 24.26 N
ATOM 46 N TYR A 7 4.307 9.328 6.810 1.00 15.42 N
ATOM 47 CA TYR A 7 3.013 9.872 6.646 1.00 14.90 C
ATOM 48 C TYR A 7 2.935 10.193 5.087 1.00 14.90 C
ATOM 49 O TYR A 7 3.882 10.785 4.560 1.00 15.20 O
ATOM 50 CB TYR A 7 2.835 11.148 7.434 1.00 14.53 C
ATOM 51 CG TYR A 7 2.562 10.816 8.888 1.00 14.98 C
ATOM 52 CD1 TYR A 7 1.288 10.445 9.292 1.00 15.60 C
ATOM 53 CD2 TYR A 7 3.589 10.879 9.824 1.00 15.91 C
ATOM 54 CE1 TYR A 7 0.996 10.147 10.701 1.00 15.76 C
ATOM 55 CE2 TYR A 7 3.361 10.584 11.246 1.00 14.81 C
ATOM 56 CZ TYR A 7 2.058 10.233 11.650 1.00 16.36 C
ATOM 57 OH TYR A 7 1.820 9.982 12.984 1.00 15.04 O
ATOM 58 N PHE A 8 1.790 9.879 4.444 1.00 14.51 N
ATOM 59 CA PHE A 8 1.518 10.156 3.006 1.00 15.24 C
ATOM 60 C PHE A 8 0.290 11.097 2.937 1.00 16.21 C
ATOM 61 O PHE A 8 -0.798 10.822 3.601 1.00 16.55 O
ATOM 62 CB PHE A 8 1.185 8.850 2.293 1.00 16.15 C
ATOM 63 CG PHE A 8 2.250 7.866 2.392 1.00 17.18 C
ATOM 64 CD1 PHE A 8 3.325 7.878 1.533 1.00 19.92 C
ATOM 65 CD2 PHE A 8 2.212 6.879 3.358 1.00 19.55 C
ATOM 66 CE1 PHE A 8 4.344 6.872 1.644 1.00 18.68 C
ATOM 67 CE2 PHE A 8 3.263 5.874 3.443 1.00 19.94 C
ATOM 68 CZ PHE A 8 4.286 5.921 2.571 1.00 18.84 C
ATOM 69 N PHE A 9 0.425 12.199 2.171 1.00 15.63 N
ATOM 70 CA PHE A 9 -0.690 13.214 2.098 1.00 15.01 C
ATOM 71 C PHE A 9 -0.962 13.484 0.604 1.00 14.71 C
ATOM 72 O PHE A 9 0.004 13.663 -0.152 1.00 14.82 O
ATOM 73 CB PHE A 9 -0.174 14.532 2.704 1.00 15.80 C
ATOM 74 CG PHE A 9 0.311 14.413 4.138 1.00 15.78 C
ATOM 75 CD1 PHE A 9 -0.610 14.518 5.198 1.00 16.22 C
ATOM 76 CD2 PHE A 9 1.670 14.239 4.419 1.00 15.78 C
ATOM 77 CE1 PHE A 9 -0.128 14.459 6.561 1.00 15.79 C
ATOM 78 CE2 PHE A 9 2.135 14.182 5.730 1.00 15.49 C
ATOM 79 CZ PHE A 9 1.261 14.290 6.778 1.00 16.09 C
ATOM 80 N THR A 10 -2.233 13.453 0.200 1.00 15.34 N
ATOM 81 CA THR A 10 -2.599 13.713 -1.188 1.00 15.51 C
ATOM 82 C THR A 10 -3.689 14.797 -1.140 1.00 16.67 C
ATOM 83 O THR A 10 -4.709 14.549 -0.491 1.00 16.50 O
ATOM 84 CB THR A 10 -3.259 12.459 -1.784 1.00 16.24 C
ATOM 85 OG1 THR A 10 -2.349 11.307 -1.683 1.00 14.83 O
ATOM 86 CG2 THR A 10 -3.655 12.734 -3.240 1.00 14.58 C
ATOM 87 N SER A 11 -3.544 15.857 -1.950 1.00 17.81 N
ATOM 88 CA SER A 11 -4.565 16.897 -2.016 1.00 19.18 C
ATOM 89 C SER A 11 -4.925 17.048 -3.480 1.00 18.60 C
ATOM 90 O SER A 11 -4.012 17.164 -4.293 1.00 18.71 O
ATOM 91 CB SER A 11 -4.012 18.225 -1.433 1.00 21.08 C
ATOM 92 OG SER A 11 -5.154 19.080 -1.185 1.00 26.60 O
ATOM 93 N VAL A 12 -6.220 16.984 -3.842 1.00 18.08 N
ATOM 94 CA VAL A 12 -6.605 17.062 -5.270 1.00 18.38 C
ATOM 95 C VAL A 12 -7.639 18.209 -5.434 1.00 19.62 C
ATOM 96 O VAL A 12 -8.637 18.236 -4.720 1.00 19.29 O
ATOM 97 CB VAL A 12 -7.273 15.732 -5.684 1.00 18.61 C
ATOM 98 CG1 VAL A 12 -7.813 15.811 -7.129 1.00 18.50 C
ATOM 99 CG2 VAL A 12 -6.224 14.481 -5.503 1.00 18.54 C
ATOM 100 N SER A 13 -7.392 19.159 -6.314 1.00 20.10 N
ATOM 101 CA SER A 13 -8.339 20.288 -6.496 1.00 20.80 C
ATOM 102 C SER A 13 -9.492 19.809 -7.317 1.00 22.33 C
ATOM 103 O SER A 13 -9.350 18.885 -8.134 1.00 21.41 O
ATOM 104 CB SER A 13 -7.679 21.485 -7.168 1.00 19.76 C
ATOM 105 OG SER A 13 -7.038 21.150 -8.383 1.00 19.53 O
ATOM 106 N ARG A 14 -10.624 20.459 -7.096 1.00 24.51 N
ATOM 107 CA ARG A 14 -11.854 20.061 -7.740 1.00 27.89 C
ATOM 108 C ARG A 14 -12.580 21.326 -8.206 1.00 29.48 C
ATOM 109 O ARG A 14 -13.642 21.618 -7.695 1.00 29.52 O
ATOM 110 CB ARG A 14 -12.760 19.400 -6.720 1.00 28.97 C
ATOM 111 CG ARG A 14 -12.148 18.226 -6.064 1.00 31.47 C
ATOM 112 CD ARG A 14 -13.208 17.498 -5.262 1.00 32.91 C
ATOM 113 NE ARG A 14 -13.334 17.915 -3.840 1.00 33.89 N
ATOM 114 CZ ARG A 14 -13.609 17.028 -2.904 1.00 33.98 C
ATOM 115 NH1 ARG A 14 -13.760 15.779 -3.305 1.00 34.17 N
ATOM 116 NH2 ARG A 14 -13.752 17.350 -1.626 1.00 33.79 N
ATOM 117 N PRO A 15 -11.997 22.074 -9.148 1.00 30.71 N
ATOM 118 CA PRO A 15 -12.562 23.329 -9.695 1.00 32.20 C
ATOM 119 C PRO A 15 -14.076 23.288 -9.837 1.00 33.38 C
ATOM 120 O PRO A 15 -14.619 22.414 -10.552 1.00 33.38 O
ATOM 121 CB PRO A 15 -11.856 23.454 -11.018 1.00 31.57 C
ATOM 122 CG PRO A 15 -10.412 22.971 -10.579 1.00 31.59 C
ATOM 123 CD PRO A 15 -10.767 21.686 -9.866 1.00 31.04 C
ATOM 124 N GLY A 16 -14.722 24.180 -9.060 1.00 34.87 N
ATOM 125 CA GLY A 16 -16.178 24.289 -8.991 1.00 37.17 C
ATOM 126 C GLY A 16 -16.820 23.426 -7.910 1.00 38.36 C
ATOM 127 O GLY A 16 -17.572 23.904 -7.053 1.00 39.53 O
ATOM 128 N ARG A 17 -16.513 22.138 -7.948 1.00 39.07 N
ATOM 129 CA ARG A 17 -17.061 21.174 -7.028 1.00 38.75 C
ATOM 130 C ARG A 17 -16.571 21.288 -5.563 1.00 38.30 C
ATOM 131 O ARG A 17 -16.396 20.252 -4.888 1.00 38.48 O
ATOM 132 CB ARG A 17 -16.764 19.805 -7.602 1.00 39.47 C
ATOM 133 CG ARG A 17 -17.209 19.695 -9.041 1.00 41.32 C
ATOM 134 CD ARG A 17 -16.834 18.364 -9.719 1.00 42.41 C
ATOM 135 NE ARG A 17 -15.392 18.049 -9.792 1.00 43.86 N
ATOM 136 CZ ARG A 17 -14.835 16.931 -9.264 1.00 44.24 C
ATOM 137 NH1 ARG A 17 -15.588 16.009 -8.594 1.00 44.28 N
ATOM 138 NH2 ARG A 17 -13.540 16.680 -9.480 1.00 44.25 N
ATOM 139 N GLY A 18 -16.329 22.520 -5.082 1.00 37.23 N
ATOM 140 CA GLY A 18 -15.896 22.739 -3.697 1.00 35.85 C
ATOM 141 C GLY A 18 -14.416 22.667 -3.288 1.00 34.44 C
ATOM 142 O GLY A 18 -13.541 22.729 -4.125 1.00 34.91 O
ATOM 143 N GLU A 19 -14.153 22.537 -1.994 1.00 32.82 N
ATOM 144 CA GLU A 19 -12.776 22.497 -1.485 1.00 31.36 C
ATOM 145 C GLU A 19 -12.049 21.261 -2.043 1.00 29.34 C
ATOM 146 O GLU A 19 -12.683 20.276 -2.407 1.00 27.93 O
ATOM 147 CB GLU A 19 -12.764 22.320 0.055 1.00 33.61 C
ATOM 148 CG GLU A 19 -13.241 23.452 0.867 1.00 36.29 C
ATOM 149 CD GLU A 19 -12.536 24.713 0.488 1.00 38.36 C
ATOM 150 OE1 GLU A 19 -11.376 24.884 0.914 1.00 39.68 O
ATOM 151 OE2 GLU A 19 -13.139 25.520 -0.263 1.00 40.14 O
ATOM 152 N PRO A 20 -10.723 21.304 -2.065 1.00 27.75 N
ATOM 153 CA PRO A 20 -9.993 20.135 -2.569 1.00 26.78 C
ATOM 154 C PRO A 20 -10.150 18.884 -1.638 1.00 25.90 C
ATOM 155 O PRO A 20 -10.408 19.006 -0.419 1.00 25.74 O
ATOM 156 CB PRO A 20 -8.522 20.600 -2.591 1.00 26.87 C
ATOM 157 CG PRO A 20 -8.571 22.107 -2.510 1.00 27.91 C
ATOM 158 CD PRO A 20 -9.805 22.370 -1.642 1.00 27.62 C
ATOM 159 N ARG A 21 -10.022 17.697 -2.204 1.00 24.80 N
ATOM 160 CA ARG A 21 -10.071 16.472 -1.410 1.00 24.51 C
ATOM 161 C ARG A 21 -8.710 16.335 -0.712 1.00 23.45 C
ATOM 162 O ARG A 21 -7.668 16.594 -1.359 1.00 24.53 O
ATOM 163 CB ARG A 21 -10.249 15.251 -2.308 1.00 26.30 C
ATOM 164 CG ARG A 21 -10.344 13.880 -1.539 1.00 27.85 C
ATOM 165 CD ARG A 21 -11.763 13.500 -1.301 1.00 29.74 C
ATOM 166 NE ARG A 21 -12.026 12.285 -0.530 1.00 31.07 N
ATOM 167 CZ ARG A 21 -12.571 11.207 -1.070 1.00 32.77 C
ATOM 168 NH1 ARG A 21 -12.892 11.180 -2.386 1.00 32.95 N
ATOM 169 NH2 ARG A 21 -12.834 10.164 -0.300 1.00 33.98 N
ATOM 170 N PHE A 22 -8.676 15.962 0.561 1.00 20.92 N
ATOM 171 CA PHE A 22 -7.363 15.851 1.209 1.00 20.60 C
ATOM 172 C PHE A 22 -7.418 14.501 1.967 1.00 19.24 C
ATOM 173 O PHE A 22 -8.353 14.281 2.755 1.00 18.41 O
ATOM 174 CB PHE A 22 -7.148 17.028 2.168 1.00 20.35 C
ATOM 175 CG PHE A 22 -6.071 16.776 3.149 1.00 22.30 C
ATOM 176 CD1 PHE A 22 -4.727 17.012 2.800 1.00 21.73 C
ATOM 177 CD2 PHE A 22 -6.399 16.334 4.444 1.00 21.98 C
ATOM 178 CE1 PHE A 22 -3.665 16.808 3.734 1.00 22.59 C
ATOM 179 CE2 PHE A 22 -5.370 16.129 5.392 1.00 23.07 C
ATOM 180 CZ PHE A 22 -3.990 16.361 5.034 1.00 21.56 C
ATOM 181 N ILE A 23 -6.480 13.599 1.704 1.00 18.02 N
ATOM 182 CA ILE A 23 -6.457 12.304 2.375 1.00 17.35 C
ATOM 183 C ILE A 23 -5.060 12.113 3.019 1.00 17.33 C
ATOM 184 O ILE A 23 -4.062 12.346 2.344 1.00 18.39 O
ATOM 185 CB ILE A 23 -6.675 11.174 1.373 1.00 18.58 C
ATOM 186 CG1 ILE A 23 -8.093 11.282 0.763 1.00 19.80 C
ATOM 187 CG2 ILE A 23 -6.646 9.876 2.096 1.00 19.41 C
ATOM 188 CD1 ILE A 23 -8.399 10.041 -0.165 1.00 23.40 C
ATOM 189 N ALA A 24 -4.987 11.760 4.314 1.00 16.20 N
ATOM 190 CA ALA A 24 -3.683 11.560 4.948 1.00 15.82 C
ATOM 191 C ALA A 24 -3.711 10.146 5.495 1.00 15.21 C
ATOM 192 O ALA A 24 -4.688 9.737 6.110 1.00 14.88 O
ATOM 193 CB ALA A 24 -3.408 12.570 6.186 1.00 14.97 C
ATOM 194 N VAL A 25 -2.584 9.444 5.394 1.00 15.11 N
ATOM 195 CA VAL A 25 -2.465 8.133 6.014 1.00 14.87 C
ATOM 196 C VAL A 25 -1.068 7.991 6.694 1.00 15.54 C
ATOM 197 O VAL A 25 -0.079 8.590 6.272 1.00 14.79 O
ATOM 198 CB VAL A 25 -2.697 6.913 5.008 1.00 15.62 C
ATOM 199 CG1 VAL A 25 -4.144 6.926 4.498 1.00 15.26 C
ATOM 200 CG2 VAL A 25 -1.753 7.038 3.840 1.00 15.66 C
ATOM 201 N GLY A 26 -1.019 7.251 7.801 1.00 14.60 N
ATOM 202 CA GLY A 26 0.275 7.020 8.458 1.00 13.63 C
ATOM 203 C GLY A 26 0.594 5.512 8.534 1.00 13.97 C
ATOM 204 O GLY A 26 -0.352 4.673 8.708 1.00 14.13 O
ATOM 205 N TYR A 27 1.884 5.144 8.376 1.00 13.35 N
ATOM 206 CA TYR A 27 2.265 3.738 8.446 1.00 14.03 C
ATOM 207 C TYR A 27 3.459 3.525 9.369 1.00 13.82 C
ATOM 208 O TYR A 27 4.315 4.458 9.502 1.00 13.28 O
ATOM 209 CB TYR A 27 2.751 3.178 7.061 1.00 14.88 C
ATOM 210 CG TYR A 27 1.619 2.890 6.086 1.00 16.65 C
ATOM 211 CD1 TYR A 27 0.983 3.934 5.390 1.00 15.98 C
ATOM 212 CD2 TYR A 27 1.218 1.565 5.811 1.00 16.91 C
ATOM 213 CE1 TYR A 27 -0.014 3.648 4.479 1.00 17.45 C
ATOM 214 CE2 TYR A 27 0.194 1.299 4.866 1.00 17.44 C
ATOM 215 CZ TYR A 27 -0.400 2.371 4.226 1.00 18.48 C
ATOM 216 OH TYR A 27 -1.427 2.117 3.245 1.00 21.74 O
ATOM 217 N VAL A 28 3.496 2.364 10.032 1.00 14.17 N
ATOM 218 CA VAL A 28 4.724 1.936 10.706 1.00 14.76 C
ATOM 219 C VAL A 28 5.053 0.625 9.891 1.00 14.65 C
ATOM 220 O VAL A 28 4.218 -0.291 9.752 1.00 14.64 O
ATOM 221 CB VAL A 28 4.595 1.637 12.244 1.00 14.66 C
ATOM 222 CG1 VAL A 28 5.946 0.928 12.737 1.00 13.00 C
ATOM 223 CG2 VAL A 28 4.633 2.973 13.006 1.00 14.28 C
ATOM 224 N ASP A 29 6.267 0.580 9.335 1.00 14.61 N
ATOM 225 CA ASP A 29 6.602 -0.508 8.407 1.00 15.31 C
ATOM 226 C ASP A 29 5.453 -0.686 7.321 1.00 14.95 C
ATOM 227 O ASP A 29 5.123 0.270 6.644 1.00 15.02 O
ATOM 228 CB ASP A 29 6.833 -1.762 9.239 1.00 15.99 C
ATOM 229 CG ASP A 29 7.984 -1.554 10.237 1.00 18.14 C
ATOM 230 OD1 ASP A 29 8.910 -0.796 9.858 1.00 17.30 O
ATOM 231 OD2 ASP A 29 7.998 -2.160 11.353 1.00 19.23 O
ATOM 232 N ASP A 30 4.900 -1.888 7.175 1.00 15.15 N
ATOM 233 CA ASP A 30 3.844 -2.150 6.225 1.00 15.92 C
ATOM 234 C ASP A 30 2.433 -2.203 6.865 1.00 14.93 C
ATOM 235 O ASP A 30 1.462 -2.715 6.231 1.00 15.50 O
ATOM 236 CB ASP A 30 4.097 -3.469 5.463 1.00 17.35 C
ATOM 237 CG ASP A 30 5.424 -3.439 4.696 1.00 19.01 C
ATOM 238 OD1 ASP A 30 5.737 -2.379 4.100 1.00 18.81 O
ATOM 239 OD2 ASP A 30 6.104 -4.469 4.732 1.00 19.26 O
ATOM 240 N THR A 31 2.305 -1.596 8.038 1.00 15.23 N
ATOM 241 CA THR A 31 0.975 -1.612 8.737 1.00 15.07 C
ATOM 242 C THR A 31 0.429 -0.180 8.820 1.00 13.96 C
ATOM 243 O THR A 31 1.070 0.678 9.360 1.00 13.94 O
ATOM 244 CB THR A 31 1.192 -2.208 10.151 1.00 15.87 C
ATOM 245 OG1 THR A 31 1.656 -3.567 9.992 1.00 15.93 O
ATOM 246 CG2 THR A 31 -0.102 -2.235 11.003 1.00 16.31 C
ATOM 247 N GLN A 32 -0.757 0.028 8.276 1.00 14.42 N
ATOM 248 CA GLN A 32 -1.361 1.383 8.321 1.00 14.02 C
ATOM 249 C GLN A 32 -1.815 1.582 9.780 1.00 14.86 C
ATOM 250 O GLN A 32 -2.245 0.578 10.339 1.00 14.42 O
ATOM 251 CB GLN A 32 -2.575 1.387 7.416 1.00 15.65 C
ATOM 252 CG GLN A 32 -2.924 2.833 7.045 1.00 15.06 C