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1N3N.pdb
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HEADER IMMUNE SYSTEM 29-OCT-02 1N3N
TITLE CRYSTAL STRUCTURE OF A MYCOBACTERIAL HSP60 EPITOPE WITH THE
TITLE 2 MURINE CLASS I MHC MOLECULE H-2DB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-B
COMPND 3 ALPHA CHAIN;
COMPND 4 CHAIN: A, C, E, G;
COMPND 5 FRAGMENT: EXTRACELLULAR DOMAINS;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: MYCOBACTERIAL HSP60 DECAMERIC EPITOPE;
COMPND 13 CHAIN: I, J, K, L;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 9 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 10 ORGANISM_TAXID: 10090;
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: SOLID-PHASE PEPTIDE SYNTHESIS
KEYWDS IMMUNOGLOBULIN FOLD, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CIATTO,G.CAPITANI,A.C.TISSOT,F.PECORARI,A.PLUCKTHUN,
AUTHOR 2 M.G.GRUTTER
REVDAT 2 24-FEB-09 1N3N 1 VERSN
REVDAT 1 27-MAY-03 1N3N 0
JRNL AUTH C.CIATTO,G.CAPITANI,A.C.TISSOT,F.PECORARI,
JRNL AUTH 2 A.PLUECKTHUN,M.G.GRUETTER
JRNL TITL STRUCTURAL ANALYSIS OF MYCOBACTERIAL AND MURINE
JRNL TITL 2 HSP60 EPITOPES IN COMPLEX WITH THE CLASS I MHC
JRNL TITL 3 MOLECULE H-2D(B)
JRNL REF FEBS LETT. V. 543 11 2003
JRNL REFN ISSN 0014-5793
JRNL PMID 12753896
JRNL DOI 10.1016/S0014-5793(03)00325-9
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 44948
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) : 0.246
REMARK 3 FREE R VALUE : 0.307
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1336
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 : 12604
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 189
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.54
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: NULL
REMARK 4
REMARK 4 1N3N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-02.
REMARK 100 THE RCSB ID CODE IS RCSB017477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.872
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
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 : 47412
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
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) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIM SULFATE, GLYCEROL, TRIS, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 64.63800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.49750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.63800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 61.49750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY CONSISTS
REMARK 300 OF ONE ALPHA CHAIN, ONE BETA-2
REMARK 300 MICROGLOBULIN CHAIN, AND A BOUND
REMARK 300 PEPTIDE ANTIGEN
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: 3940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I
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: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, L
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: 3
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: 4270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, K
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: 4
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: 3990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, L
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 APPLY THE FOLLOWING TO CHAINS: C, D, J
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 129.24967
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 150.83300
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, K
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 APPLY THE FOLLOWING TO CHAINS: A, B, I
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 129.24967
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 150.83300
REMARK 410
REMARK 410 IMGT/3Dstructure-DB annotations
REMARK 410 (http://www.imgt.org)
REMARK 410
REMARK 410 ligand(s)
REMARK 410 HSP60 epitope peptide
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Chain ID
REMARK 410 1n3n_I
REMARK 410
REMARK 410 ligand(s)
REMARK 410 HSP60 epitope peptide
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Chain ID
REMARK 410 1n3n_L
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1-D1b (H2-D1b)
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Mus musculus (house mouse)
REMARK 410 Chain ID
REMARK 410 1n3n_G,1n3n_H
REMARK 410
REMARK 410 ligand(s)
REMARK 410 HSP60 epitope peptide
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Chain ID
REMARK 410 1n3n_J
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1-D1b (H2-D1b)
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Mus musculus (house mouse)
REMARK 410 Chain ID
REMARK 410 1n3n_A,1n3n_B
REMARK 410
REMARK 410 ligand(s)
REMARK 410 HSP60 epitope peptide
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Chain ID
REMARK 410 1n3n_K
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1-D1b (H2-D1b)
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Mus musculus (house mouse)
REMARK 410 Chain ID
REMARK 410 1n3n_E,1n3n_F
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1-D1b (H2-D1b)
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Mus musculus (house mouse)
REMARK 410 Chain ID
REMARK 410 1n3n_C,1n3n_D
REMARK 410
REMARK 410
REMARK 410 Chain ID 1n3n_G (1N3NG)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQK
REMARK 410 ][ G-ALPHA
REMARK 410 AKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKT
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGE
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHE
REMARK 410 ]
REMARK 410 GLPEPLTLRWEPPPST
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 G-DOMAIN ..........GPHSMRY.FETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAE
REMARK 410 G-DOMAIN NPRYEPRA.......PWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYN
REMARK 410 G-DOMAIN QSAG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 G-DOMAIN ..........GSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNED..L
REMARK 410 G-DOMAIN KTWTAAD.......MAAQITRRKWEQS.GAAEHYKAYLEGECVEWLHRYLKN
REMARK 410 G-DOMAIN GNATLLRT.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DSPKAHVTHHPRSK......GEVTLRCWALGFYP..ADITLTWQL
REMARK 410 C-LIKE-DOMAIN NGEELTQ..DMELVETRPAGD......GTFQKWASVVVPLG.....KEQNYT
REMARK 410 C-LIKE-DOMAIN CRVYHEG..LPEPLTLRW
REMARK 410
REMARK 410 Chain ID 1n3n_H (1N3NH)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (1-99) [D1]
REMARK 410 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILA
REMARK 410 ]
REMARK 410 HTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus B2M*01 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQKTPQIQVYSRHPPEN....GKPNILNCYVTQFHP..PHIEIQMLK
REMARK 410 C-LIKE-DOMAIN NGKKIP...KVEMSDMSFSKD......WSFYILAHTEFTPTE.....TDTYA
REMARK 410 C-LIKE-DOMAIN CRVKHDS..MAEPKTVYWDRDM
REMARK 410
REMARK 410 Chain ID 1n3n_A (1N3NA)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQK
REMARK 410 ][ G-ALPHA
REMARK 410 AKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKT
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGE
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHE
REMARK 410 ]
REMARK 410 GLPEPLTLRWEPPPST
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 G-DOMAIN ..........GPHSMRY.FETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAE
REMARK 410 G-DOMAIN NPRYEPRA.......PWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYN
REMARK 410 G-DOMAIN QSAG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 G-DOMAIN ..........GSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNED..L
REMARK 410 G-DOMAIN KTWTAAD.......MAAQITRRKWEQS.GAAEHYKAYLEGECVEWLHRYLKN
REMARK 410 G-DOMAIN GNATLLRT.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DSPKAHVTHHPRSK......GEVTLRCWALGFYP..ADITLTWQL
REMARK 410 C-LIKE-DOMAIN NGEELTQ..DMELVETRPAGD......GTFQKWASVVVPLG.....KEQNYT
REMARK 410 C-LIKE-DOMAIN CRVYHEG..LPEPLTLRW
REMARK 410
REMARK 410 Chain ID 1n3n_B (1N3NB)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (1-99) [D1]
REMARK 410 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILA
REMARK 410 ]
REMARK 410 HTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus B2M*01 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQKTPQIQVYSRHPPEN....GKPNILNCYVTQFHP..PHIEIQMLK
REMARK 410 C-LIKE-DOMAIN NGKKIP...KVEMSDMSFSKD......WSFYILAHTEFTPTE.....TDTYA
REMARK 410 C-LIKE-DOMAIN CRVKHDS..MAEPKTVYWDRDM
REMARK 410
REMARK 410 Chain ID 1n3n_E (1N3NE)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQK
REMARK 410 ][ G-ALPHA
REMARK 410 AKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKT
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGE
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHE
REMARK 410 ]
REMARK 410 GLPEPLTLRWEPPPST
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 G-DOMAIN ..........GPHSMRY.FETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAE
REMARK 410 G-DOMAIN NPRYEPRA.......PWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYN
REMARK 410 G-DOMAIN QSAG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 G-DOMAIN ..........GSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNED..L
REMARK 410 G-DOMAIN KTWTAAD.......MAAQITRRKWEQS.GAAEHYKAYLEGECVEWLHRYLKN
REMARK 410 G-DOMAIN GNATLLRT.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DSPKAHVTHHPRSK......GEVTLRCWALGFYP..ADITLTWQL
REMARK 410 C-LIKE-DOMAIN NGEELTQ..DMELVETRPAGD......GTFQKWASVVVPLG.....KEQNYT
REMARK 410 C-LIKE-DOMAIN CRVYHEG..LPEPLTLRW
REMARK 410
REMARK 410 Chain ID 1n3n_F (1N3NF)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (1-99) [D1]
REMARK 410 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILA
REMARK 410 ]
REMARK 410 HTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus B2M*01 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQKTPQIQVYSRHPPEN....GKPNILNCYVTQFHP..PHIEIQMLK
REMARK 410 C-LIKE-DOMAIN NGKKIP...KVEMSDMSFSKD......WSFYILAHTEFTPTE.....TDTYA
REMARK 410 C-LIKE-DOMAIN CRVKHDS..MAEPKTVYWDRDM
REMARK 410
REMARK 410 Chain ID 1n3n_C (1N3NC)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQK
REMARK 410 ][ G-ALPHA
REMARK 410 AKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKT
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGE
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHE
REMARK 410 ]
REMARK 410 GLPEPLTLRWEPPPST
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 G-DOMAIN ..........GPHSMRY.FETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAE
REMARK 410 G-DOMAIN NPRYEPRA.......PWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYN
REMARK 410 G-DOMAIN QSAG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 G-DOMAIN ..........GSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNED..L
REMARK 410 G-DOMAIN KTWTAAD.......MAAQITRRKWEQS.GAAEHYKAYLEGECVEWLHRYLKN
REMARK 410 G-DOMAIN GNATLLRT.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus H2-D1b (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DSPKAHVTHHPRSK......GEVTLRCWALGFYP..ADITLTWQL
REMARK 410 C-LIKE-DOMAIN NGEELTQ..DMELVETRPAGD......GTFQKWASVVVPLG.....KEQNYT
REMARK 410 C-LIKE-DOMAIN CRVYHEG..LPEPLTLRW
REMARK 410
REMARK 410 Chain ID 1n3n_D (1N3ND)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (1-99) [D1]
REMARK 410 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILA
REMARK 410 ]
REMARK 410 HTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus B2M*01 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQKTPQIQVYSRHPPEN....GKPNILNCYVTQFHP..PHIEIQMLK
REMARK 410 C-LIKE-DOMAIN NGKKIP...KVEMSDMSFSKD......WSFYILAHTEFTPTE.....TDTYA
REMARK 410 C-LIKE-DOMAIN CRVKHDS..MAEPKTVYWDRDM
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 277
REMARK 465 PRO A 278
REMARK 465 SER A 279
REMARK 465 THR A 280
REMARK 465 PRO C 277
REMARK 465 PRO C 278
REMARK 465 SER C 279
REMARK 465 THR C 280
REMARK 465 PRO E 277
REMARK 465 PRO E 278
REMARK 465 SER E 279
REMARK 465 THR E 280
REMARK 465 PRO G 277
REMARK 465 PRO G 278
REMARK 465 SER G 279
REMARK 465 THR G 280
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 OE2 GLU A 166 O HOH A 305 2.19
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 CYS A 203 CA - CB - SG ANGL. DEV. = 9.7 DEGREES
REMARK 500 CYS C 203 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 CYS E 203 CA - CB - SG ANGL. DEV. = 6.6 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 LEU A 17 91.75 -59.89
REMARK 500 GLU A 18 -177.58 -52.40
REMARK 500 GLU A 19 94.50 89.53
REMARK 500 PHE A 33 -5.76 -140.44
REMARK 500 ARG A 44 129.94 175.27
REMARK 500 ALA A 49 133.73 -177.03
REMARK 500 MET A 52 -5.74 -51.38
REMARK 500 GLN A 54 34.97 -88.73
REMARK 500 TRP A 107 1.49 80.88
REMARK 500 LEU A 110 -31.30 -141.72
REMARK 500 ASN A 174 -81.09 -71.33
REMARK 500 THR A 178 -24.60 170.42
REMARK 500 LEU A 180 41.70 -96.36
REMARK 500 HIS A 188 153.57 176.92
REMARK 500 SER A 195 -143.04 -172.38
REMARK 500 ASN A 220 65.74 69.54
REMARK 500 THR A 225 44.67 -93.94
REMARK 500 LEU A 230 -155.53 -105.17
REMARK 500 VAL A 231 122.94 173.55
REMARK 500 LEU A 251 135.24 -38.77
REMARK 500 ASN B 21 -163.37 177.21
REMARK 500 HIS B 31 137.36 178.33
REMARK 500 PRO B 32 170.18 -58.82
REMARK 500 PRO B 47 -84.99 -59.41
REMARK 500 MET B 54 119.21 -36.97
REMARK 500 LEU C 17 91.36 -65.50
REMARK 500 GLU C 18 -179.18 -52.17
REMARK 500 GLU C 19 96.01 90.14
REMARK 500 PHE C 33 -10.72 -147.29
REMARK 500 ARG C 44 133.55 173.51
REMARK 500 ALA C 49 129.83 -177.65
REMARK 500 MET C 52 -6.81 -49.98
REMARK 500 GLN C 54 35.48 -92.64
REMARK 500 TYR C 59 -73.48 -57.26
REMARK 500 TRP C 107 -1.90 83.25
REMARK 500 LEU C 110 -30.39 -139.06
REMARK 500 TYR C 123 -60.36 -121.63
REMARK 500 ALA C 177 -98.19 -95.72
REMARK 500 LEU C 180 -46.86 -27.34
REMARK 500 ARG C 181 -168.08 -129.61
REMARK 500 HIS C 188 157.02 177.35
REMARK 500 SER C 195 -143.35 -172.06
REMARK 500 ASN C 220 64.60 70.31
REMARK 500 THR C 225 46.46 -96.04
REMARK 500 LEU C 230 -152.16 -105.47
REMARK 500 VAL C 231 120.85 170.75
REMARK 500 ASN D 21 -163.19 176.59
REMARK 500 GLN D 29 14.34 57.41
REMARK 500 HIS D 31 138.77 -179.70
REMARK 500 PRO D 47 -80.38 -64.86
REMARK 500 PRO D 90 170.95 -49.82
REMARK 500 LEU E 17 123.77 166.18
REMARK 500 GLU E 19 98.87 64.34
REMARK 500 ARG E 44 130.06 177.94
REMARK 500 ALA E 49 132.74 -178.98
REMARK 500 MET E 52 -7.91 -49.43
REMARK 500 GLN E 54 35.48 -91.64
REMARK 500 TRP E 107 -1.33 84.51
REMARK 500 LEU E 110 -33.87 -143.74
REMARK 500 GLN E 149 -8.92 -57.56
REMARK 500 ASN E 176 82.36 -66.38
REMARK 500 ALA E 177 -42.08 -152.35
REMARK 500 THR E 178 -10.03 -165.90
REMARK 500 HIS E 188 155.48 178.65
REMARK 500 SER E 195 -140.41 -170.41
REMARK 500 ASN E 220 63.70 70.08
REMARK 500 THR E 225 44.95 -95.47
REMARK 500 LEU E 230 -153.43 -106.54
REMARK 500 VAL E 231 118.37 171.84
REMARK 500 LEU E 251 137.32 -39.54
REMARK 500 ASN F 17 126.17 -38.52
REMARK 500 ASN F 21 -164.19 179.22
REMARK 500 HIS F 31 138.97 -174.86
REMARK 500 PRO F 47 -85.81 -58.98
REMARK 500 MET F 54 115.79 -39.12
REMARK 500 LYS F 58 -38.92 -39.34
REMARK 500 THR F 73 -165.96 -108.96
REMARK 500 HIS F 84 146.81 -172.00
REMARK 500 PRO F 90 174.58 -51.24
REMARK 500 ARG F 97 -18.51 -49.50
REMARK 500 LEU G 17 124.82 164.87
REMARK 500 GLU G 19 96.43 60.06
REMARK 500 ARG G 44 125.88 175.41
REMARK 500 ALA G 49 138.44 -176.47
REMARK 500 MET G 52 -10.28 -45.19
REMARK 500 GLN G 54 35.88 -89.78
REMARK 500 TRP G 107 -0.00 80.69
REMARK 500 LEU G 110 -34.73 -138.83
REMARK 500 GLN G 149 -6.98 -59.48
REMARK 500 ASN G 176 43.95 -74.04
REMARK 500 ALA G 177 -58.94 -146.87
REMARK 500 LEU G 180 47.59 -66.16
REMARK 500 HIS G 188 155.54 178.79
REMARK 500 SER G 195 -141.87 -169.18
REMARK 500 ASN G 220 62.08 71.95
REMARK 500 THR G 225 44.99 -93.82
REMARK 500 LEU G 230 -153.97 -106.64
REMARK 500 VAL G 231 123.62 171.66
REMARK 500 ASN H 17 126.64 -35.98
REMARK 500 ASN H 21 -162.19 -179.77
REMARK 500 HIS H 31 137.96 -175.01
REMARK 500 PRO H 47 -88.12 -60.76
REMARK 500 MET H 54 114.44 -39.34
REMARK 500 LYS H 58 -39.65 -35.31
REMARK 500 THR H 73 -164.89 -106.08
REMARK 500 HIS H 84 148.46 -173.71
REMARK 500 PRO H 90 174.12 -49.47
REMARK 500 ASN K 5 164.56 -49.12
REMARK 500 ASN L 5 162.21 -45.01
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 C 22 0.08 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 281
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 281
DBREF 1N3N A 1 280 UNP P01899 HA11_MOUSE 25 304
DBREF 1N3N B 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1N3N C 1 280 UNP P01899 HA11_MOUSE 25 304
DBREF 1N3N D 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1N3N E 1 280 UNP P01899 HA11_MOUSE 25 304
DBREF 1N3N F 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1N3N G 1 280 UNP P01899 HA11_MOUSE 25 304
DBREF 1N3N H 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1N3N I 1 10 PDB 1N3N 1N3N 1 10
DBREF 1N3N J 1 10 PDB 1N3N 1N3N 1 10
DBREF 1N3N K 1 10 PDB 1N3N 1N3N 1 10
DBREF 1N3N L 1 10 PDB 1N3N 1N3N 1 10
SEQRES 1 A 280 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 A 280 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 A 280 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 A 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 A 280 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 A 280 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 A 280 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 A 280 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 A 280 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 A 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 A 280 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 A 280 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 A 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 A 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 A 280 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 A 280 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 A 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 A 280 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 A 280 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 A 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 B 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 B 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 B 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 B 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 B 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 B 99 ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO LYS
SEQRES 8 B 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 C 280 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 C 280 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 C 280 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 C 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 C 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 C 280 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 C 280 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 C 280 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 C 280 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 C 280 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 C 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 C 280 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 C 280 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 C 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 C 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 C 280 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 C 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 C 280 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 C 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 C 280 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 C 280 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 C 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 D 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 D 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 D 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 D 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 D 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 D 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 D 99 ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO LYS
SEQRES 8 D 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 E 280 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 E 280 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 E 280 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 E 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 E 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 E 280 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 E 280 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 E 280 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 E 280 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 E 280 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 E 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 E 280 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 E 280 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 E 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 E 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 E 280 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 E 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 E 280 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 E 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 E 280 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 E 280 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 E 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 F 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 F 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 F 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 F 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 F 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 F 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 F 99 ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO LYS
SEQRES 8 F 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 G 280 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 G 280 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 G 280 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 G 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 G 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 G 280 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 G 280 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 G 280 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 G 280 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 G 280 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 G 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 G 280 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 G 280 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 G 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 G 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 G 280 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 G 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 G 280 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 G 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 G 280 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 G 280 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 G 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 H 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 H 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 H 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 H 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 H 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 H 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 H 99 ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO LYS
SEQRES 8 H 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 I 10 SER ALA LEU GLN ASN ALA ALA SER ILE ALA
SEQRES 1 J 10 SER ALA LEU GLN ASN ALA ALA SER ILE ALA
SEQRES 1 K 10 SER ALA LEU GLN ASN ALA ALA SER ILE ALA
SEQRES 1 L 10 SER ALA LEU GLN ASN ALA ALA SER ILE ALA
HET SO4 3 5
HET SO4 3 5
HETNAM SO4 SULFATE ION
FORMUL 13 SO4 2(O4 S 2-)
FORMUL 15 HOH *189(H2 O)
HELIX 1 1 PRO A 50 GLU A 55 5 6
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 ASP A 1049 GLN A 1061 1 13
HELIX 4 4 GLY A 1062 GLY A 1072A 1 12
HELIX 5 5 GLY A 1072A GLY A 1085 1 14
HELIX 6 6 PRO C 50 GLU C 55 5 6
HELIX 7 7 GLY C 56 TYR C 85 1 30
HELIX 8 8 ASP C 1049 GLN C 1061 1 13
HELIX 9 9 GLY C 1062 GLY C 1072A 1 12
HELIX 10 10 GLY C 1072A ASN C 1084 1 13
HELIX 11 11 LYS C 2098 TYR C 2102 5 5
HELIX 12 12 PRO E 50 GLU E 55 5 6
HELIX 13 13 GLY E 56 TYR E 85 1 30
HELIX 14 14 ASP E 1049 GLN E 1061 1 13
HELIX 15 15 GLY E 1062 GLY E 1072A 1 12
HELIX 16 16 GLY E 1072A ASN E 1086 1 15
HELIX 17 17 LYS E 2098 TYR E 2102 5 5
HELIX 18 18 PRO G 50 GLU G 55 5 6
HELIX 19 19 GLY G 56 TYR G 85 1 30
HELIX 20 20 ASP G 1049 GLN G 1061 1 13
HELIX 21 21 GLY G 1062 GLY G 1072A 1 12
HELIX 22 22 GLY G 1072A GLY G 1085 1 14
HELIX 23 23 LYS G 2098 TYR G 2102 5 5
SHEET 1 A 8 GLU A 46 PRO A 47 0
SHEET 2 A 8 LYS A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 A 8 ARG A 21 VAL A 28 -1 N SER A 24 O PHE A 36
SHEET 4 A 8 HIS A 3 SER A 13 -1 N THR A 10 O ILE A 23
SHEET 5 A 8 HIS A1003 LEU A1013 -1 O GLN A1007 N GLU A 9
SHEET 6 A 8 LEU A1019 TYR A1028 -1 O ALA A1027 N GLN A1006
SHEET 7 A 8 ARG A1031 LEU A1036 -1 O ILE A1034 N PHE A1026
SHEET 8 A 8 TRP A1045 ALA A1047 -1 O THR A1046 N ALA A1035
SHEET 1 B 4 LYS A2003 PRO A2010 0
SHEET 2 B 4 GLU A2018 PHE A2028 -1 O THR A2020 N HIS A2009
SHEET 3 B 4 PHE A2085B PRO A2092 -1 O ALA A2087 N CYS A2023
SHEET 4 B 4 ARG A2084 PRO A2084A-1 N ARG A2084 O GLN A2085A
SHEET 1 C 4 GLU A2045A GLU A2045B 0
SHEET 2 C 4 THR A2038 LEU A2043 -1 N LEU A2043 O GLU A2045A
SHEET 3 C 4 THR A2103 TYR A2107 -1 O THR A2103 N GLN A2042
SHEET 4 C 4 LEU A2117 LEU A2119 -1 O LEU A2119 N CYS A2104
SHEET 1 D 4 VAL B 6 SER B 8 0
SHEET 2 D 4 ASN B 19 PHE B 28 -1 O ASN B 22 N TYR B 7
SHEET 3 D 4 PHE B 85B PHE B 91 -1 O ALA B 87 N CYS B 23
SHEET 4 D 4 GLU B 79 MET B 80 -1 N GLU B 79 O HIS B 88
SHEET 1 E 4 VAL B 6 SER B 8 0
SHEET 2 E 4 ASN B 19 PHE B 28 -1 O ASN B 22 N TYR B 7
SHEET 3 E 4 PHE B 85B PHE B 91 -1 O ALA B 87 N CYS B 23
SHEET 4 E 4 SER B 84 PHE B 84A-1 N SER B 84 O TYR B 85A
SHEET 1 F 4 LYS B 45A LYS B 45B 0
SHEET 2 F 4 GLU B 38 LYS B 43 -1 N LYS B 43 O LYS B 45A
SHEET 3 F 4 TYR B 102 LYS B 107 -1 O ALA B 103 N LEU B 42
SHEET 4 F 4 LYS B 117 TYR B 120 -1 O LYS B 117 N VAL B 106
SHEET 1 G 8 GLU C 46 PRO C 47 0
SHEET 2 G 8 LYS C 31 ASP C 37 -1 N ARG C 35 O GLU C 46
SHEET 3 G 8 ARG C 21 VAL C 28 -1 N SER C 24 O PHE C 36
SHEET 4 G 8 HIS C 3 SER C 13 -1 N THR C 10 O ILE C 23
SHEET 5 G 8 HIS C1003 LEU C1013 -1 O GLN C1007 N GLU C 9
SHEET 6 G 8 LEU C1019 TYR C1028 -1 O ALA C1027 N GLN C1006
SHEET 7 G 8 ARG C1031 LEU C1036 -1 O ILE C1034 N PHE C1026
SHEET 8 G 8 TRP C1045 ALA C1047 -1 O THR C1046 N ALA C1035
SHEET 1 H 4 LYS C2003 PRO C2010 0