HEADER COMPLEX (TRANSMEMBRANE/GLYCOPROTEIN) 22-FEB-98 1A6A
TITLE THE STRUCTURE OF AN INTERMEDIATE IN CLASS II MHC MATURATION: CLIP
TITLE 2 BOUND TO HLA-DR3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR-1 BETA CHAIN;
COMPND 6 CHAIN: B;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, GAMMA CHAIN;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: CLIP FRAGMENT 87 - 101 OF INVARIANT CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: 9.5.3;
SOURCE 6 CELL: B-LYMPHOCYTE;
SOURCE 7 CELLULAR_LOCATION: PLASMA MEMBRANE;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 CELL_LINE: 9.5.3;
SOURCE 13 CELL: B-LYMPHOCYTE;
SOURCE 14 CELLULAR_LOCATION: PLASMA MEMBRANE;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 CELL_LINE: 9.5.3;
SOURCE 20 CELL: B-LYMPHOCYTE;
SOURCE 21 CELLULAR_LOCATION: PLASMA MEMBRANE
KEYWDS MHC GLYCOPROTEIN, COMPLEX (TRANSMEMBRANE-GLYCOPROTEIN), COMPLEX
KEYWDS 2 (TRANSMEMBRANE-GLYCOPROTEIN) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GHOSH,M.AMAYA,E.MELLINS,D.C.WILEY
REVDAT 4 29-JUL-20 1A6A 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 13-JUL-11 1A6A 1 VERSN
REVDAT 2 24-FEB-09 1A6A 1 VERSN
REVDAT 1 27-MAY-98 1A6A 0
JRNL AUTH P.GHOSH,M.AMAYA,E.MELLINS,D.C.WILEY
JRNL TITL THE STRUCTURE OF AN INTERMEDIATE IN CLASS II MHC MATURATION:
JRNL TITL 2 CLIP BOUND TO HLA-DR3.
JRNL REF NATURE V. 378 457 1995
JRNL REFN ISSN 0028-0836
JRNL PMID 7477400
JRNL DOI 10.1038/378457A0
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 13095
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) : 0.246
REMARK 3 FREE R VALUE : 0.325
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1323
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1442
REMARK 3 BIN R VALUE (WORKING SET) : 0.3730
REMARK 3 BIN FREE R VALUE : 0.4440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 162
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3108
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 22
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.00000
REMARK 3 B22 (A**2) : -10.00000
REMARK 3 B33 (A**2) : 10.00000
REMARK 3 B12 (A**2) : -10.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM SIGMAA (A) : 0.61
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) : 0.53
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.72
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.310
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) : 3.530 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.980 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.520 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.350 ; 6.000
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : PARAM3_MOD.CHO
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : TOPH3.CHO
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESIDUES 5 - 180 OF THE ALPHA SUBUNIT AND RESIDUES 5 - 191
REMARK 3 OF THE BETA SUBUNIT ARE CLEARLY VISIBLE IN 2FO-FC ELECTRON
REMARK 3 DENSITY MAPS. THREE SMALL BREAKS IN MAIN-CHAIN DENSITY
REMARK 3 OCCUR IN LOOP REGIONS OF THE BETA 2 DOMAIN (AT BETA 109,
REMARK 3 172, AND 189).
REMARK 4
REMARK 4 1A6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-94
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, ROTAVATA/AGROVATA
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14428
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.31400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DLH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4K, 100 MM MGCL2, 100 MM
REMARK 280 ACETATE BUFFER, PH 4.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -Y,-X,-Z+1/3
REMARK 290 5555 -X+Y,Y,-Z+2/3
REMARK 290 6555 X,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 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.06667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.03333
REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 53.03333
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 106.06667
REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: 7340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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 BIOMT1 2 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 123 CG CD NE CZ NH1 NH2
REMARK 480 ASN B 19 CG OD1 ND2
REMARK 480 GLU B 22 CG CD OE1 OE2
REMARK 480 ARG B 23 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 105 CG CD CE NZ
REMARK 480 GLN B 107 CG CD OE1 NE2
REMARK 480 LEU B 109 CG CD1 CD2
REMARK 480 GLN B 110 CG CD OE1 NE2
REMARK 480 HIS B 111 CG ND1 CD2 CE1 NE2
REMARK 480 GLN B 136 CG CD OE1 NE2
REMARK 480 GLU B 138 CG CD OE1 OE2
REMARK 480 ARG B 166 CG CD NE CZ NH1 NH2
REMARK 480 SER B 167 OG
REMARK 480 ARG B 189 CG CD NE CZ NH1 NH2
REMARK 480 ARG B 191 CG CD NE CZ NH1 NH2
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 PHE B 31 C HIS B 32 N -0.159
REMARK 500 GLU B 87 CD GLU B 87 OE2 0.083
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 PHE B 31 O - C - N ANGL. DEV. = -10.0 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 PHE A 32 -176.31 -171.75
REMARK 500 THR A 90 116.89 -163.29
REMARK 500 LYS A 111 73.71 46.38
REMARK 500 THR A 130 76.22 -66.28
REMARK 500 HIS A 143 43.33 39.60
REMARK 500 LEU A 144 -166.23 -109.78
REMARK 500 LYS A 147 133.60 177.85
REMARK 500 SER A 156 -164.53 -125.40
REMARK 500 THR A 157 -2.32 -140.14
REMARK 500 LEU A 170 102.73 -175.38
REMARK 500 ASP A 171 -73.12 -35.99
REMARK 500 PRO A 173 99.39 -60.90
REMARK 500 GLU A 179 144.41 -170.93
REMARK 500 ASN B 19 70.53 58.37
REMARK 500 GLU B 22 -71.62 -52.47
REMARK 500 GLN B 34 -7.37 71.60
REMARK 500 SER B 88 -71.83 -52.62
REMARK 500 THR B 90 -74.71 -120.03
REMARK 500 HIS B 112 92.20 -61.30
REMARK 500 TYR B 123 130.30 -175.42
REMARK 500 PRO B 124 -172.28 -64.34
REMARK 500 ASN B 134 21.48 49.43
REMARK 500 GLU B 138 89.09 -60.77
REMARK 500 ASP B 152 36.13 -99.97
REMARK 500 SER B 167 67.98 -63.12
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 A 150 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A6A A 5 180 UNP P01903 2DRA_HUMAN 30 205
DBREF 1A6A B 5 191 UNP P01912 HB2B_HUMAN 34 220
DBREF 1A6A C 87 101 UNP P04233 HG2A_HUMAN 103 117
SEQRES 1 A 176 HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN PRO ASP
SEQRES 2 A 176 GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY ASP GLU
SEQRES 3 A 176 ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR VAL TRP
SEQRES 4 A 176 ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE GLU ALA
SEQRES 5 A 176 GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS ALA ASN
SEQRES 6 A 176 LEU GLU ILE MET THR LYS ARG SER ASN TYR THR PRO ILE
SEQRES 7 A 176 THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR ASN SER
SEQRES 8 A 176 PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE CYS PHE
SEQRES 9 A 176 ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL THR TRP
SEQRES 10 A 176 LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL SER GLU
SEQRES 11 A 176 THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE ARG LYS
SEQRES 12 A 176 PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU ASP VAL
SEQRES 13 A 176 TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP GLU PRO
SEQRES 14 A 176 LEU LEU LYS HIS TRP GLU PHE
SEQRES 1 B 187 PRO ARG PHE LEU GLU TYR SER THR SER GLU CYS HIS PHE
SEQRES 2 B 187 PHE ASN GLY THR GLU ARG VAL ARG TYR LEU ASP ARG TYR
SEQRES 3 B 187 PHE HIS ASN GLN GLU GLU ASN VAL ARG PHE ASP SER ASP
SEQRES 4 B 187 VAL GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO
SEQRES 5 B 187 ASP ALA GLU TYR TRP ASN SER GLN LYS ASP LEU LEU GLU
SEQRES 6 B 187 GLN LYS ARG GLY ARG VAL ASP ASN TYR CYS ARG HIS ASN
SEQRES 7 B 187 TYR GLY VAL VAL GLU SER PHE THR VAL GLN ARG ARG VAL
SEQRES 8 B 187 HIS PRO LYS VAL THR VAL TYR PRO SER LYS THR GLN PRO
SEQRES 9 B 187 LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL SER GLY
SEQRES 10 B 187 PHE TYR PRO GLY SER ILE GLU VAL ARG TRP PHE ARG ASN
SEQRES 11 B 187 GLY GLN GLU GLU LYS THR GLY VAL VAL SER THR GLY LEU
SEQRES 12 B 187 ILE HIS ASN GLY ASP TRP THR PHE GLN THR LEU VAL MET
SEQRES 13 B 187 LEU GLU THR VAL PRO ARG SER GLY GLU VAL TYR THR CYS
SEQRES 14 B 187 GLN VAL GLU HIS PRO SER VAL THR SER PRO LEU THR VAL
SEQRES 15 B 187 GLU TRP ARG ALA ARG
SEQRES 1 C 15 PRO VAL SER LYS MET ARG MET ALA THR PRO LEU LEU MET
SEQRES 2 C 15 GLN ALA
MODRES 1A6A ASN A 78 ASN GLYCOSYLATION SITE
MODRES 1A6A ASN A 118 ASN GLYCOSYLATION SITE
HET NAG A 181 14
HET NAG A 200 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 6 HOH *22(H2 O)
HELIX 1 1 GLU A 46 PHE A 51 1 6
HELIX 2 2 ALA A 56 ARG A 76 1 21
HELIX 3 3 GLU B 52 SER B 63 5 12
HELIX 4 4 LYS B 65 ASN B 77 1 13
HELIX 5 5 CYS B 79 VAL B 86 1 8
SHEET 1 A 4 ILE A 7 LEU A 14 0
SHEET 2 A 4 SER A 19 PHE A 26 -1 N ASP A 25 O ILE A 8
SHEET 3 A 4 ASP A 29 ASP A 35 -1 N PHE A 32 O PHE A 24
SHEET 4 A 4 GLU A 40 TRP A 43 -1 N VAL A 42 O HIS A 33
SHEET 1 B 4 THR A 90 THR A 93 0
SHEET 2 B 4 ASN A 103 ILE A 109 -1 N PHE A 108 O THR A 90
SHEET 3 B 4 LYS A 147 PHE A 153 -1 N PHE A 153 O ASN A 103
SHEET 4 B 4 VAL A 132 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 C 3 ASN A 118 ARG A 123 0
SHEET 2 C 3 VAL A 160 GLU A 166 -1 N GLU A 166 O ASN A 118
SHEET 3 C 3 LEU A 174 GLU A 179 -1 N TRP A 178 O TYR A 161
SHEET 1 D 4 GLU B 9 PHE B 18 0
SHEET 2 D 4 ARG B 23 HIS B 32 -1 N PHE B 31 O TYR B 10
SHEET 3 D 4 GLU B 35 ASP B 41 -1 N PHE B 40 O ASP B 28
SHEET 4 D 4 PHE B 47 ALA B 49 -1 N ARG B 48 O ARG B 39
SHEET 1 E 3 LYS B 98 PRO B 103 0
SHEET 2 E 3 LEU B 115 SER B 120 -1 N SER B 120 O LYS B 98
SHEET 3 E 3 GLN B 156 LEU B 158 -1 N THR B 157 O VAL B 119
SHEET 1 F 3 ILE B 127 ARG B 133 0
SHEET 2 F 3 VAL B 170 HIS B 177 -1 N GLU B 176 O GLU B 128
SHEET 3 F 3 LEU B 184 ARG B 189 -1 N TRP B 188 O TYR B 171
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.03
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.05
LINK ND2 ASN A 78 C1 NAG A 181 1555 1555 1.45
LINK ND2 ASN A 118 C1 NAG A 200 1555 1555 1.44
CISPEP 1 THR A 113 PRO A 114 0 -0.11
CISPEP 2 TYR B 123 PRO B 124 0 -0.51
CRYST1 78.450 78.450 159.100 90.00 90.00 120.00 P 32 1 2 6
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 0.012747 0.007359 0.000000 0.00000
SCALE2 0.000000 0.014719 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006285 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
