HEADER COMPLEX (MHC CLASS II/SUPERANTIGEN) 16-OCT-97 2SEB
TITLE X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH A PEPTIDE FROM HUMAN
TITLE 2 COLLAGEN II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 SYNONYM: HLA-DR4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 11 SYNONYM: HLA-DR4;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ENTEROTOXIN TYPE B;
COMPND 15 CHAIN: D;
COMPND 16 SYNONYM: SEB, SUPERANTIGEN;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: PEPTIDE FROM COLLAGEN II;
COMPND 19 CHAIN: E
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7215;
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: S2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PRMHA-3;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7215;
SOURCE 17 EXPRESSION_SYSTEM_CELLULAR_LOCATION: S2;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: PRMHA-3;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 21 ORGANISM_TAXID: 1280;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606
KEYWDS COMPLEX (MHC CLASS II-SUPERANTIGEN), COMPLEX (MHC CLASS II-
KEYWDS 2 SUPERANTIGEN) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DESSEN,C.M.LAWRENCE,S.CUPO,D.M.ZALLER,D.C.WILEY
REVDAT 6 09-AUG-23 2SEB 1 REMARK HETSYN
REVDAT 5 29-JUL-20 2SEB 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE
REVDAT 4 13-JUL-11 2SEB 1 VERSN
REVDAT 3 24-FEB-09 2SEB 1 VERSN
REVDAT 2 01-APR-03 2SEB 1 JRNL
REVDAT 1 28-JAN-98 2SEB 0
JRNL AUTH A.DESSEN,C.M.LAWRENCE,S.CUPO,D.M.ZALLER,D.C.WILEY
JRNL TITL X-RAY CRYSTAL STRUCTURE OF HLA-DR4 (DRA*0101, DRB1*0401)
JRNL TITL 2 COMPLEXED WITH A PEPTIDE FROM HUMAN COLLAGEN II.
JRNL REF IMMUNITY V. 7 473 1997
JRNL REFN ISSN 1074-7613
JRNL PMID 9354468
JRNL DOI 10.1016/S1074-7613(00)80369-6
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.7
REMARK 3 NUMBER OF REFLECTIONS : 26704
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) : 0.229
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2642
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.015
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2897
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 317
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4781
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 62
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.70
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.500
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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19M.SOL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2SEB 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_1000178620.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-96
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 : BENT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27635
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 87.7
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.21800
REMARK 200 R SYM FOR SHELL (I) : 0.21800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1SEB
REMARK 200
REMARK 200 REMARK: FURTHER REFINEMENT PERFORMED USING PDB ENTRY 1SE2
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA ACETATE PH 4.6 9 - 14% PEG
REMARK 280 4000 0.2 M AMMONIUM ACETATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 39.26500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.43500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.14000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.43500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.26500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.14000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 181
REMARK 465 GLY B 1
REMARK 465 LYS B 105
REMARK 465 THR B 106
REMARK 465 GLN B 107
REMARK 465 PRO B 108
REMARK 465 LEU B 109
REMARK 465 GLN B 110
REMARK 465 HIS B 111
REMARK 465 HIS B 112
REMARK 465 PRO B 165
REMARK 465 ARG B 166
REMARK 465 SER B 167
REMARK 465 GLY B 168
REMARK 465 ARG B 191
REMARK 465 SER B 192
REMARK 465 GLU D 1
REMARK 465 ASP D 55
REMARK 465 THR D 56
REMARK 465 LYS D 57
REMARK 465 LEU D 58
REMARK 465 GLY D 59
REMARK 465 ASN D 60
REMARK 465 LYS D 98
REMARK 465 THR D 99
REMARK 465 ASN D 100
REMARK 465 ASP D 101
REMARK 465 ILE D 102
REMARK 465 ASN D 103
REMARK 465 SER D 104
REMARK 465 HIS D 105
REMARK 465 GLN D 106
REMARK 465 THR D 107
REMARK 465 ASP D 108
REMARK 465 LYS D 109
REMARK 465 LYS D 237
REMARK 465 LYS D 238
REMARK 465 LYS D 239
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 1 CG1 CG2 CD1
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 ARG A 100 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 65 CG CD CE NZ
REMARK 470 GLU B 69 CG CD OE1 OE2
REMARK 470 ASN B 113 CG OD1 ND2
REMARK 470 LYS B 139 CG CD CE NZ
REMARK 470 VAL B 164 CG1 CG2
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 LYS D 54 CG CD CE NZ
REMARK 470 ASP D 72 CG OD1 OD2
REMARK 470 LYS D 97 CG CD CE NZ
REMARK 470 ASP D 127 CG OD1 OD2
REMARK 470 ASN D 192 CG OD1 ND2
REMARK 470 GLU D 193 CG CD OE1 OE2
REMARK 470 LYS D 207 CG CD CE NZ
REMARK 470 LYS D 212 CG CD CE NZ
REMARK 470 ASP D 224 CG OD1 OD2
REMARK 470 ASP D 227 CG OD1 OD2
REMARK 470 THR D 236 OG1 CG2
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 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 ARG B 189 CG CD NE CZ NH1 NH2
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 30 O HOH A 957 2.18
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 PRO A 127 CD PRO A 127 N -0.174
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 ARG B 23 O - C - N ANGL. DEV. = -11.6 DEGREES
REMARK 500 ASN D 37 N - CA - CB ANGL. DEV. = 11.6 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 THR A 130 109.63 -57.08
REMARK 500 ASN B 19 71.94 47.88
REMARK 500 TYR B 32 -97.59 -59.12
REMARK 500 GLN B 34 -8.04 -147.47
REMARK 500 TYR B 78 -67.29 -104.23
REMARK 500 GLU B 87 -57.25 -19.45
REMARK 500 THR B 90 -69.54 -120.29
REMARK 500 ASP B 152 40.93 -145.92
REMARK 500 PRO D 8 -31.63 -38.93
REMARK 500 ASP D 29 -166.14 -101.42
REMARK 500 ASN D 37 38.37 99.29
REMARK 500 ASP D 42 -170.39 171.16
REMARK 500 TYR D 91 -77.63 -49.31
REMARK 500 GLN D 92 25.16 -76.30
REMARK 500 ASN D 178 -67.11 -94.39
REMARK 500 ASN D 192 -131.38 63.79
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2SEB A 1 181 UNP P01903 2DRA_HUMAN 26 206
DBREF 2SEB B 1 192 UNP P13760 2B14_HUMAN 30 221
DBREF 2SEB D 1 239 UNP P01552 ETXB_STAAU 28 266
DBREF 2SEB E 1169 1178 UNP P02458 CO2A1_HUMAN 1169 1178
SEQADV 2SEB ALA E 1174 UNP P02458 GLN 1174 CONFLICT
SEQRES 1 A 181 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 181 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 181 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 181 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 181 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 A 181 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 181 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 181 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 181 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 181 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 181 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 181 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 181 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 181 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES 1 B 192 GLY ASP THR ARG PRO ARG PHE LEU GLU GLN VAL LYS HIS
SEQRES 2 B 192 GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE
SEQRES 3 B 192 LEU ASP ARG TYR PHE TYR HIS GLN GLU GLU TYR VAL ARG
SEQRES 4 B 192 PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES 5 B 192 LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES 6 B 192 ASP LEU LEU GLU GLN LYS ARG ALA ALA VAL ASP THR TYR
SEQRES 7 B 192 CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES 8 B 192 GLN ARG ARG VAL TYR PRO GLU VAL THR VAL TYR PRO ALA
SEQRES 9 B 192 LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES 10 B 192 SER VAL ASN GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES 11 B 192 TRP PHE ARG ASN GLY GLN GLU GLU LYS THR GLY VAL VAL
SEQRES 12 B 192 SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES 13 B 192 THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES 14 B 192 VAL TYR THR CYS GLN VAL GLU HIS PRO SER LEU THR SER
SEQRES 15 B 192 PRO LEU THR VAL GLU TRP ARG ALA ARG SER
SEQRES 1 D 239 GLU SER GLN PRO ASP PRO LYS PRO ASP GLU LEU HIS LYS
SEQRES 2 D 239 SER SER LYS PHE THR GLY LEU MET GLU ASN MET LYS VAL
SEQRES 3 D 239 LEU TYR ASP ASP ASN HIS VAL SER ALA ILE ASN VAL LYS
SEQRES 4 D 239 SER ILE ASP GLN PHE LEU TYR PHE ASP LEU ILE TYR SER
SEQRES 5 D 239 ILE LYS ASP THR LYS LEU GLY ASN TYR ASP ASN VAL ARG
SEQRES 6 D 239 VAL GLU PHE LYS ASN LYS ASP LEU ALA ASP LYS TYR LYS
SEQRES 7 D 239 ASP LYS TYR VAL ASP VAL PHE GLY ALA ASN TYR TYR TYR
SEQRES 8 D 239 GLN CYS TYR PHE SER LYS LYS THR ASN ASP ILE ASN SER
SEQRES 9 D 239 HIS GLN THR ASP LYS ARG LYS THR CYS MET TYR GLY GLY
SEQRES 10 D 239 VAL THR GLU HIS ASN GLY ASN GLN LEU ASP LYS TYR ARG
SEQRES 11 D 239 SER ILE THR VAL ARG VAL PHE GLU ASP GLY LYS ASN LEU
SEQRES 12 D 239 LEU SER PHE ASP VAL GLN THR ASN LYS LYS LYS VAL THR
SEQRES 13 D 239 ALA GLN GLU LEU ASP TYR LEU THR ARG HIS TYR LEU VAL
SEQRES 14 D 239 LYS ASN LYS LYS LEU TYR GLU PHE ASN ASN SER PRO TYR
SEQRES 15 D 239 GLU THR GLY TYR ILE LYS PHE ILE GLU ASN GLU ASN SER
SEQRES 16 D 239 PHE TRP TYR ASP MET MET PRO ALA PRO GLY ASP LYS PHE
SEQRES 17 D 239 ASP GLN SER LYS TYR LEU MET MET TYR ASN ASP ASN LYS
SEQRES 18 D 239 MET VAL ASP SER LYS ASP VAL LYS ILE GLU VAL TYR LEU
SEQRES 19 D 239 THR THR LYS LYS LYS
SEQRES 1 E 12 ALA TYR MET ARG ALA ASP ALA ALA ALA GLY GLY ALA
MODRES 2SEB ASN A 118 ASN GLYCOSYLATION SITE
HET NAG A 900 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 5 NAG C8 H15 N O6
FORMUL 6 HOH *62(H2 O)
HELIX 1 1 GLU A 46 ARG A 50 5 5
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 THR B 77 1 13
HELIX 5 5 CYS B 79 GLY B 86 1 8
HELIX 6 6 SER D 14 LYS D 16 5 3
HELIX 7 7 MET D 21 TYR D 28 5 8
HELIX 8 8 LYS D 71 LYS D 78 1 8
HELIX 9 9 GLU D 138 GLY D 140 5 3
HELIX 10 10 ALA D 157 VAL D 169 1 13
HELIX 11 11 GLN D 210 TYR D 217 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 3 GLU A 88 THR A 93 0
SHEET 2 B 3 PRO A 102 PHE A 112 -1 N ASP A 110 O GLU A 88
SHEET 3 B 3 PHE A 145 LEU A 154 -1 N PHE A 153 O ASN A 103
SHEET 1 C 4 LYS A 126 VAL A 128 0
SHEET 2 C 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS A 126
SHEET 3 C 4 VAL A 160 GLU A 166 -1 N GLU A 166 O ASN A 118
SHEET 4 C 4 LEU A 174 GLU A 179 -1 N TRP A 178 O TYR A 161
SHEET 1 D 4 GLN B 10 PHE B 18 0
SHEET 2 D 4 ARG B 23 PHE B 31 -1 N PHE B 31 O GLN B 10
SHEET 3 D 4 GLU B 36 ASP B 41 -1 N PHE B 40 O ASP B 28
SHEET 4 D 4 GLU B 46 ALA B 49 -1 N ARG B 48 O ARG B 39
SHEET 1 E 4 GLU B 98 PRO B 103 0
SHEET 2 E 4 ASN B 113 PHE B 122 -1 N ASN B 120 O GLU B 98
SHEET 3 E 4 PHE B 155 THR B 163 -1 N THR B 163 O ASN B 113
SHEET 4 E 4 VAL B 142 SER B 144 -1 N VAL B 143 O MET B 160
SHEET 1 F 4 GLN B 136 GLU B 138 0
SHEET 2 F 4 ILE B 127 ARG B 133 -1 N ARG B 133 O GLN B 136
SHEET 3 F 4 TYR B 171 HIS B 177 -1 N GLU B 176 O GLU B 128
SHEET 4 F 4 LEU B 184 TRP B 188 -1 N TRP B 188 O TYR B 171
SHEET 1 G 3 ASP D 48 SER D 52 0
SHEET 2 G 3 ASN D 63 GLU D 67 -1 N VAL D 66 O LEU D 49
SHEET 3 G 3 LYS D 111 TYR D 115 1 N THR D 112 O ASN D 63
SHEET 1 H 3 VAL D 118 GLU D 120 0
SHEET 2 H 3 VAL D 82 GLY D 86 -1 N ASP D 83 O THR D 119
SHEET 3 H 3 VAL D 33 VAL D 38 -1 N VAL D 38 O VAL D 82
SHEET 1 I 5 ASN D 194 ASP D 199 0
SHEET 2 I 5 THR D 184 GLU D 191 -1 N GLU D 191 O ASN D 194
SHEET 3 I 5 VAL D 228 THR D 235 -1 N THR D 235 O THR D 184
SHEET 4 I 5 ARG D 130 GLU D 138 1 N ARG D 135 O ILE D 230
SHEET 5 I 5 LYS D 141 THR D 150 -1 N THR D 150 O ARG D 130
SHEET 1 J 2 LYS D 154 THR D 156 0
SHEET 2 J 2 MET D 222 ASP D 224 -1 N VAL D 223 O VAL D 155
SSBOND 1 CYS A 107 CYS A 163 1555 1555 1.93
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.06
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.02
SSBOND 4 CYS D 93 CYS D 113 1555 1555 2.04
LINK ND2 ASN A 118 C1 NAG A 900 1555 1555 1.39
CISPEP 1 ASN A 15 PRO A 16 0 -0.03
CISPEP 2 THR A 113 PRO A 114 0 -0.06
CISPEP 3 TYR B 123 PRO B 124 0 -0.59
CRYST1 78.530 100.280 100.870 90.00 90.00 90.00 P 21 21 21 4
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 0.012734 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009972 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009914 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
