HEADER IMMUNE SYSTEM 13-MAR-14 4P4R
TITLE STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: BRIDGING THE GAP
TITLE 2 BETWEEN ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 32-214;
COMPND 5 SYNONYM: DP(W3),DP(W4),HLA-SB ALPHA CHAIN,MHC CLASS II DP3-ALPHA,MHC
COMPND 6 CLASS II DPA1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: MIM2 PEPTIDE,HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP
COMPND 10 BETA 1 CHAIN;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: UNP RESIDUES 32-218;
COMPND 13 SYNONYM: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,DP(W4) BETA CHAIN,
COMPND 14 MHC CLASS II ANTIGEN DPB1;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-DPA1, HLA-DP1A, HLASB;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: HLA-DPB1, HLA-DP1B;
SOURCE 13 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS HLA-DP2, IMMUNE SYSTEM, ALLERGY, BERYLLIOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.CLAYTON,F.CRAWFORD,J.W.KAPPLER
REVDAT 3 29-JUL-20 4P4R 1 COMPND SOURCE REMARK SEQADV
REVDAT 3 2 1 HETNAM LINK SITE
REVDAT 2 07-JAN-15 4P4R 1 DBREF
REVDAT 1 16-JUL-14 4P4R 0
JRNL AUTH G.M.CLAYTON,Y.WANG,F.CRAWFORD,A.NOVIKOV,B.T.WIMBERLY,
JRNL AUTH 2 J.S.KIEFT,M.T.FALTA,N.A.BOWERMAN,P.MARRACK,A.P.FONTENOT,
JRNL AUTH 3 S.DAI,J.W.KAPPLER
JRNL TITL STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: LINKING
JRNL TITL 2 ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY.
JRNL REF CELL V. 158 132 2014
JRNL REFN ISSN 1097-4172
JRNL PMID 24995984
JRNL DOI 10.1016/J.CELL.2014.04.048
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 3 NUMBER OF REFLECTIONS : 18022
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 + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 917
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 : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.91
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2730
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2436
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2575
REMARK 3 BIN R VALUE (WORKING SET) : 0.2386
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.68
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 155
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 : 6057
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -15.75310
REMARK 3 B22 (A**2) : 18.73150
REMARK 3 B33 (A**2) : -2.97840
REMARK 3 B12 (A**2) : 0.00000
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) : 0.508
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.462
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.892
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.836
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6308 ; 1.500 ; HARMONIC
REMARK 3 BOND ANGLES : 8620 ; 1.500 ; HARMONIC
REMARK 3 TORSION ANGLES : 2072 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 183 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 919 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6308 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 806 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6825 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.34
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.10
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4P4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18043
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 90.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.7700
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NH4TARTRATE DIBASIC, 20% PEG
REMARK 280 -3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 38.62500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.43900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.22000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.43900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.62500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.22000
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 ILE A 1
REMARK 465 ALA A 180
REMARK 465 GLN A 181
REMARK 465 GLU A 182
REMARK 465 PRO A 183
REMARK 465 GLY B -13
REMARK 465 GLY B -12
REMARK 465 SER B -11
REMARK 465 LEU B -10
REMARK 465 VAL B -9
REMARK 465 PRO B -8
REMARK 465 ARG B -7
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 GLY B -4
REMARK 465 GLY B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 ILE C 1
REMARK 465 ALA C 180
REMARK 465 GLN C 181
REMARK 465 GLU C 182
REMARK 465 PRO C 183
REMARK 465 GLY D -13
REMARK 465 GLY D -12
REMARK 465 SER D -11
REMARK 465 LEU D -10
REMARK 465 VAL D -9
REMARK 465 PRO D -8
REMARK 465 ARG D -7
REMARK 465 GLY D -6
REMARK 465 SER D -5
REMARK 465 GLY D -4
REMARK 465 GLY D -3
REMARK 465 GLY D -2
REMARK 465 GLY D -1
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 LYS A 2 CG CD CE NZ
REMARK 470 ARG A 17 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 38 CG CD CE NZ
REMARK 470 GLU A 40 CG CD OE1 OE2
REMARK 470 LEU A 99 CG CD1 CD2
REMARK 470 GLN A 172 CG CD OE1 NE2
REMARK 470 GLN B -25 CG CD OE1 NE2
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 ARG B 75 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 89 CG CD1 CD2
REMARK 470 GLN B 90 CG CD OE1 NE2
REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 LEU B 107 CG CD1 CD2
REMARK 470 GLN B 108 CG CD OE1 NE2
REMARK 470 GLN B 134 CG CD OE1 NE2
REMARK 470 GLN B 165 CG CD OE1 NE2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 GLN B 189 CG CD OE1 NE2
REMARK 470 LYS C 2 CG CD CE NZ
REMARK 470 ARG C 17 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 99 CG CD1 CD2
REMARK 470 GLU C 158 CG CD OE1 OE2
REMARK 470 GLN C 172 CG CD OE1 NE2
REMARK 470 GLN D -25 CG CD OE1 NE2
REMARK 470 LYS D 63 CG CD CE NZ
REMARK 470 GLN D 90 CG CD OE1 NE2
REMARK 470 ARG D 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 103 CG CD CE NZ
REMARK 470 LYS D 104 CG CD CE NZ
REMARK 470 LEU D 107 CG CD1 CD2
REMARK 470 HIS D 109 CG ND1 CD2 CE1 NE2
REMARK 470 ASN D 144 CG OD1 ND2
REMARK 470 GLN D 165 CG CD OE1 NE2
REMARK 470 LYS D 187 CG CD CE NZ
REMARK 470 GLN D 189 CG CD OE1 NE2
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 B 76 N - CA - CB ANGL. DEV. = 19.2 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 GLU A 134 149.93 -172.18
REMARK 500 GLU A 158 37.59 -91.46
REMARK 500 ASN B 31 -104.76 59.21
REMARK 500 ARG B 75 -71.29 -91.45
REMARK 500 GLN B 108 -38.72 -151.77
REMARK 500 ASP B 119 75.31 57.79
REMARK 500 ASP B 150 29.82 -141.69
REMARK 500 ASN C 124 17.33 58.33
REMARK 500 GLU C 158 35.46 -90.42
REMARK 500 ASN D 31 -109.00 59.11
REMARK 500 ARG D 75 -84.32 -103.92
REMARK 500 LEU D 83 -73.22 -60.51
REMARK 500 PRO D 86 70.23 -68.70
REMARK 500 MET D 87 -30.29 -157.45
REMARK 500 THR D 88 -50.60 -138.76
REMARK 500 GLN D 108 -42.47 -152.05
REMARK 500 ASP D 119 70.89 58.20
REMARK 500 PRO D 122 -170.25 -65.62
REMARK 500 SER D 124 104.25 -53.12
REMARK 500 ASN D 144 -164.48 72.88
REMARK 500 ASP D 150 30.98 -141.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P4K RELATED DB: PDB
REMARK 900 RELATED ID: 4P57 RELATED DB: PDB
REMARK 900 RELATED ID: 4P5M RELATED DB: PDB
REMARK 900 RELATED ID: 4P5K RELATED DB: PDB
DBREF 4P4R A 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P4R B -25 -15 PDB 4P4R 4P4R -25 -15
DBREF 4P4R B 3 189 UNP P04440 DPB1_HUMAN 32 218
DBREF 4P4R C 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P4R D -25 -15 PDB 4P4R 4P4R -25 -15
DBREF 4P4R D 3 189 UNP P04440 DPB1_HUMAN 32 218
SEQADV 4P4R GLY B -14 UNP P04440 LINKER
SEQADV 4P4R GLY B -13 UNP P04440 LINKER
SEQADV 4P4R GLY B -12 UNP P04440 LINKER
SEQADV 4P4R SER B -11 UNP P04440 LINKER
SEQADV 4P4R LEU B -10 UNP P04440 LINKER
SEQADV 4P4R VAL B -9 UNP P04440 LINKER
SEQADV 4P4R PRO B -8 UNP P04440 LINKER
SEQADV 4P4R ARG B -7 UNP P04440 LINKER
SEQADV 4P4R GLY B -6 UNP P04440 LINKER
SEQADV 4P4R SER B -5 UNP P04440 LINKER
SEQADV 4P4R GLY B -4 UNP P04440 LINKER
SEQADV 4P4R GLY B -3 UNP P04440 LINKER
SEQADV 4P4R GLY B -2 UNP P04440 LINKER
SEQADV 4P4R GLY B -1 UNP P04440 LINKER
SEQADV 4P4R SER B 3 UNP P04440 THR 32 VARIANT
SEQADV 4P4R VAL B 36 UNP P04440 ALA 65 VARIANT
SEQADV 4P4R ASP B 55 UNP P04440 ALA 84 VARIANT
SEQADV 4P4R GLU B 56 UNP P04440 ALA 85 VARIANT
SEQADV 4P4R GLU B 69 UNP P04440 LYS 98 VARIANT
SEQADV 4P4R GLY D -14 UNP P04440 LINKER
SEQADV 4P4R GLY D -13 UNP P04440 LINKER
SEQADV 4P4R GLY D -12 UNP P04440 LINKER
SEQADV 4P4R SER D -11 UNP P04440 LINKER
SEQADV 4P4R LEU D -10 UNP P04440 LINKER
SEQADV 4P4R VAL D -9 UNP P04440 LINKER
SEQADV 4P4R PRO D -8 UNP P04440 LINKER
SEQADV 4P4R ARG D -7 UNP P04440 LINKER
SEQADV 4P4R GLY D -6 UNP P04440 LINKER
SEQADV 4P4R SER D -5 UNP P04440 LINKER
SEQADV 4P4R GLY D -4 UNP P04440 LINKER
SEQADV 4P4R GLY D -3 UNP P04440 LINKER
SEQADV 4P4R GLY D -2 UNP P04440 LINKER
SEQADV 4P4R GLY D -1 UNP P04440 LINKER
SEQADV 4P4R SER D 3 UNP P04440 THR 32 VARIANT
SEQADV 4P4R VAL D 36 UNP P04440 ALA 65 VARIANT
SEQADV 4P4R ASP D 55 UNP P04440 ALA 84 VARIANT
SEQADV 4P4R GLU D 56 UNP P04440 ALA 85 VARIANT
SEQADV 4P4R GLU D 69 UNP P04440 LYS 98 VARIANT
SEQRES 1 A 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 A 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 A 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 A 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 A 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 A 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 A 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 A 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 A 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 A 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 A 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 A 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 A 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 A 183 PRO
SEQRES 1 B 212 GLN ALA PHE TRP ILE ASP LEU PHE GLU THR ILE GLY GLY
SEQRES 2 B 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 B 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 B 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 B 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 B 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 B 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 B 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 B 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 B 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 B 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 B 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 B 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 B 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 B 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 B 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 B 212 TRP LYS ALA GLN
SEQRES 1 C 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 C 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 C 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 C 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 C 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 C 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 C 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 C 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 C 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 C 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 C 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 C 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 C 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 C 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 C 183 PRO
SEQRES 1 D 212 GLN ALA PHE TRP ILE ASP LEU PHE GLU THR ILE GLY GLY
SEQRES 2 D 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 D 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 D 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 D 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 D 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 D 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 D 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 D 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 D 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 D 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 D 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 D 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 D 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 D 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 D 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 D 212 TRP LYS ALA GLN
HET NAG A 201 14
HET NAG A 202 14
HET NAG C 201 14
HET NAG C 202 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 9 HOH *119(H2 O)
HELIX 1 AA1 LEU A 45 PHE A 52 1 8
HELIX 2 AA2 GLU A 55 SER A 77 1 23
HELIX 3 AA3 THR B 49 LEU B 51 5 3
HELIX 4 AA4 GLY B 52 GLN B 62 1 11
HELIX 5 AA5 GLN B 62 GLY B 84 1 23
HELIX 6 AA6 LEU C 45 PHE C 52 1 8
HELIX 7 AA7 GLU C 55 SER C 77 1 23
HELIX 8 AA8 THR D 49 LEU D 51 5 3
HELIX 9 AA9 GLY D 52 GLN D 62 1 11
HELIX 10 AB1 GLN D 62 VAL D 72 1 11
HELIX 11 AB2 ARG D 75 GLY D 84 1 10
SHEET 1 AA1 8 GLU A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N ASP A 35 O GLU A 40
SHEET 3 AA1 8 GLY A 20 PHE A 26 -1 N PHE A 24 O PHE A 32
SHEET 4 AA1 8 HIS A 5 GLN A 14 -1 N THR A 8 O GLU A 25
SHEET 5 AA1 8 LEU B 8 PHE B 18 -1 O CYS B 15 N SER A 7
SHEET 6 AA1 8 THR B 21 TYR B 30 -1 O ILE B 29 N GLN B 10
SHEET 7 AA1 8 GLU B 33 ASP B 39 -1 O GLU B 33 N TYR B 30
SHEET 8 AA1 8 PHE B 45 ALA B 47 -1 O ARG B 46 N ARG B 37
SHEET 1 AA2 4 GLU A 88 PRO A 93 0
SHEET 2 AA2 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 AA2 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 AA2 4 VAL A 132 GLU A 134 -1 N ALA A 133 O TYR A 150
SHEET 1 AA3 4 GLU A 88 PRO A 93 0
SHEET 2 AA3 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 AA3 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 AA3 4 LEU A 138 PRO A 139 -1 N LEU A 138 O HIS A 146
SHEET 1 AA4 4 GLU A 126 LEU A 127 0
SHEET 2 AA4 4 ASN A 118 CYS A 123 -1 N CYS A 123 O GLU A 126
SHEET 3 AA4 4 TYR A 161 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 AA4 4 LEU A 174 TRP A 178 -1 O LEU A 174 N VAL A 165
SHEET 1 AA5 4 ARG B 96 PRO B 101 0
SHEET 2 AA5 4 ASN B 111 PHE B 120 -1 O HIS B 116 N ASN B 98
SHEET 3 AA5 4 PHE B 153 MET B 161 -1 O MET B 161 N ASN B 111
SHEET 4 AA5 4 VAL B 140 SER B 142 -1 N VAL B 141 O MET B 158
SHEET 1 AA6 4 ARG B 96 PRO B 101 0
SHEET 2 AA6 4 ASN B 111 PHE B 120 -1 O HIS B 116 N ASN B 98
SHEET 3 AA6 4 PHE B 153 MET B 161 -1 O MET B 161 N ASN B 111
SHEET 4 AA6 4 ILE B 146 ARG B 147 -1 N ILE B 146 O GLN B 154
SHEET 1 AA7 4 GLN B 134 GLU B 136 0
SHEET 2 AA7 4 GLN B 126 LEU B 131 -1 N TRP B 129 O GLU B 136
SHEET 3 AA7 4 VAL B 168 GLU B 174 -1 O THR B 170 N PHE B 130
SHEET 4 AA7 4 VAL B 182 LYS B 187 -1 O VAL B 182 N VAL B 173
SHEET 1 AA8 8 GLU C 40 TRP C 43 0
SHEET 2 AA8 8 ASP C 29 ASP C 35 -1 N ASP C 35 O GLU C 40
SHEET 3 AA8 8 GLY C 20 PHE C 26 -1 N PHE C 24 O PHE C 32
SHEET 4 AA8 8 HIS C 5 GLN C 14 -1 N THR C 8 O GLU C 25
SHEET 5 AA8 8 LEU D 8 PHE D 18 -1 O CYS D 15 N SER C 7
SHEET 6 AA8 8 THR D 21 TYR D 30 -1 O ILE D 29 N GLN D 10
SHEET 7 AA8 8 GLU D 33 ASP D 39 -1 O GLU D 33 N TYR D 30
SHEET 8 AA8 8 PHE D 45 ALA D 47 -1 O ARG D 46 N ARG D 37
SHEET 1 AA9 4 GLU C 88 PRO C 93 0
SHEET 2 AA9 4 ASN C 103 PHE C 112 -1 O ILE C 106 N PHE C 92
SHEET 3 AA9 4 PHE C 145 PHE C 153 -1 O LEU C 151 N LEU C 105
SHEET 4 AA9 4 VAL C 132 GLU C 134 -1 N ALA C 133 O TYR C 150
SHEET 1 AB1 4 GLU C 88 PRO C 93 0
SHEET 2 AB1 4 ASN C 103 PHE C 112 -1 O ILE C 106 N PHE C 92
SHEET 3 AB1 4 PHE C 145 PHE C 153 -1 O LEU C 151 N LEU C 105
SHEET 4 AB1 4 LEU C 138 PRO C 139 -1 N LEU C 138 O HIS C 146
SHEET 1 AB2 4 GLU C 126 LEU C 127 0
SHEET 2 AB2 4 ASN C 118 CYS C 123 -1 N CYS C 123 O GLU C 126
SHEET 3 AB2 4 TYR C 161 GLU C 166 -1 O ARG C 164 N THR C 120
SHEET 4 AB2 4 LEU C 174 TRP C 178 -1 O LYS C 176 N CYS C 163
SHEET 1 AB3 4 ARG D 96 PRO D 101 0
SHEET 2 AB3 4 ASN D 111 PHE D 120 -1 O HIS D 116 N ASN D 98
SHEET 3 AB3 4 PHE D 153 MET D 161 -1 O MET D 161 N ASN D 111
SHEET 4 AB3 4 VAL D 140 SER D 142 -1 N VAL D 141 O MET D 158
SHEET 1 AB4 4 ARG D 96 PRO D 101 0
SHEET 2 AB4 4 ASN D 111 PHE D 120 -1 O HIS D 116 N ASN D 98
SHEET 3 AB4 4 PHE D 153 MET D 161 -1 O MET D 161 N ASN D 111
SHEET 4 AB4 4 ILE D 146 ARG D 147 -1 N ILE D 146 O GLN D 154
SHEET 1 AB5 4 GLN D 134 GLU D 135 0
SHEET 2 AB5 4 GLN D 126 LEU D 131 -1 N LEU D 131 O GLN D 134
SHEET 3 AB5 4 VAL D 168 GLU D 174 -1 O THR D 170 N PHE D 130
SHEET 4 AB5 4 VAL D 182 LYS D 187 -1 O VAL D 182 N VAL D 173
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.02
SSBOND 2 CYS B 15 CYS B 77 1555 1555 2.04
SSBOND 3 CYS B 115 CYS B 171 1555 1555 2.04
SSBOND 4 CYS C 107 CYS C 163 1555 1555 2.02
SSBOND 5 CYS D 15 CYS D 77 1555 1555 2.06
SSBOND 6 CYS D 115 CYS D 171 1555 1555 2.03
LINK ND2 ASN A 78 C1 NAG A 202 1555 1555 1.44
LINK ND2 ASN A 118 C1 NAG A 201 1555 1555 1.43
LINK ND2 ASN C 78 C1 NAG C 202 1555 1555 1.43
LINK ND2 ASN C 118 C1 NAG C 201 1555 1555 1.44
CISPEP 1 ARG A 17 PRO A 18 0 3.64
CISPEP 2 PHE A 113 PRO A 114 0 2.41
CISPEP 3 ILE B -15 GLY B -14 0 5.55
CISPEP 4 TYR B 121 PRO B 122 0 -0.41
CISPEP 5 ARG C 17 PRO C 18 0 -0.28
CISPEP 6 PHE C 113 PRO C 114 0 2.82
CISPEP 7 TYR D 121 PRO D 122 0 0.32
CRYST1 77.250 102.440 120.878 90.00 90.00 90.00 P 21 21 21 8
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 0.012945 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009762 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008273 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
