HEADER IMMUNE SYSTEM 10-FEB-10 3LQZ
TITLE CRYSTAL STRUCTURE OF HLA-DP2
CAVEAT 3LQZ NAG B 190 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HLA-SB ALPHA CHAIN, MHC CLASS II DP3-ALPHA, DP(W3), DP(W4);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HLA-DP2 BETA CHAIN LINKED WITH DRA PEPTIDE;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: MAJOR HISTOCOMPATIBILITY COMPLEX, CLASS II, DP BETA 1;
COMPND 10 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-DP1A, HLA-DPA1, HLA-DPA1*0103, HLASB;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BTI-TN-5B1-4;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: DAMA-245O6.7-001, HLA-DPB1, HLA-DPB1*0201;
SOURCE 14 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BTI-TN-5B1-4
KEYWDS HLA, MHC, IMMUNE, DISULFIDE BOND, GLYCOPROTEIN, IMMUNE RESPONSE,
KEYWDS 2 MEMBRANE, MHC II, TRANSMEMBRANE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DAI
REVDAT 5 29-JUL-20 3LQZ 1 CAVEAT COMPND REMARK HET
REVDAT 5 2 1 HETNAM FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 04-SEP-19 3LQZ 1 LINK CRYST1
REVDAT 3 13-JUL-11 3LQZ 1 VERSN
REVDAT 2 05-MAY-10 3LQZ 1 JRNL
REVDAT 1 14-APR-10 3LQZ 0
JRNL AUTH S.DAI,G.A.MURPHY,F.CRAWFORD,D.G.MACK,M.T.FALTA,P.MARRACK,
JRNL AUTH 2 J.W.KAPPLER,A.P.FONTENOT
JRNL TITL CRYSTAL STRUCTURE OF HLA-DP2 AND IMPLICATIONS FOR CHRONIC
JRNL TITL 2 BERYLLIUM DISEASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 7425 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20356827
JRNL DOI 10.1073/PNAS.1001772107
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0040
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.2
REMARK 3 NUMBER OF REFLECTIONS : 11332
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 645
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 902
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.3700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3114
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.94000
REMARK 3 B22 (A**2) : 5.94000
REMARK 3 B33 (A**2) : -8.91000
REMARK 3 B12 (A**2) : 2.97000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.439
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.355
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.178
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3252 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4426 ; 1.490 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 375 ; 6.719 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 179 ;41.920 ;24.246
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 506 ;21.430 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;20.275 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 467 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2564 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1383 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2177 ; 0.319 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 89 ; 0.182 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 26 ; 0.221 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.079 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1930 ; 0.364 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3076 ; 0.672 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1488 ; 0.957 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1350 ; 1.661 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 181
REMARK 3 ORIGIN FOR THE GROUP (A): 54.0400 -37.2810 5.3790
REMARK 3 T TENSOR
REMARK 3 T11: -0.3006 T22: -0.2296
REMARK 3 T33: -0.2938 T12: -0.0666
REMARK 3 T13: -0.1266 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 1.8359 L22: 2.3171
REMARK 3 L33: 4.3693 L12: 0.4828
REMARK 3 L13: -1.6206 L23: -0.2668
REMARK 3 S TENSOR
REMARK 3 S11: 0.0777 S12: -0.1584 S13: 0.2297
REMARK 3 S21: -0.0476 S22: -0.0119 S23: 0.2631
REMARK 3 S31: -0.8404 S32: -0.5076 S33: -0.0659
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 189
REMARK 3 ORIGIN FOR THE GROUP (A): 51.8590 -53.4290 2.2190
REMARK 3 T TENSOR
REMARK 3 T11: -0.4210 T22: -0.3195
REMARK 3 T33: -0.2652 T12: -0.2041
REMARK 3 T13: -0.1996 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 2.5036 L22: 1.9270
REMARK 3 L33: 4.2617 L12: 0.6654
REMARK 3 L13: -1.3225 L23: -0.8028
REMARK 3 S TENSOR
REMARK 3 S11: -0.0501 S12: -0.1263 S13: -0.2653
REMARK 3 S21: -0.0530 S22: -0.0407 S23: -0.0557
REMARK 3 S31: 0.1003 S32: -0.3247 S33: 0.0908
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -22 B -8
REMARK 3 ORIGIN FOR THE GROUP (A): 70.2640 -41.6900 -11.0350
REMARK 3 T TENSOR
REMARK 3 T11: -0.2836 T22: -0.4628
REMARK 3 T33: -0.0249 T12: -0.1997
REMARK 3 T13: 0.0796 T23: 0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 1.6055 L22: 11.0906
REMARK 3 L33: 3.0329 L12: -3.7948
REMARK 3 L13: 0.2394 L23: -3.0525
REMARK 3 S TENSOR
REMARK 3 S11: 0.5502 S12: 0.7031 S13: 0.7665
REMARK 3 S21: -1.4606 S22: -0.9247 S23: -0.6661
REMARK 3 S31: 1.5095 S32: 1.0758 S33: 0.3745
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3LQZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057620.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 170; NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS; APS
REMARK 200 BEAMLINE : 8.2.2; 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 1.0
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12053
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250
REMARK 200 RESOLUTION RANGE LOW (A) : 136.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.100
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) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
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; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 300MM SODIUM CHLORIDE,
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 20.60160
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 41.20320
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 0.00000
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 41.20320
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 20.60160
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 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 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 GLY B 1
REMARK 465 GLY B 2
REMARK 465 PRO B 106
REMARK 465 LEU B 107
REMARK 465 GLN B 108
REMARK 465 HIS B 109
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 ARG A 17 -77.18 0.31
REMARK 500 GLU A 28 -15.12 71.90
REMARK 500 MET A 31 -62.71 -90.07
REMARK 500 GLN A 75 -80.21 -74.57
REMARK 500 ARG A 76 54.29 -62.33
REMARK 500 SER A 77 19.77 -175.50
REMARK 500 ASN A 78 36.52 39.27
REMARK 500 LEU A 99 114.22 -26.68
REMARK 500 PRO A 102 125.30 -36.21
REMARK 500 THR A 129 -68.25 -109.52
REMARK 500 GLU A 134 149.50 -170.74
REMARK 500 PHE A 137 91.90 -59.50
REMARK 500 PRO A 155 94.17 -47.88
REMARK 500 ASP A 159 120.65 179.40
REMARK 500 LEU A 170 -160.00 -103.29
REMARK 500 ASP A 171 -24.69 -169.97
REMARK 500 PHE B 18 -124.30 -112.67
REMARK 500 ARG B 32 -19.32 82.16
REMARK 500 ARG B 37 144.45 -179.71
REMARK 500 PRO B 73 -25.20 -38.55
REMARK 500 ARG B 75 -95.41 -78.75
REMARK 500 THR B 88 -64.12 -104.05
REMARK 500 PRO B 101 -153.82 -64.34
REMARK 500 SER B 102 82.46 135.52
REMARK 500 LYS B 103 -87.07 -126.65
REMARK 500 LYS B 104 -176.38 -59.52
REMARK 500 ASN B 111 121.36 -170.05
REMARK 500 ASP B 119 60.16 70.94
REMARK 500 ASP B 150 31.45 -153.94
REMARK 500 THR B 162 77.04 -152.48
REMARK 500 GLN B 164 -85.49 -91.49
REMARK 500 GLN B 165 -67.31 -152.24
REMARK 500 SER B 177 -73.54 -70.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DRA PEPTIDE + LINKER + HLA-DP2 BETA CHAIN
DBREF 3LQZ A 1 181 UNP P20036 DPA1_HUMAN 32 212
DBREF 3LQZ B 4 189 UNP Q5EP54 Q5EP54_HUMAN 33 218
SEQADV 3LQZ ARG B -22 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ LYS B -21 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ PHE B -20 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ HIS B -19 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ TYR B -18 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ LEU B -17 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ PRO B -16 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ PHE B -15 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ LEU B -14 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ PRO B -13 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ SER B -12 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ THR B -11 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ GLY B -10 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ GLY B -9 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ SER B -8 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ LEU B -7 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ VAL B -6 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ PRO B -5 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ ARG B -4 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ GLY B -3 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ SER B -2 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ GLY B -1 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ GLY B 0 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ GLY B 1 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ GLY B 2 UNP Q5EP54 SEE REMARK 999
SEQADV 3LQZ SER B 3 UNP Q5EP54 SEE REMARK 999
SEQRES 1 A 181 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 A 181 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 A 181 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 A 181 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 A 181 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 A 181 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 A 181 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 A 181 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 A 181 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 A 181 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 A 181 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 A 181 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 A 181 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 181 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN
SEQRES 1 B 212 ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR 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
MODRES 3LQZ ASN B 19 ASN GLYCOSYLATION SITE
MODRES 3LQZ ASN A 118 ASN GLYCOSYLATION SITE
MODRES 3LQZ ASN A 78 ASN GLYCOSYLATION SITE
HET NAG A 182 14
HET NAG A 183 14
HET NAG B 190 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 3 NAG 3(C8 H15 N O6)
HELIX 1 1 LEU A 45 GLN A 50 1 6
HELIX 2 2 GLU A 55 ARG A 76 1 22
HELIX 3 3 THR B 49 LEU B 51 5 3
HELIX 4 4 GLY B 52 SER B 61 1 10
HELIX 5 5 GLN B 62 VAL B 72 1 11
HELIX 6 6 ARG B 75 LEU B 89 1 15
SHEET 1 A 8 GLU A 40 TRP A 43 0
SHEET 2 A 8 ASP A 29 ASP A 35 -1 N TYR A 33 O VAL A 42
SHEET 3 A 8 GLY A 20 PHE A 26 -1 N PHE A 26 O ASP A 29
SHEET 4 A 8 HIS A 5 GLN A 14 -1 N ALA A 10 O MET A 23
SHEET 5 A 8 LEU B 8 ALA B 17 -1 O CYS B 15 N SER A 7
SHEET 6 A 8 GLN B 22 TYR B 30 -1 O ILE B 29 N GLN B 10
SHEET 7 A 8 GLU B 33 ASP B 39 -1 O GLU B 33 N TYR B 30
SHEET 8 A 8 PHE B 45 ALA B 47 -1 O ARG B 46 N ARG B 37
SHEET 1 B 4 GLU A 88 PRO A 93 0
SHEET 2 B 4 ASN A 103 PHE A 112 -1 O ILE A 106 N PHE A 92
SHEET 3 B 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 B 4 VAL A 132 GLU A 134 -1 N ALA A 133 O TYR A 150
SHEET 1 C 4 GLU A 88 PRO A 93 0
SHEET 2 C 4 ASN A 103 PHE A 112 -1 O ILE A 106 N PHE A 92
SHEET 3 C 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 C 4 LEU A 138 PRO A 139 -1 N LEU A 138 O HIS A 146
SHEET 1 D 4 GLU A 126 LEU A 127 0
SHEET 2 D 4 ASN A 118 CYS A 123 -1 N CYS A 123 O GLU A 126
SHEET 3 D 4 TYR A 161 GLU A 166 -1 O GLU A 166 N ASN A 118
SHEET 4 D 4 LEU A 174 TRP A 178 -1 O LYS A 176 N CYS A 163
SHEET 1 E 4 VAL B 99 SER B 100 0
SHEET 2 E 4 LEU B 112 PHE B 120 -1 O VAL B 114 N SER B 100
SHEET 3 E 4 PHE B 153 GLU B 160 -1 O ILE B 155 N VAL B 117
SHEET 4 E 4 VAL B 141 SER B 142 -1 N VAL B 141 O MET B 158
SHEET 1 F 4 VAL B 99 SER B 100 0
SHEET 2 F 4 LEU B 112 PHE B 120 -1 O VAL B 114 N SER B 100
SHEET 3 F 4 PHE B 153 GLU B 160 -1 O ILE B 155 N VAL B 117
SHEET 4 F 4 ILE B 146 ARG B 147 -1 N ILE B 146 O GLN B 154
SHEET 1 G 4 GLN B 134 GLU B 135 0
SHEET 2 G 4 ILE B 125 LEU B 131 -1 N LEU B 131 O GLN B 134
SHEET 3 G 4 TYR B 169 HIS B 175 -1 O GLN B 172 N ARG B 128
SHEET 4 G 4 THR B 183 TRP B 186 -1 O VAL B 184 N CYS B 171
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.06
SSBOND 2 CYS B 15 CYS B 77 1555 1555 2.06
SSBOND 3 CYS B 115 CYS B 171 1555 1555 2.05
LINK ND2 ASN A 78 C1 NAG A 183 1555 1555 1.46
LINK ND2 ASN A 118 C1 NAG A 182 1555 1555 1.46
LINK ND2 ASN B 19 C1 NAG B 190 1555 1555 1.45
CISPEP 1 PHE A 113 PRO A 114 0 -0.90
CISPEP 2 TYR B 121 PRO B 122 0 -1.30
CRYST1 157.282 157.282 61.805 90.00 90.00 120.00 P 31 2 1 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 0.006362 0.003673 0.000000 0.00000
SCALE2 0.000000 0.007347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016172 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
