HEADER IMMUNE SYSTEM 10-SEP-18 6MFF
TITLE HLA-DQ2-GLIA-OMEGA1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ ALPHA 1 CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DC-1 ALPHA CHAIN,DC-ALPHA,HLA-DCA,MHC CLASS II DQA1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MHC CLASS II HLA-DQ-BETA-1 - DQ2-GLIA-OMEGA1 CHIMERIC
COMPND 8 PROTEIN;
COMPND 9 CHAIN: C;
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-DQA1;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
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-DQB1;
SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS IMMUNE COMPLEX, CELIAC DISEASE, GLIADIN EPITOPE, TCR CROSS-
KEYWDS 2 REACTIVITY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PETERSEN,L.CIACCHI,J.ROSSJOHN
REVDAT 4 29-JUL-20 6MFF 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 30-JAN-19 6MFF 1 JRNL
REVDAT 2 12-DEC-18 6MFF 1 JRNL
REVDAT 1 21-NOV-18 6MFF 0
JRNL AUTH S.DAHAL-KOIRALA,L.CIACCHI,J.PETERSEN,L.F.RISNES,R.S.NEUMANN,
JRNL AUTH 2 A.CHRISTOPHERSEN,K.E.A.LUNDIN,H.H.REID,S.W.QIAO,J.ROSSJOHN,
JRNL AUTH 3 L.M.SOLLID
JRNL TITL DISCRIMINATIVE T-CELL RECEPTOR RECOGNITION OF HIGHLY
JRNL TITL 2 HOMOLOGOUS HLA-DQ2-BOUND GLUTEN EPITOPES.
JRNL REF J. BIOL. CHEM. V. 294 941 2019
JRNL REFN ESSN 1083-351X
JRNL PMID 30455354
JRNL DOI 10.1074/JBC.RA118.005736
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 15303
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 771
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.9427 - 4.7234 1.00 2557 116 0.1746 0.1662
REMARK 3 2 4.7234 - 3.7496 1.00 2412 124 0.1670 0.2207
REMARK 3 3 3.7496 - 3.2758 1.00 2442 120 0.2113 0.2835
REMARK 3 4 3.2758 - 2.9763 1.00 2385 138 0.2628 0.3058
REMARK 3 5 2.9763 - 2.7630 1.00 2381 122 0.2794 0.3277
REMARK 3 6 2.7630 - 2.6001 1.00 2355 151 0.3656 0.4207
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.520
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 3113
REMARK 3 ANGLE : 0.575 4251
REMARK 3 CHIRALITY : 0.051 476
REMARK 3 PLANARITY : 0.004 548
REMARK 3 DIHEDRAL : 13.212 1850
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7739 17.4168 20.7540
REMARK 3 T TENSOR
REMARK 3 T11: 1.1748 T22: 0.5248
REMARK 3 T33: 0.5766 T12: -0.1464
REMARK 3 T13: -0.3801 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 7.9837 L22: 8.2285
REMARK 3 L33: 2.3727 L12: -2.3892
REMARK 3 L13: -2.1066 L23: -2.8573
REMARK 3 S TENSOR
REMARK 3 S11: -1.2585 S12: 1.3183 S13: 1.4199
REMARK 3 S21: 0.1466 S22: -0.2319 S23: 0.1223
REMARK 3 S31: -1.6509 S32: 0.6659 S33: 1.0831
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0589 8.8066 22.3053
REMARK 3 T TENSOR
REMARK 3 T11: 0.5588 T22: 0.3808
REMARK 3 T33: 0.3365 T12: -0.0254
REMARK 3 T13: -0.1121 T23: -0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 4.9917 L22: 6.4457
REMARK 3 L33: 3.2421 L12: -1.4910
REMARK 3 L13: 0.2132 L23: 0.0498
REMARK 3 S TENSOR
REMARK 3 S11: -0.2930 S12: -0.2663 S13: 0.4614
REMARK 3 S21: 0.4329 S22: 0.0145 S23: 0.2940
REMARK 3 S31: -0.7423 S32: -0.0693 S33: 0.2813
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.5319 -10.3542 15.4960
REMARK 3 T TENSOR
REMARK 3 T11: 0.4809 T22: 0.4282
REMARK 3 T33: 0.3934 T12: -0.0131
REMARK 3 T13: -0.1487 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 3.3012 L22: 5.8855
REMARK 3 L33: 3.4893 L12: 1.8949
REMARK 3 L13: 0.5146 L23: -0.4936
REMARK 3 S TENSOR
REMARK 3 S11: -0.2305 S12: 0.2792 S13: 0.1697
REMARK 3 S21: -0.9190 S22: 0.2602 S23: 0.9574
REMARK 3 S31: 0.1852 S32: -0.5950 S33: -0.0795
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 39 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2950 13.4784 14.0581
REMARK 3 T TENSOR
REMARK 3 T11: 0.6932 T22: 0.5374
REMARK 3 T33: 0.3769 T12: -0.1502
REMARK 3 T13: -0.1717 T23: 0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 3.0088 L22: 5.4358
REMARK 3 L33: 2.5150 L12: 0.9343
REMARK 3 L13: -0.4687 L23: -0.7290
REMARK 3 S TENSOR
REMARK 3 S11: -0.1814 S12: 0.1976 S13: 0.4549
REMARK 3 S21: -0.1656 S22: -0.0820 S23: -0.2293
REMARK 3 S31: -0.8250 S32: 0.3484 S33: 0.2219
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 130 THROUGH 226 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6356 -24.9612 11.1349
REMARK 3 T TENSOR
REMARK 3 T11: 0.9095 T22: 0.4892
REMARK 3 T33: 0.5782 T12: 0.2301
REMARK 3 T13: 0.1061 T23: 0.1408
REMARK 3 L TENSOR
REMARK 3 L11: 3.2507 L22: 9.1356
REMARK 3 L33: 4.5262 L12: -1.6317
REMARK 3 L13: -0.5672 L23: 0.7048
REMARK 3 S TENSOR
REMARK 3 S11: 0.1132 S12: 0.1544 S13: -0.6202
REMARK 3 S21: -0.6162 S22: -0.1624 S23: -1.0149
REMARK 3 S31: 1.5371 S32: 0.5902 S33: 0.0424
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6MFF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000235851.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15331
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 67.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
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 (%): 51.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG3350 AND 0.1 M NAH2PO4, PH 6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 53.52500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.52500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 46.93500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.30500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.93500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.30500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.52500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.93500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.30500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.52500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.93500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.30500
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 GLU A -1
REMARK 465 ASP A 0
REMARK 465 GLU A 181
REMARK 465 SER A 182
REMARK 465 GLY A 183
REMARK 465 ASP A 184
REMARK 465 ASP A 185
REMARK 465 ASP A 186
REMARK 465 ASP A 187
REMARK 465 LYS A 188
REMARK 465 GLY C 22
REMARK 465 SER C 23
REMARK 465 GLY C 24
REMARK 465 GLY C 25
REMARK 465 SER C 26
REMARK 465 ILE C 27
REMARK 465 GLU C 28
REMARK 465 GLY C 29
REMARK 465 ARG C 30
REMARK 465 GLY C 31
REMARK 465 GLY C 32
REMARK 465 SER C 33
REMARK 465 GLY C 34
REMARK 465 ALA C 35
REMARK 465 SER C 36
REMARK 465 ARG C 37
REMARK 465 ASP C 38
REMARK 465 THR C 142
REMARK 465 GLU C 143
REMARK 465 ALA C 144
REMARK 465 LEU C 145
REMARK 465 ASN C 146
REMARK 465 HIS C 147
REMARK 465 HIS C 148
REMARK 465 GLN C 227
REMARK 465 SER C 228
REMARK 465 THR C 229
REMARK 465 GLY C 230
REMARK 465 GLY C 231
REMARK 465 ASP C 232
REMARK 465 ASP C 233
REMARK 465 ASP C 234
REMARK 465 ASP C 235
REMARK 465 LYS C 236
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 172 CG CD CE NZ
REMARK 470 GLN C 0 CG CD OE1 NE2
REMARK 470 ARG C 141 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 203 CG CD NE CZ NH1 NH2
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 ASP A 35 95.03 -67.59
REMARK 500 PRO A 115 67.18 -68.27
REMARK 500 VAL A 117 144.03 -170.06
REMARK 500 ASN C 69 -105.98 53.42
REMARK 500 THR C 125 -83.30 -135.76
REMARK 500 ASP C 157 74.77 57.45
REMARK 500 ASP C 171 18.48 59.66
REMARK 500 ASP C 188 35.04 -99.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6MFF A -1 181 UNP P01909 DQA1_HUMAN 24 206
DBREF 6MFF C 0 10 PDB 6MFF 6MFF 0 10
DBREF 6MFF C 37 228 UNP O19712 O19712_HUMAN 1 192
SEQADV 6MFF SER A 182 UNP P01909 EXPRESSION TAG
SEQADV 6MFF GLY A 183 UNP P01909 EXPRESSION TAG
SEQADV 6MFF ASP A 184 UNP P01909 EXPRESSION TAG
SEQADV 6MFF ASP A 185 UNP P01909 EXPRESSION TAG
SEQADV 6MFF ASP A 186 UNP P01909 EXPRESSION TAG
SEQADV 6MFF ASP A 187 UNP P01909 EXPRESSION TAG
SEQADV 6MFF LYS A 188 UNP P01909 EXPRESSION TAG
SEQADV 6MFF GLY C 22 PDB LINKER
SEQADV 6MFF SER C 23 PDB LINKER
SEQADV 6MFF GLY C 24 PDB LINKER
SEQADV 6MFF GLY C 25 PDB LINKER
SEQADV 6MFF SER C 26 PDB LINKER
SEQADV 6MFF ILE C 27 PDB LINKER
SEQADV 6MFF GLU C 28 PDB LINKER
SEQADV 6MFF GLY C 29 PDB LINKER
SEQADV 6MFF ARG C 30 PDB LINKER
SEQADV 6MFF GLY C 31 PDB LINKER
SEQADV 6MFF GLY C 32 PDB LINKER
SEQADV 6MFF SER C 33 PDB LINKER
SEQADV 6MFF GLY C 34 PDB LINKER
SEQADV 6MFF ALA C 35 PDB LINKER
SEQADV 6MFF SER C 36 PDB LINKER
SEQADV 6MFF THR C 229 UNP O19712 EXPRESSION TAG
SEQADV 6MFF GLY C 230 UNP O19712 EXPRESSION TAG
SEQADV 6MFF GLY C 231 UNP O19712 EXPRESSION TAG
SEQADV 6MFF ASP C 232 UNP O19712 EXPRESSION TAG
SEQADV 6MFF ASP C 233 UNP O19712 EXPRESSION TAG
SEQADV 6MFF ASP C 234 UNP O19712 EXPRESSION TAG
SEQADV 6MFF ASP C 235 UNP O19712 EXPRESSION TAG
SEQADV 6MFF LYS C 236 UNP O19712 EXPRESSION TAG
SEQRES 1 A 190 GLU ASP ILE VAL ALA ASP HIS VAL ALA SER TYR GLY VAL
SEQRES 2 A 190 ASN LEU TYR GLN SER TYR GLY PRO SER GLY GLN TYR THR
SEQRES 3 A 190 HIS GLU PHE ASP GLY ASP GLU GLN PHE TYR VAL ASP LEU
SEQRES 4 A 190 GLY ARG LYS GLU THR VAL TRP CYS LEU PRO VAL LEU ARG
SEQRES 5 A 190 GLN PHE ARG PHE ASP PRO GLN PHE ALA LEU THR ASN ILE
SEQRES 6 A 190 ALA VAL LEU LYS HIS ASN LEU ASN SER LEU ILE LYS ARG
SEQRES 7 A 190 SER ASN SER THR ALA ALA THR ASN GLU VAL PRO GLU VAL
SEQRES 8 A 190 THR VAL PHE SER LYS SER PRO VAL THR LEU GLY GLN PRO
SEQRES 9 A 190 ASN ILE LEU ILE CYS LEU VAL ASP ASN ILE PHE PRO PRO
SEQRES 10 A 190 VAL VAL ASN ILE THR TRP LEU SER ASN GLY HIS SER VAL
SEQRES 11 A 190 THR GLU GLY VAL SER GLU THR SER PHE LEU SER LYS SER
SEQRES 12 A 190 ASP HIS SER PHE PHE LYS ILE SER TYR LEU THR LEU LEU
SEQRES 13 A 190 PRO SER ALA GLU GLU SER TYR ASP CYS LYS VAL GLU HIS
SEQRES 14 A 190 TRP GLY LEU ASP LYS PRO LEU LEU LYS HIS TRP GLU PRO
SEQRES 15 A 190 GLU SER GLY ASP ASP ASP ASP LYS
SEQRES 1 C 226 GLN PRO PHE PRO GLN PRO GLU GLN PRO PHE PRO GLY SER
SEQRES 2 C 226 GLY GLY SER ILE GLU GLY ARG GLY GLY SER GLY ALA SER
SEQRES 3 C 226 ARG ASP SER PRO GLU ASP PHE VAL TYR GLN PHE LYS GLY
SEQRES 4 C 226 MET CYS TYR PHE THR ASN GLY THR GLU ARG VAL ARG LEU
SEQRES 5 C 226 VAL SER ARG SER ILE TYR ASN ARG GLU GLU ILE VAL ARG
SEQRES 6 C 226 PHE ASP SER ASP VAL GLY GLU PHE ARG ALA VAL THR LEU
SEQRES 7 C 226 LEU GLY LEU PRO ALA ALA GLU TYR TRP ASN SER GLN LYS
SEQRES 8 C 226 ASP ILE LEU GLU ARG LYS ARG ALA ALA VAL ASP ARG VAL
SEQRES 9 C 226 CYS ARG HIS ASN TYR GLN LEU GLU LEU ARG THR THR LEU
SEQRES 10 C 226 GLN ARG ARG VAL GLU PRO THR VAL THR ILE SER PRO SER
SEQRES 11 C 226 ARG THR GLU ALA LEU ASN HIS HIS ASN LEU LEU VAL CYS
SEQRES 12 C 226 SER VAL THR ASP PHE TYR PRO ALA GLN ILE LYS VAL ARG
SEQRES 13 C 226 TRP PHE ARG ASN ASP GLN GLU GLU THR ALA GLY VAL VAL
SEQRES 14 C 226 SER THR PRO LEU ILE ARG ASN GLY ASP TRP THR PHE GLN
SEQRES 15 C 226 ILE LEU VAL MET LEU GLU MET THR PRO GLN ARG GLY ASP
SEQRES 16 C 226 VAL TYR THR CYS HIS VAL GLU HIS PRO SER LEU GLN SER
SEQRES 17 C 226 PRO ILE THR VAL GLU TRP ARG ALA GLN SER THR GLY GLY
SEQRES 18 C 226 ASP ASP ASP ASP LYS
HET NAG A1001 14
HET NAG A1002 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 5 HOH *25(H2 O)
HELIX 1 AA1 LEU A 45 PHE A 51 5 7
HELIX 2 AA2 ASP A 55 SER A 77 1 23
HELIX 3 AA3 THR C 87 LEU C 89 5 3
HELIX 4 AA4 GLY C 90 GLN C 100 1 11
HELIX 5 AA5 GLN C 100 ALA C 109 1 10
HELIX 6 AA6 ALA C 109 VAL C 114 1 6
HELIX 7 AA7 VAL C 114 ARG C 124 1 11
HELIX 8 AA8 THR C 125 ARG C 129 5 5
SHEET 1 AA1 8 GLU A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N TYR A 33 O VAL A 42
SHEET 3 AA1 8 SER A 19 PHE A 26 -1 N HIS A 24 O GLN A 31
SHEET 4 AA1 8 HIS A 5 GLN A 14 -1 N VAL A 10 O THR A 23
SHEET 5 AA1 8 VAL C 44 THR C 54 -1 O GLY C 49 N TYR A 9
SHEET 6 AA1 8 ARG C 59 TYR C 68 -1 O ILE C 67 N GLN C 46
SHEET 7 AA1 8 GLU C 71 ASP C 77 -1 O GLU C 71 N TYR C 68
SHEET 8 AA1 8 PHE C 83 ALA C 85 -1 O ARG C 84 N ARG C 75
SHEET 1 AA2 4 GLU A 88 SER A 93 0
SHEET 2 AA2 4 ASN A 103 ILE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 AA2 4 PHE A 145 LEU A 153 -1 O PHE A 145 N ILE A 112
SHEET 4 AA2 4 VAL A 132 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 AA3 4 GLU A 88 SER A 93 0
SHEET 2 AA3 4 ASN A 103 ILE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 AA3 4 PHE A 145 LEU A 153 -1 O PHE A 145 N ILE A 112
SHEET 4 AA3 4 LEU A 138 SER A 139 -1 N LEU A 138 O PHE A 146
SHEET 1 AA4 4 HIS A 126 VAL A 128 0
SHEET 2 AA4 4 ASN A 118 SER A 123 -1 N SER A 123 O HIS A 126
SHEET 3 AA4 4 TYR A 161 GLU A 166 -1 O LYS A 164 N THR A 120
SHEET 4 AA4 4 LEU A 174 TRP A 178 -1 O LYS A 176 N CYS A 163
SHEET 1 AA5 4 THR C 134 PRO C 139 0
SHEET 2 AA5 4 LEU C 150 PHE C 158 -1 O SER C 154 N THR C 136
SHEET 3 AA5 4 PHE C 191 GLU C 198 -1 O LEU C 197 N LEU C 151
SHEET 4 AA5 4 VAL C 178 SER C 180 -1 N VAL C 179 O MET C 196
SHEET 1 AA6 4 THR C 134 PRO C 139 0
SHEET 2 AA6 4 LEU C 150 PHE C 158 -1 O SER C 154 N THR C 136
SHEET 3 AA6 4 PHE C 191 GLU C 198 -1 O LEU C 197 N LEU C 151
SHEET 4 AA6 4 ILE C 184 ARG C 185 -1 N ILE C 184 O GLN C 192
SHEET 1 AA7 4 GLN C 172 GLU C 174 0
SHEET 2 AA7 4 LYS C 164 ARG C 169 -1 N ARG C 169 O GLN C 172
SHEET 3 AA7 4 TYR C 207 GLU C 212 -1 O HIS C 210 N ARG C 166
SHEET 4 AA7 4 ILE C 220 TRP C 224 -1 O ILE C 220 N VAL C 211
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS C 51 CYS C 115 1555 1555 2.03
SSBOND 3 CYS C 153 CYS C 209 1555 1555 2.03
LINK ND2 ASN A 78 C1 NAG A1002 1555 1555 1.44
LINK ND2 ASN A 118 C1 NAG A1001 1555 1555 1.45
CISPEP 1 TYR A 9 GLY A 9A 0 -3.56
CISPEP 2 GLY A 17 PRO A 18 0 -1.14
CISPEP 3 PHE A 113 PRO A 114 0 -0.82
CISPEP 4 TYR C 159 PRO C 160 0 4.40
CRYST1 93.870 96.610 107.050 90.00 90.00 90.00 C 2 2 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 0.010653 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009341 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
