HEADER IMMUNE SYSTEM 29-AUG-17 6ATZ
TITLE HLA-DRB1*1402 IN COMPLEX WITH CITRULLINATED FIBRINOGEN PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 29-205;
COMPND 5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MHC CLASS II ANTIGEN;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: UNP RESIDUES 32-219;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: FIBRINOGEN BETA CHAIN;
COMPND 14 CHAIN: E, F;
COMPND 15 FRAGMENT: RESIDUES 69-81;
COMPND 16 SYNONYM: FIBRINOGEN BETA- 74CIT69-81;
COMPND 17 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-DRA, HLA-DRA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768;
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-DRB1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606
KEYWDS HLA, MHC, CITRULLINE, RHEUMATOID ARTHRITIS, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.T.TING,S.W.SCALLY,J.ROSSJOHN
REVDAT 3 29-JUL-20 6ATZ 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 18-OCT-17 6ATZ 1 JRNL
REVDAT 1 20-SEP-17 6ATZ 0
JRNL AUTH S.W.SCALLY,S.C.LAW,Y.T.TING,J.V.HEEMST,J.SOKOLOVE,
JRNL AUTH 2 A.J.DEUTSCH,E.BRIDIE CLEMENS,A.K.MOUSTAKAS,G.K.PAPADOPOULOS,
JRNL AUTH 3 D.V.WOUDE,I.SMOLIK,C.A.HITCHON,D.B.ROBINSON,E.D.FERUCCI,
JRNL AUTH 4 C.N.BERNSTEIN,X.MENG,V.ANAPARTI,T.HUIZINGA,K.KEDZIERSKA,
JRNL AUTH 5 H.H.REID,S.RAYCHAUDHURI,R.E.TOES,J.ROSSJOHN,H.EL-GABALAWY,
JRNL AUTH 6 R.THOMAS
JRNL TITL MOLECULAR BASIS FOR INCREASED SUSCEPTIBILITY OF INDIGENOUS
JRNL TITL 2 NORTH AMERICANS TO SEROPOSITIVE RHEUMATOID ARTHRITIS.
JRNL REF ANN. RHEUM. DIS. V. 76 1915 2017
JRNL REFN ISSN 1468-2060
JRNL PMID 28801345
JRNL DOI 10.1136/ANNRHEUMDIS-2017-211300
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 24007
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.610
REMARK 3 FREE R VALUE TEST SET COUNT : 1106
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 45.4846 - 5.3975 0.99 2928 170 0.2131 0.2168
REMARK 3 2 5.3975 - 4.2852 1.00 2859 157 0.1602 0.1859
REMARK 3 3 4.2852 - 3.7438 0.99 2868 148 0.1715 0.2135
REMARK 3 4 3.7438 - 3.4017 0.99 2858 125 0.1938 0.2593
REMARK 3 5 3.4017 - 3.1579 0.99 2863 115 0.2214 0.2545
REMARK 3 6 3.1579 - 2.9718 0.99 2847 137 0.2342 0.3220
REMARK 3 7 2.9718 - 2.8230 0.99 2833 140 0.2614 0.3715
REMARK 3 8 2.8230 - 2.7001 0.99 2845 114 0.2547 0.3308
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.83
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 : 0.002 6322
REMARK 3 ANGLE : 0.572 8608
REMARK 3 CHIRALITY : 0.044 934
REMARK 3 PLANARITY : 0.003 1115
REMARK 3 DIHEDRAL : 14.582 3656
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN B AND (RESID 3 THROUGH 21 OR
REMARK 3 (RESID 22 THROUGH 23 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 24 THROUGH 34 OR (RESID 35 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 36 THROUGH 51 OR
REMARK 3 RESID 53 THROUGH 97 OR RESID 99 THROUGH
REMARK 3 137 OR (RESID 138 AND (NAME N OR NAME CA
REMARK 3 OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 139 THROUGH 161 OR RESID 163
REMARK 3 THROUGH 167 OR RESID 169 THROUGH 190))
REMARK 3 SELECTION : (CHAIN D AND (RESID 3 THROUGH 51 OR RESID
REMARK 3 53 THROUGH 97 OR RESID 99 THROUGH 161 OR
REMARK 3 RESID 163 THROUGH 188 OR (RESID 189
REMARK 3 THROUGH 190 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB ))))
REMARK 3 ATOM PAIRS NUMBER : 2247
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ATZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229813.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
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 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24028
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.48100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4MCY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0.2 M POTASSIUM NITRATE,
REMARK 280 0.1 M BIS-TRIS PROPANE, PH 7.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 36.44250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F
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 GLY D 168
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 GLU A 40 CG CD OE1 OE2
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 ARG A 100 CG CD NE CZ NH1 NH2
REMARK 470 THR A 130 OG1 CG2
REMARK 470 ARG B 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 65 CG CD CE NZ
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 LEU B 109 CG CD1 CD2
REMARK 470 GLN B 110 CG CD OE1 NE2
REMARK 470 ARG B 189 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 38 CG CD CE NZ
REMARK 470 LYS C 39 CG CD CE NZ
REMARK 470 GLU C 40 CG CD OE1 OE2
REMARK 470 GLU C 46 CG CD OE1 OE2
REMARK 470 GLU C 71 CG CD OE1 OE2
REMARK 470 ARG C 100 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 141 CG CD OE1 OE2
REMARK 470 ASP C 171 CG OD1 OD2
REMARK 470 GLU C 172 CG CD OE1 OE2
REMARK 470 GLU D 22 CG CD OE1 OE2
REMARK 470 ARG D 23 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 35 CG CD OE1 OE2
REMARK 470 GLU D 52 CG CD OE1 OE2
REMARK 470 LYS D 65 CG CD CE NZ
REMARK 470 LYS D 105 CG CD CE NZ
REMARK 470 LEU D 109 CG CD1 CD2
REMARK 470 GLN D 110 CG CD OE1 NE2
REMARK 470 GLU D 138 CG CD OE1 OE2
REMARK 470 LYS E 8 CG CD CE NZ
REMARK 470 LYS F 8 CG CD CE NZ
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 ND2 ASN C 78 O5 NAG C 201 1.95
REMARK 500 CG ASN A 78 C1 NAG A 201 2.06
REMARK 500 O HOH B 313 O HOH B 317 2.08
REMARK 500 ND2 ASN A 78 C2 NAG A 201 2.17
REMARK 500 OD1 ASN A 78 C1 NAG A 201 2.19
REMARK 500 O HOH A 329 O HOH B 311 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP B 76 NH1 ARG B 166 1455 2.19
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 ARG A 100 15.32 58.95
REMARK 500 HIS A 143 3.03 58.83
REMARK 500 ASN B 33 -113.84 59.05
REMARK 500 THR B 90 -65.35 -128.97
REMARK 500 HIS B 112 96.80 -64.78
REMARK 500 ASN D 33 -113.03 57.08
REMARK 500 THR D 90 -64.96 -130.02
REMARK 500 HIS D 112 95.97 -67.20
REMARK 500 ALA F 10 -179.32 -68.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ATI RELATED DB: PDB
REMARK 900 RELATED ID: 6ATF RELATED DB: PDB
DBREF 6ATZ A 4 180 UNP P01903 DRA_HUMAN 29 205
DBREF1 6ATZ B 3 190 UNP A0A0A1I7H6_HUMAN
DBREF2 6ATZ B A0A0A1I7H6 32 219
DBREF 6ATZ C 4 180 UNP P01903 DRA_HUMAN 29 205
DBREF1 6ATZ D 3 190 UNP A0A0A1I7H6_HUMAN
DBREF2 6ATZ D A0A0A1I7H6 32 219
DBREF 6ATZ E 0 11 PDB 6ATZ 6ATZ 0 11
DBREF 6ATZ F 0 11 PDB 6ATZ 6ATZ 0 11
SEQRES 1 A 177 GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN PRO
SEQRES 2 A 177 ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY ASP
SEQRES 3 A 177 GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR VAL
SEQRES 4 A 177 TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE GLU
SEQRES 5 A 177 ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS ALA
SEQRES 6 A 177 ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR PRO
SEQRES 7 A 177 ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR ASN
SEQRES 8 A 177 SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE CYS
SEQRES 9 A 177 PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL THR
SEQRES 10 A 177 TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL SER
SEQRES 11 A 177 GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE ARG
SEQRES 12 A 177 LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU ASP
SEQRES 13 A 177 VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP GLU
SEQRES 14 A 177 PRO LEU LEU LYS HIS TRP GLU PHE
SEQRES 1 B 188 THR ARG PRO ARG PHE LEU GLU TYR SER THR SER GLU CYS
SEQRES 2 B 188 HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE LEU GLU
SEQRES 3 B 188 ARG TYR PHE HIS ASN GLN GLU GLU ASN VAL ARG PHE ASP
SEQRES 4 B 188 SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU GLY
SEQRES 5 B 188 ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS ASP LEU
SEQRES 6 B 188 LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR CYS ARG
SEQRES 7 B 188 HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL GLN ARG
SEQRES 8 B 188 ARG VAL HIS PRO LYS VAL THR VAL TYR PRO SER LYS THR
SEQRES 9 B 188 GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL
SEQRES 10 B 188 SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG TRP PHE
SEQRES 11 B 188 ARG ASN GLY GLN GLU GLU LYS THR GLY VAL VAL SER THR
SEQRES 12 B 188 GLY LEU ILE HIS ASN GLY ASP TRP THR PHE GLN THR LEU
SEQRES 13 B 188 VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU VAL TYR
SEQRES 14 B 188 THR CYS GLN VAL GLU HIS PRO SER VAL THR SER PRO LEU
SEQRES 15 B 188 THR VAL GLU TRP ARG ALA
SEQRES 1 C 177 GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN PRO
SEQRES 2 C 177 ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY ASP
SEQRES 3 C 177 GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR VAL
SEQRES 4 C 177 TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE GLU
SEQRES 5 C 177 ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS ALA
SEQRES 6 C 177 ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR PRO
SEQRES 7 C 177 ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR ASN
SEQRES 8 C 177 SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE CYS
SEQRES 9 C 177 PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL THR
SEQRES 10 C 177 TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL SER
SEQRES 11 C 177 GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE ARG
SEQRES 12 C 177 LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU ASP
SEQRES 13 C 177 VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP GLU
SEQRES 14 C 177 PRO LEU LEU LYS HIS TRP GLU PHE
SEQRES 1 D 188 THR ARG PRO ARG PHE LEU GLU TYR SER THR SER GLU CYS
SEQRES 2 D 188 HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE LEU GLU
SEQRES 3 D 188 ARG TYR PHE HIS ASN GLN GLU GLU ASN VAL ARG PHE ASP
SEQRES 4 D 188 SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU GLY
SEQRES 5 D 188 ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS ASP LEU
SEQRES 6 D 188 LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR CYS ARG
SEQRES 7 D 188 HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL GLN ARG
SEQRES 8 D 188 ARG VAL HIS PRO LYS VAL THR VAL TYR PRO SER LYS THR
SEQRES 9 D 188 GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL
SEQRES 10 D 188 SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG TRP PHE
SEQRES 11 D 188 ARG ASN GLY GLN GLU GLU LYS THR GLY VAL VAL SER THR
SEQRES 12 D 188 GLY LEU ILE HIS ASN GLY ASP TRP THR PHE GLN THR LEU
SEQRES 13 D 188 VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU VAL TYR
SEQRES 14 D 188 THR CYS GLN VAL GLU HIS PRO SER VAL THR SER PRO LEU
SEQRES 15 D 188 THR VAL GLU TRP ARG ALA
SEQRES 1 E 12 GLY GLY TYR ARG ALA CIR PRO ALA LYS ALA ALA THR
SEQRES 1 F 12 GLY GLY TYR ARG ALA CIR PRO ALA LYS ALA ALA THR
MODRES 6ATZ CIR E 5 ARG MODIFIED RESIDUE
MODRES 6ATZ CIR F 5 ARG MODIFIED RESIDUE
HET CIR E 5 22
HET CIR F 5 22
HET NAG A 201 27
HET NAG A 202 27
HET B3P B 201 45
HET NAG C 201 27
HET NAG C 202 27
HETNAM CIR CITRULLINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-
HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
FORMUL 5 CIR 2(C6 H13 N3 O3)
FORMUL 7 NAG 4(C8 H15 N O6)
FORMUL 9 B3P C11 H26 N2 O6
FORMUL 12 HOH *112(H2 O)
HELIX 1 AA1 LEU A 45 ARG A 50 1 6
HELIX 2 AA2 GLU A 55 SER A 77 1 23
HELIX 3 AA3 THR B 51 LEU B 53 5 3
HELIX 4 AA4 GLY B 54 SER B 63 1 10
HELIX 5 AA5 GLN B 64 ALA B 73 1 10
HELIX 6 AA6 ALA B 73 TYR B 78 1 6
HELIX 7 AA7 TYR B 78 GLY B 86 1 9
HELIX 8 AA8 GLU B 87 THR B 90 5 4
HELIX 9 AA9 LEU C 45 PHE C 51 5 7
HELIX 10 AB1 GLU C 55 SER C 77 1 23
HELIX 11 AB2 THR D 51 LEU D 53 5 3
HELIX 12 AB3 GLY D 54 SER D 63 1 10
HELIX 13 AB4 GLN D 64 ALA D 73 1 10
HELIX 14 AB5 ALA D 73 TYR D 78 1 6
HELIX 15 AB6 TYR D 78 GLY D 86 1 9
HELIX 16 AB7 GLU D 87 THR D 90 5 4
SHEET 1 AA1 8 GLU A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N HIS A 33 O VAL A 42
SHEET 3 AA1 8 SER A 19 PHE A 26 -1 N PHE A 26 O ASP A 29
SHEET 4 AA1 8 HIS A 5 ASN A 15 -1 N ILE A 8 O ASP A 25
SHEET 5 AA1 8 PHE B 7 PHE B 18 -1 O PHE B 17 N HIS A 5
SHEET 6 AA1 8 ARG B 23 HIS B 32 -1 O ARG B 25 N HIS B 16
SHEET 7 AA1 8 GLU B 35 ASP B 41 -1 O ASN B 37 N TYR B 30
SHEET 8 AA1 8 TYR B 47 ALA B 49 -1 O ARG B 48 N ARG B 39
SHEET 1 AA2 4 GLU A 88 THR A 93 0
SHEET 2 AA2 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 AA2 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 AA2 4 SER A 133 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 AA3 4 GLU A 88 THR A 93 0
SHEET 2 AA3 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
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 ARG A 146
SHEET 1 AA4 4 LYS A 126 VAL A 128 0
SHEET 2 AA4 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS 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 TRP A 178 N TYR A 161
SHEET 1 AA5 4 LYS B 98 SER B 104 0
SHEET 2 AA5 4 LEU B 114 PHE B 122 -1 O LEU B 114 N SER B 104
SHEET 3 AA5 4 PHE B 155 GLU B 162 -1 O THR B 157 N VAL B 119
SHEET 4 AA5 4 VAL B 142 SER B 144 -1 N VAL B 143 O MET B 160
SHEET 1 AA6 4 LYS B 98 SER B 104 0
SHEET 2 AA6 4 LEU B 114 PHE B 122 -1 O LEU B 114 N SER B 104
SHEET 3 AA6 4 PHE B 155 GLU B 162 -1 O THR B 157 N VAL B 119
SHEET 4 AA6 4 ILE B 148 HIS B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 AA7 4 GLN B 136 GLU B 138 0
SHEET 2 AA7 4 GLU B 128 ARG B 133 -1 N ARG B 133 O GLN B 136
SHEET 3 AA7 4 VAL B 170 GLU B 176 -1 O GLN B 174 N ARG B 130
SHEET 4 AA7 4 LEU B 184 ARG B 189 -1 O LEU B 184 N VAL B 175
SHEET 1 AA8 8 GLU C 40 TRP C 43 0
SHEET 2 AA8 8 ASP C 29 ASP C 35 -1 N HIS C 33 O VAL C 42
SHEET 3 AA8 8 SER C 19 PHE C 26 -1 N PHE C 26 O ASP C 29
SHEET 4 AA8 8 HIS C 5 ASN C 15 -1 N ALA C 10 O MET C 23
SHEET 5 AA8 8 PHE D 7 PHE D 18 -1 O CYS D 15 N ILE C 7
SHEET 6 AA8 8 ARG D 23 HIS D 32 -1 O ARG D 25 N HIS D 16
SHEET 7 AA8 8 GLU D 35 ASP D 41 -1 O ASN D 37 N TYR D 30
SHEET 8 AA8 8 TYR D 47 ALA D 49 -1 O ARG D 48 N ARG D 39
SHEET 1 AA9 4 GLU C 88 THR C 93 0
SHEET 2 AA9 4 ASN C 103 PHE C 112 -1 O ILE C 106 N LEU C 92
SHEET 3 AA9 4 PHE C 145 PHE C 153 -1 O HIS C 149 N CYS C 107
SHEET 4 AA9 4 SER C 133 GLU C 134 -1 N SER C 133 O TYR C 150
SHEET 1 AB1 4 GLU C 88 THR C 93 0
SHEET 2 AB1 4 ASN C 103 PHE C 112 -1 O ILE C 106 N LEU C 92
SHEET 3 AB1 4 PHE C 145 PHE C 153 -1 O HIS C 149 N CYS C 107
SHEET 4 AB1 4 LEU C 138 PRO C 139 -1 N LEU C 138 O ARG C 146
SHEET 1 AB2 4 LYS C 126 VAL C 128 0
SHEET 2 AB2 4 ASN C 118 ARG C 123 -1 N TRP C 121 O VAL C 128
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 LEU C 174 N VAL C 165
SHEET 1 AB3 4 LYS D 98 SER D 104 0
SHEET 2 AB3 4 LEU D 114 PHE D 122 -1 O SER D 118 N THR D 100
SHEET 3 AB3 4 PHE D 155 GLU D 162 -1 O THR D 157 N VAL D 119
SHEET 4 AB3 4 VAL D 142 SER D 144 -1 N VAL D 143 O MET D 160
SHEET 1 AB4 4 LYS D 98 SER D 104 0
SHEET 2 AB4 4 LEU D 114 PHE D 122 -1 O SER D 118 N THR D 100
SHEET 3 AB4 4 PHE D 155 GLU D 162 -1 O THR D 157 N VAL D 119
SHEET 4 AB4 4 ILE D 148 HIS D 149 -1 N ILE D 148 O GLN D 156
SHEET 1 AB5 4 GLN D 136 GLU D 138 0
SHEET 2 AB5 4 GLU D 128 ARG D 133 -1 N ARG D 133 O GLN D 136
SHEET 3 AB5 4 VAL D 170 GLU D 176 -1 O GLN D 174 N ARG D 130
SHEET 4 AB5 4 LEU D 184 ARG D 189 -1 O LEU D 184 N VAL D 175
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.04
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.03
SSBOND 4 CYS C 107 CYS C 163 1555 1555 2.03
SSBOND 5 CYS D 15 CYS D 79 1555 1555 2.04
SSBOND 6 CYS D 117 CYS D 173 1555 1555 2.03
LINK ND2 ASN A 78 C1 NAG A 201 1555 1555 1.44
LINK ND2 ASN A 118 C1 NAG A 202 1555 1555 1.44
LINK ND2 ASN C 78 C1 NAG C 201 1555 1555 1.43
LINK ND2 ASN C 118 C1 NAG C 202 1555 1555 1.43
LINK C ALA E 4 N2 CIR E 5 1555 1555 1.34
LINK C1 CIR E 5 N PRO E 6 1555 1555 1.30
LINK C ALA F 4 N2 CIR F 5 1555 1555 1.33
LINK C1 CIR F 5 N PRO F 6 1555 1555 1.31
CISPEP 1 ASN A 15 PRO A 16 0 -2.25
CISPEP 2 THR A 113 PRO A 114 0 0.21
CISPEP 3 TYR B 123 PRO B 124 0 2.93
CISPEP 4 ASN C 15 PRO C 16 0 1.31
CISPEP 5 THR C 113 PRO C 114 0 0.59
CISPEP 6 TYR D 123 PRO D 124 0 3.08
CRYST1 66.881 72.885 95.316 90.00 107.40 90.00 P 1 21 1 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 0.014952 0.000000 0.004685 0.00000
SCALE2 0.000000 0.013720 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010994 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
