Header list of 1iie.pdb file
Complete list - t 27 2 Bytes
HEADER MAJOR HISTOCOMPATIBILITY COMPLEX 02-FEB-99 1IIE
TITLE HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN);
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: ECTOPLASMIC TRIMERIZATION DOMAIN (RESIDUES 118-192);
COMPND 5 SYNONYM: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, GAMMA CHAIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: TYPE II TRANSMEMBRANE PROTEIN;
SOURCE 6 GENE: CD74 OR DHLAG;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: XA90;
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: II H94-216 (I94);
SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PQE9;
SOURCE 14 OTHER_DETAILS: TRYPSIN-GENERATED FRAGMENT OF RECOMBINANT DOMAIN
KEYWDS MAJOR HISTOCOMPATIBILITY COMPLEX, ANTIGEN PROCESSING,
KEYWDS 2 OLIGOMERIZATION, CHAPERONIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.JASANOFF,G.WAGNER,D.C.WILEY
REVDAT 4 27-OCT-21 1IIE 1 REMARK
REVDAT 3 06-NOV-19 1IIE 1 REMARK
REVDAT 2 24-FEB-09 1IIE 1 VERSN
REVDAT 1 16-FEB-99 1IIE 0
JRNL AUTH A.JASANOFF,G.WAGNER,D.C.WILEY
JRNL TITL STRUCTURE OF A TRIMERIC DOMAIN OF THE MHC CLASS
JRNL TITL 2 II-ASSOCIATED CHAPERONIN AND TARGETING PROTEIN II.
JRNL REF EMBO J. V. 17 6812 1998
JRNL REFN ISSN 0261-4189
JRNL PMID 9843486
JRNL DOI 10.1093/EMBOJ/17.23.6812
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.JASANOFF
REMARK 1 TITL AN ASYMMETRIC DEUTERIUM LABELING STRATEGY TO IDENTIFY
REMARK 1 TITL 2 INTERPROTOMER AND INTRAPROTOMER NOES IN OLIGOMERIC PROTEINS
REMARK 1 REF J.BIOMOL.NMR V. 12 299 1998
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.-J.PARK,S.SADEGH-NASSERI,D.C.WILEY
REMARK 1 TITL INVARIANT CHAIN MADE IN ESCHERICHIA COLI HAS AN EXPOSED
REMARK 1 TITL 2 N-TERMINAL SEGMENT THAT BLOCKS ANTIGEN BINDING TO HLA-DR1
REMARK 1 TITL 3 AND A TRIMERIC C-TERMINAL SEGMENT THAT BINDS EMPTY HLA-DR1
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 92 11289 1995
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE TRIMER STRUCTURE WAS CALCULATED
REMARK 3 USING A SIMULATED ANNEALING PROTOCOL BASED ON THE DIMER
REMARK 3 REFINEMENT METHODS OF NILGES, PROTEINS 17 : 297-309 (1993)
REMARK 4
REMARK 4 1IIE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000436.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; HSQC; TRIPLE
REMARK 210 RESONANCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION, GOOD
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 14
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING DOUBLE- AND TRIPLE
REMARK 210 -RESONANCE EXPERIMENTS ON SAMPLES OF II 118-192 LABELED WITH
REMARK 210 COMBINATIONS OF 2H, 13C, AND 15N
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 O SER B 145 H ASN B 149 1.46
REMARK 500 O SER C 145 H ASN C 149 1.46
REMARK 500 O SER A 145 H ASN A 149 1.47
REMARK 500 O ARG C 151 H ASN C 155 1.59
REMARK 500 O PHE C 175 H ARG C 179 1.59
REMARK 500 O ARG B 151 H ASN B 155 1.59
REMARK 500 O ARG A 151 H ASN A 155 1.59
REMARK 500 O PHE A 175 H ARG A 179 1.59
REMARK 500 O LEU A 174 H SER A 178 1.60
REMARK 500 O LEU B 174 H SER B 178 1.60
REMARK 500 O LEU C 174 H SER C 178 1.60
REMARK 500 O PHE B 175 H ARG B 179 1.60
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 1 ASN A 120 -117.22 -113.20
REMARK 500 1 MET A 157 176.08 -58.33
REMARK 500 1 THR A 187 -152.08 -150.95
REMARK 500 1 ASN B 120 -117.05 -113.41
REMARK 500 1 MET B 157 176.10 -58.09
REMARK 500 1 THR B 187 -152.13 -151.06
REMARK 500 1 ASN C 120 -117.11 -113.07
REMARK 500 1 MET C 157 175.88 -58.18
REMARK 500 1 THR C 187 -152.09 -150.79
REMARK 500 2 THR A 122 -54.13 -167.64
REMARK 500 2 MET A 157 178.43 -57.90
REMARK 500 2 ALA A 189 69.31 -159.38
REMARK 500 2 THR B 122 -54.07 -167.66
REMARK 500 2 MET B 157 178.26 -57.91
REMARK 500 2 ALA B 189 69.25 -159.16
REMARK 500 2 THR C 122 -54.09 -167.61
REMARK 500 2 MET C 157 178.14 -57.98
REMARK 500 2 ALA C 189 69.26 -159.12
REMARK 500 3 ASN A 120 -163.34 -171.46
REMARK 500 3 PRO A 141 98.80 -67.04
REMARK 500 3 MET A 157 177.69 -57.50
REMARK 500 3 THR A 187 46.94 -159.16
REMARK 500 3 ASN B 120 -163.34 -171.82
REMARK 500 3 PRO B 141 98.75 -66.97
REMARK 500 3 MET B 157 177.80 -57.18
REMARK 500 3 THR B 187 46.83 -159.20
REMARK 500 3 ASN C 120 -163.23 -171.49
REMARK 500 3 PRO C 141 98.94 -66.95
REMARK 500 3 MET C 157 177.46 -57.24
REMARK 500 3 THR C 187 46.36 -159.09
REMARK 500 4 PRO A 141 94.33 -68.13
REMARK 500 4 THR A 156 -60.32 -121.97
REMARK 500 4 MET A 157 -172.94 -60.00
REMARK 500 4 HIS A 180 47.49 -84.87
REMARK 500 4 PRO B 141 92.84 -68.18
REMARK 500 4 THR B 156 -60.37 -121.73
REMARK 500 4 MET B 157 -173.00 -59.94
REMARK 500 4 HIS B 180 48.57 -85.96
REMARK 500 4 PRO C 141 94.27 -68.05
REMARK 500 4 THR C 156 -60.31 -121.76
REMARK 500 4 MET C 157 -172.86 -59.93
REMARK 500 4 HIS C 180 47.67 -85.02
REMARK 500 5 ASN A 120 8.34 -151.15
REMARK 500 5 PRO A 141 98.09 -67.46
REMARK 500 5 MET A 157 177.25 -58.84
REMARK 500 5 LEU A 182 -58.24 -171.64
REMARK 500 5 ALA A 189 52.94 -154.84
REMARK 500 5 ASN B 120 8.29 -151.04
REMARK 500 5 PRO B 141 98.05 -67.35
REMARK 500 5 MET B 157 177.28 -58.85
REMARK 500
REMARK 500 THIS ENTRY HAS 248 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 151 0.20 SIDE CHAIN
REMARK 500 1 ARG A 179 0.16 SIDE CHAIN
REMARK 500 1 ARG B 151 0.20 SIDE CHAIN
REMARK 500 1 ARG B 179 0.16 SIDE CHAIN
REMARK 500 1 ARG C 151 0.20 SIDE CHAIN
REMARK 500 1 ARG C 179 0.16 SIDE CHAIN
REMARK 500 2 ARG A 151 0.30 SIDE CHAIN
REMARK 500 2 ARG A 179 0.25 SIDE CHAIN
REMARK 500 2 ARG B 151 0.29 SIDE CHAIN
REMARK 500 2 ARG B 179 0.25 SIDE CHAIN
REMARK 500 2 ARG C 151 0.30 SIDE CHAIN
REMARK 500 2 ARG C 179 0.25 SIDE CHAIN
REMARK 500 3 ARG A 151 0.30 SIDE CHAIN
REMARK 500 3 ARG A 179 0.26 SIDE CHAIN
REMARK 500 3 ARG B 151 0.30 SIDE CHAIN
REMARK 500 3 ARG B 179 0.26 SIDE CHAIN
REMARK 500 3 ARG C 151 0.30 SIDE CHAIN
REMARK 500 3 ARG C 179 0.26 SIDE CHAIN
REMARK 500 4 ARG A 151 0.26 SIDE CHAIN
REMARK 500 4 ARG A 179 0.23 SIDE CHAIN
REMARK 500 4 ARG B 151 0.25 SIDE CHAIN
REMARK 500 4 ARG B 179 0.23 SIDE CHAIN
REMARK 500 4 ARG C 151 0.26 SIDE CHAIN
REMARK 500 4 ARG C 179 0.23 SIDE CHAIN
REMARK 500 5 ARG A 151 0.28 SIDE CHAIN
REMARK 500 5 ARG A 179 0.32 SIDE CHAIN
REMARK 500 5 ARG B 151 0.28 SIDE CHAIN
REMARK 500 5 ARG B 179 0.32 SIDE CHAIN
REMARK 500 5 ARG C 151 0.28 SIDE CHAIN
REMARK 500 5 ARG C 179 0.32 SIDE CHAIN
REMARK 500 6 ARG A 151 0.28 SIDE CHAIN
REMARK 500 6 ARG A 179 0.19 SIDE CHAIN
REMARK 500 6 ARG B 151 0.28 SIDE CHAIN
REMARK 500 6 ARG B 179 0.19 SIDE CHAIN
REMARK 500 6 ARG C 151 0.28 SIDE CHAIN
REMARK 500 6 ARG C 179 0.19 SIDE CHAIN
REMARK 500 7 ARG A 151 0.20 SIDE CHAIN
REMARK 500 7 ARG A 179 0.25 SIDE CHAIN
REMARK 500 7 ARG B 151 0.20 SIDE CHAIN
REMARK 500 7 ARG B 179 0.26 SIDE CHAIN
REMARK 500 7 ARG C 151 0.20 SIDE CHAIN
REMARK 500 7 ARG C 179 0.26 SIDE CHAIN
REMARK 500 8 ARG A 151 0.18 SIDE CHAIN
REMARK 500 8 ARG A 179 0.20 SIDE CHAIN
REMARK 500 8 ARG B 151 0.18 SIDE CHAIN
REMARK 500 8 ARG B 179 0.20 SIDE CHAIN
REMARK 500 8 ARG C 151 0.18 SIDE CHAIN
REMARK 500 8 ARG C 179 0.20 SIDE CHAIN
REMARK 500 9 ARG A 151 0.28 SIDE CHAIN
REMARK 500 9 ARG A 179 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 120 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IIE A 118 192 UNP P04233 HG2A_HUMAN 118 192
DBREF 1IIE B 118 192 UNP P04233 HG2A_HUMAN 118 192
DBREF 1IIE C 118 192 UNP P04233 HG2A_HUMAN 118 192
SEQRES 1 A 75 TYR GLY ASN MET THR GLU ASP HIS VAL MET HIS LEU LEU
SEQRES 2 A 75 GLN ASN ALA ASP PRO LEU LYS VAL TYR PRO PRO LEU LYS
SEQRES 3 A 75 GLY SER PHE PRO GLU ASN LEU ARG HIS LEU LYS ASN THR
SEQRES 4 A 75 MET GLU THR ILE ASP TRP LYS VAL PHE GLU SER TRP MET
SEQRES 5 A 75 HIS HIS TRP LEU LEU PHE GLU MET SER ARG HIS SER LEU
SEQRES 6 A 75 GLU GLN LYS PRO THR ASP ALA PRO PRO LYS
SEQRES 1 B 75 TYR GLY ASN MET THR GLU ASP HIS VAL MET HIS LEU LEU
SEQRES 2 B 75 GLN ASN ALA ASP PRO LEU LYS VAL TYR PRO PRO LEU LYS
SEQRES 3 B 75 GLY SER PHE PRO GLU ASN LEU ARG HIS LEU LYS ASN THR
SEQRES 4 B 75 MET GLU THR ILE ASP TRP LYS VAL PHE GLU SER TRP MET
SEQRES 5 B 75 HIS HIS TRP LEU LEU PHE GLU MET SER ARG HIS SER LEU
SEQRES 6 B 75 GLU GLN LYS PRO THR ASP ALA PRO PRO LYS
SEQRES 1 C 75 TYR GLY ASN MET THR GLU ASP HIS VAL MET HIS LEU LEU
SEQRES 2 C 75 GLN ASN ALA ASP PRO LEU LYS VAL TYR PRO PRO LEU LYS
SEQRES 3 C 75 GLY SER PHE PRO GLU ASN LEU ARG HIS LEU LYS ASN THR
SEQRES 4 C 75 MET GLU THR ILE ASP TRP LYS VAL PHE GLU SER TRP MET
SEQRES 5 C 75 HIS HIS TRP LEU LEU PHE GLU MET SER ARG HIS SER LEU
SEQRES 6 C 75 GLU GLN LYS PRO THR ASP ALA PRO PRO LYS
HELIX 1 1 GLU A 123 ALA A 133 1 11
HELIX 2 2 PHE A 146 THR A 156 1 11
HELIX 3 3 THR A 159 SER A 178 1 20
HELIX 4 4 GLU B 123 ALA B 133 1 11
HELIX 5 5 PHE B 146 THR B 156 1 11
HELIX 6 6 THR B 159 SER B 178 1 20
HELIX 7 7 GLU C 123 ALA C 133 1 11
HELIX 8 8 PHE C 146 THR C 156 1 11
HELIX 9 9 THR C 159 SER C 178 1 20
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - t 27 2 Bytes