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HEADER IMMUNE SYSTEM 07-AUG-08 3E3Q TITLE STRUCTURE OF THE 3ALPHAM13 HIGH-AFFINITY MUTANT OF THE 2C TCR IN TITLE 2 COMPLEX WITH LD/QL9 COMPND MOL_ID: 1; COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, L-D ALPHA CHAIN; COMPND 3 CHAIN: A, B, c, H, L, P, U, Y; COMPND 4 FRAGMENT: UNP RESIDUES 25-199; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: QL9 PEPTIDE; COMPND 9 CHAIN: Q, G, f, K, O, T, X, b; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: T-CELL RECEPTOR ALPHA CHAIN V REGION PHDS58; COMPND 13 CHAIN: D, C, d, I, M, R, V, Z; COMPND 14 ENGINEERED: YES; COMPND 15 MUTATION: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: TCR BETA CHAIN; COMPND 18 CHAIN: E, F, e, J, N, S, W, a; COMPND 19 ENGINEERED: YES; COMPND 20 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: H2-L; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28A; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN MOUSE; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_COMMON: MOUSE; SOURCE 16 ORGANISM_TAXID: 10090; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PET22B; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 23 ORGANISM_TAXID: 10090; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 26 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PET22B KEYWDS TCR, MHC, HIGH AFFINITY, CROSS REACTIVITY, GLYCOPROTEIN, IMMUNE KEYWDS 2 RESPONSE, MEMBRANE, MHC I, PHOSPHOPROTEIN, TRANSMEMBRANE, KEYWDS 3 IMMUNOGLOBULIN DOMAIN, RECEPTOR, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR L.A.COLF,K.C.GARCIA REVDAT 5 30-AUG-23 3E3Q 1 REMARK REVDAT 4 20-OCT-21 3E3Q 1 SEQADV REVDAT 3 25-OCT-17 3E3Q 1 REMARK REVDAT 2 24-FEB-09 3E3Q 1 VERSN REVDAT 1 04-NOV-08 3E3Q 0 JRNL AUTH L.L.JONES,L.A.COLF,J.D.STONE,K.C.GARCIA,D.M.KRANZ JRNL TITL DISTINCT CDR3 CONFORMATIONS IN TCRS DETERMINE THE LEVEL OF JRNL TITL 2 CROSS-REACTIVITY FOR DIVERSE ANTIGENS, BUT NOT THE DOCKING JRNL TITL 3 ORIENTATION. JRNL REF J.IMMUNOL. V. 181 6255 2008 JRNL REFN ISSN 0022-1767 JRNL PMID 18941216 REMARK 2 REMARK 2 RESOLUTION. 2.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.52 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 93313 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : 5% REMARK 3 R VALUE (WORKING SET) : 0.250 REMARK 3 FREE R VALUE : 0.275 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 4687 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 : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL 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 : 25808 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.95 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 5.95900 REMARK 3 B22 (A**2) : 1.01700 REMARK 3 B33 (A**2) : -6.97600 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) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.465 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.248 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.203 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.747 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.804 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 23.07 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : CNS_TOPPAR:DNA-RNA.TOP REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3E3Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-08. REMARK 100 THE DEPOSITION ID IS D_1000048836. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JAN-07 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 : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93313 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 4.100 REMARK 200 R MERGE (I) : 0.13000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3 REMARK 200 DATA REDUNDANCY IN SHELL : 4.10 REMARK 200 R MERGE FOR SHELL (I) : 0.65600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000 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 2OI9 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.37 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM CITRATE, 20% PEG 3350, REMARK 280 3% TRIMETHYL AMINE N-OXIDE DIHYDRATE, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z 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 REMARK 290 7555 -X+1/2,Y+1/2,-Z 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 0.00000 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 0.00000 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 79.23600 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 80.22900 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 79.23600 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 80.22900 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 79.23600 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 80.22900 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 79.23600 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 80.22900 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Q, D, 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, C, 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: c, f, d, 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, K, I, J 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, O, M, N 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, T, R, S 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: 7 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, X, V, W 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: 8 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, b, Z, a 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 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 OG SER A 88 OE2 GLU E 73 6545 1.93 REMARK 500 OG SER A 88 OE1 GLU E 73 6545 2.12 REMARK 500 O ASN A 86 OD1 ASN E 28 6545 2.14 REMARK 500 REMARK 500 REMARK: NULL 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 CYS A 164 CA - CB - SG ANGL. DEV. = -10.9 DEGREES REMARK 500 PRO D 100 C - N - CA ANGL. DEV. = -12.7 DEGREES REMARK 500 CYS B 164 CA - CB - SG ANGL. DEV. = -11.8 DEGREES REMARK 500 PRO C 100 C - N - CA ANGL. DEV. = -12.9 DEGREES REMARK 500 CYS c 164 CA - CB - SG ANGL. DEV. = -11.9 DEGREES REMARK 500 PRO d 100 C - N - CA ANGL. DEV. = -12.2 DEGREES REMARK 500 CYS H 164 CA - CB - SG ANGL. DEV. = -11.9 DEGREES REMARK 500 PRO I 100 C - N - CA ANGL. DEV. = -13.3 DEGREES REMARK 500 CYS L 164 CA - CB - SG ANGL. DEV. = -12.5 DEGREES REMARK 500 PRO M 100 C - N - CA ANGL. DEV. = -13.2 DEGREES REMARK 500 CYS P 164 CA - CB - SG ANGL. DEV. = -13.0 DEGREES REMARK 500 PRO R 100 C - N - CA ANGL. DEV. = -11.8 DEGREES REMARK 500 CYS U 164 CA - CB - SG ANGL. DEV. = -12.6 DEGREES REMARK 500 PRO V 100 C - N - CA ANGL. DEV. = -12.6 DEGREES REMARK 500 CYS Y 164 CA - CB - SG ANGL. DEV. = -12.8 DEGREES REMARK 500 PRO Z 100 C - N - CA ANGL. DEV. = -11.8 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 ARG A 15 106.12 -29.28 REMARK 500 LEU A 17 42.58 -93.05 REMARK 500 ASP A 29 -125.97 56.64 REMARK 500 SER A 88 -164.13 -66.90 REMARK 500 GLU A 114 112.48 -169.51 REMARK 500 ARG A 131 -32.60 -136.10 REMARK 500 ALA A 136 -82.23 -41.48 REMARK 500 ASP A 137 -159.42 -106.77 REMARK 500 ALA D 28 -176.73 -61.88 REMARK 500 PRO D 39 132.17 -34.41 REMARK 500 TYR D 50 -61.74 -109.11 REMARK 500 PHE D 73 63.30 -153.84 REMARK 500 ALA D 86 -175.17 177.56 REMARK 500 ASP D 99 -135.26 -73.67 REMARK 500 THR E 39 12.61 -165.55 REMARK 500 HIS E 41 -147.88 -99.59 REMARK 500 ARG E 69 72.94 -117.97 REMARK 500 ARG B 15 105.75 -30.33 REMARK 500 LEU B 17 41.61 -93.23 REMARK 500 ASP B 29 -122.59 57.03 REMARK 500 SER B 88 -161.70 -62.90 REMARK 500 GLU B 114 112.10 -166.93 REMARK 500 TYR B 123 -63.68 -121.97 REMARK 500 ARG B 131 -32.81 -136.75 REMARK 500 ALA B 136 -82.35 -43.46 REMARK 500 ASP B 137 -160.55 -105.51 REMARK 500 ALA C 28 -172.15 -66.60 REMARK 500 PRO C 39 133.00 -32.84 REMARK 500 PHE C 73 62.49 -155.39 REMARK 500 ALA C 86 -171.24 -178.36 REMARK 500 ASP C 99 -134.05 -75.58 REMARK 500 THR F 39 10.23 -166.97 REMARK 500 HIS F 41 -145.92 -97.61 REMARK 500 ARG F 69 71.13 -115.22 REMARK 500 ARG c 15 106.38 -21.29 REMARK 500 LEU c 17 39.97 -95.01 REMARK 500 ASP c 29 -121.27 60.53 REMARK 500 SER c 88 -163.20 -62.19 REMARK 500 ARG c 111 136.12 -170.60 REMARK 500 GLU c 114 114.86 -171.28 REMARK 500 TYR c 123 -64.33 -122.84 REMARK 500 ARG c 131 -33.65 -134.34 REMARK 500 ALA c 136 -81.24 -46.52 REMARK 500 ASP c 137 -161.70 -107.61 REMARK 500 ALA d 28 -174.23 -64.69 REMARK 500 PRO d 39 135.26 -30.95 REMARK 500 TYR d 50 -66.96 -107.75 REMARK 500 PHE d 73 62.09 -154.27 REMARK 500 ALA d 86 -170.49 -177.97 REMARK 500 ASP d 99 -136.01 -74.96 REMARK 500 REMARK 500 THIS ENTRY HAS 148 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 TYR D 49 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2OI9 RELATED DB: PDB REMARK 900 WILD-TYPE COMPLEX REMARK 900 RELATED ID: 2E7L RELATED DB: PDB REMARK 900 HIGH AFFINITY COMPLEX REMARK 900 RELATED ID: 3E2H RELATED DB: PDB REMARK 900 HIGH AFFINITY COMPLEX DBREF 3E3Q A 1 175 UNP P01897 HA1L_MOUSE 25 199 DBREF 3E3Q D 2 115 UNP P01738 TVA1_MOUSE 22 130 DBREF 3E3Q B 1 175 UNP P01897 HA1L_MOUSE 25 199 DBREF 3E3Q C 2 115 UNP P01738 TVA1_MOUSE 22 130 DBREF 3E3Q c 1 175 UNP P01897 HA1L_MOUSE 25 199 DBREF 3E3Q d 2 115 UNP P01738 TVA1_MOUSE 22 130 DBREF 3E3Q H 1 175 UNP P01897 HA1L_MOUSE 25 199 DBREF 3E3Q I 2 115 UNP P01738 TVA1_MOUSE 22 130 DBREF 3E3Q L 1 175 UNP P01897 HA1L_MOUSE 25 199 DBREF 3E3Q M 2 115 UNP P01738 TVA1_MOUSE 22 130 DBREF 3E3Q P 1 175 UNP P01897 HA1L_MOUSE 25 199 DBREF 3E3Q R 2 115 UNP P01738 TVA1_MOUSE 22 130 DBREF 3E3Q U 1 175 UNP P01897 HA1L_MOUSE 25 199 DBREF 3E3Q V 2 115 UNP P01738 TVA1_MOUSE 22 130 DBREF 3E3Q Y 1 175 UNP P01897 HA1L_MOUSE 25 199 DBREF 3E3Q Z 2 115 UNP P01738 TVA1_MOUSE 22 130 DBREF 3E3Q Q 1 9 PDB 3E3Q 3E3Q 1 9 DBREF 3E3Q G 1 9 PDB 3E3Q 3E3Q 1 9 DBREF 3E3Q f 1 9 PDB 3E3Q 3E3Q 1 9 DBREF 3E3Q K 1 9 PDB 3E3Q 3E3Q 1 9 DBREF 3E3Q O 1 9 PDB 3E3Q 3E3Q 1 9 DBREF 3E3Q T 1 9 PDB 3E3Q 3E3Q 1 9 DBREF 3E3Q X 1 9 PDB 3E3Q 3E3Q 1 9 DBREF 3E3Q b 1 9 PDB 3E3Q 3E3Q 1 9 DBREF 3E3Q E 1 118 PDB 3E3Q 3E3Q 1 118 DBREF 3E3Q F 1 118 PDB 3E3Q 3E3Q 1 118 DBREF 3E3Q e 1 118 PDB 3E3Q 3E3Q 1 118 DBREF 3E3Q J 1 118 PDB 3E3Q 3E3Q 1 118 DBREF 3E3Q N 1 118 PDB 3E3Q 3E3Q 1 118 DBREF 3E3Q S 1 118 PDB 3E3Q 3E3Q 1 118 DBREF 3E3Q W 1 118 PDB 3E3Q 3E3Q 1 118 DBREF 3E3Q a 1 118 PDB 3E3Q 3E3Q 1 118