HEADER IMMUNE SYSTEM/PEPTIDE 28-NOV-13 4NSK
TITLE CRYSTAL STRUCTURE OF THE MURINE CLASS I MAJOR HISTOCOMPATIBILITY
TITLE 2 COMPLEX H-2DB IN COMPLEX WITH LCMV-DERIVED GP33 ALTERED PEPTIDE
TITLE 3 LIGAND V3P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-B ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: H-2D(B);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PRE-GLYCOPROTEIN POLYPROTEIN GP;
COMPND 12 CHAIN: C;
COMPND 13 ENGINEERED: YES;
COMPND 14 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-D1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: B2M;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 OTHER_DETAILS: PEPTIDE GP33 FROM GLYCOPROTEIN OF LYMPHOCYTIC
SOURCE 24 CHORIOMENINGITIS VIRUS
KEYWDS MURINE MHC, LCMV, RECEPTOR BINDING, BETA2-MICROGLOBULIN, IMMUNE
KEYWDS 2 SYSTEM, T CELL RECOGNITION, ANTIGEN PRESENTATION, ALTERED PEPTIDE
KEYWDS 3 LIGAND, AGONISM, ANTAGONISM, T CELL RECEPTOR, CD8, CELL SURFACE,
KEYWDS 4 IMMUNE SYSTEM-PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.B.ALLERBRING,A.D.DURU,H.UCHTENHAGEN,P.A.MAZUMDAR,D.BADIA-MARTINEZ,
AUTHOR 2 C.MADHURANTAKAM,T.SANDALOVA,P.NYGREN,A.ACHOUR
REVDAT 2 20-SEP-23 4NSK 1 SEQADV
REVDAT 1 01-JAN-14 4NSK 0
SPRSDE 01-JAN-14 4NSK 3TBX
JRNL AUTH E.B.ALLERBRING,A.D.DURU,H.UCHTENHAGEN,P.A.MAZUMDAR,
JRNL AUTH 2 D.BADIA-MARTINEZ,C.MADHURANTAKAM,T.SANDALOVA,P.NYGREN,
JRNL AUTH 3 A.ACHOUR
JRNL TITL CRYSTAL STRUCTURE OF THE MURINE CLASS I MAJOR
JRNL TITL 2 HISTOCOMPATIBILITY COMPLEX H-2DB IN COMPLEX WITH
JRNL TITL 3 LCMV-DERIVED GP33 ALTERED PEPTIDE LIGAND V3P
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 13636
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) : 0.216
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 721
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 984
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3142
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 45
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.086
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.362
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.302
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.495
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3239 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2244 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4397 ; 1.319 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5418 ; 0.839 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 378 ; 7.198 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 169 ;36.330 ;23.609
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 533 ;19.642 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;20.013 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 440 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3603 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 688 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1908 ; 0.603 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 760 ; 0.070 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3078 ; 1.134 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1331 ; 1.227 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1319 ; 2.130 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 4NSK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083602.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.826
REMARK 200 MONOCHROMATOR : MONOCHROMATOR SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14534
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.570
REMARK 200 RESOLUTION RANGE LOW (A) : 54.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.55200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1S7U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6-1.8 M AMMONIUM SULFATE, 0.1 M TRIS
REMARK 280 HCL PH 7.0-9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -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 45.23000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.27000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.23000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 54.27000
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
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 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 A 224
REMARK 465 THR A 225
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 O HOH A 301 O HOH A 301 2555 1.75
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 ASP A 39 CB - CA - C ANGL. DEV. = -29.4 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 ASP A 29 43.41 36.88
REMARK 500 ASN A 30 -13.70 72.55
REMARK 500 TRP A 51 9.70 -69.52
REMARK 500 LEU A 110 -60.56 -101.87
REMARK 500 LEU A 114 97.88 -160.08
REMARK 500 TYR A 123 -60.45 -123.98
REMARK 500 ARG A 194 -57.87 -138.70
REMARK 500 SER A 195 -164.36 -124.60
REMARK 500 PRO A 210 -178.66 -66.94
REMARK 500 LEU A 219 62.60 -101.20
REMARK 500 ASN A 220 -54.66 70.18
REMARK 500 GLU A 222 117.55 -162.39
REMARK 500 LYS A 253 45.95 -80.38
REMARK 500 HIS B 31 132.39 -170.56
REMARK 500 LYS B 48 40.62 -103.67
REMARK 500 TRP B 60 -6.10 81.16
REMARK 500 PHE C 6 -113.43 -111.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 39 ALA A 40 148.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S7U RELATED DB: PDB
REMARK 900 H-2DB/GP33_WT (KAVYNFATM)
REMARK 900 RELATED ID: 1S7V RELATED DB: PDB
REMARK 900 H-2DB/GP33_F6L (KAVYNLATM)
REMARK 900 RELATED ID: 1S7W RELATED DB: PDB
REMARK 900 H-2DB/GP33_V3L (KALYNFATM)
REMARK 900 RELATED ID: 1S7X RELATED DB: PDB
REMARK 900 H-2DB/GP33_Y4F (KAVFNFATM)
REMARK 900 RELATED ID: 3QUK RELATED DB: PDB
REMARK 900 H-2DB/GP33_Y4A (KAVANFATM)
REMARK 900 RELATED ID: 3QUL RELATED DB: PDB
REMARK 900 H-2DB/GP33_Y4S (KAVSNFATM)
REMARK 900 RELATED ID: 3TBS RELATED DB: PDB
REMARK 900 H-2DB/GP33_V3P,Y4A (KAVANFATM)
REMARK 900 RELATED ID: 3TBT RELATED DB: PDB
REMARK 900 H-2DB/GP33_V3P,Y4S (KAPSNFATM)
REMARK 900 RELATED ID: 3TBW RELATED DB: PDB
REMARK 900 H-2DB/GP33_A2G,V3P,Y4S(KGPSNFATM)
REMARK 900 RELATED ID: 3TBV RELATED DB: PDB
REMARK 900 H-2DB/GP33_A2G,V3P,Y4A(KGPANFATM)
REMARK 900 RELATED ID: 3TBY RELATED DB: PDB
REMARK 900 H-2DB/GP33_V3P,Y4F(KAPFNFATM)
DBREF 4NSK A 1 276 UNP P01899 HA11_MOUSE 25 300
DBREF 4NSK B 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 4NSK C 1 9 PDB 4NSK 4NSK 1 9
SEQADV 4NSK ASP B 85 UNP P01887 ALA 105 CONFLICT
SEQRES 1 A 276 GLY PRO HIS SER MET ARG TYR PHE GLU THR ALA VAL SER
SEQRES 2 A 276 ARG PRO GLY LEU GLU GLU PRO ARG TYR ILE SER VAL GLY
SEQRES 3 A 276 TYR VAL ASP ASN LYS GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 276 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA PRO TRP MET
SEQRES 5 A 276 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 A 276 LYS ALA LYS GLY GLN GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 A 276 ARG ASN LEU LEU GLY TYR TYR ASN GLN SER ALA GLY GLY
SEQRES 8 A 276 SER HIS THR LEU GLN GLN MET SER GLY CYS ASP LEU GLY
SEQRES 9 A 276 SER ASP TRP ARG LEU LEU ARG GLY TYR LEU GLN PHE ALA
SEQRES 10 A 276 TYR GLU GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 A 276 LYS THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR
SEQRES 12 A 276 ARG ARG LYS TRP GLU GLN SER GLY ALA ALA GLU HIS TYR
SEQRES 13 A 276 LYS ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU HIS
SEQRES 14 A 276 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 A 276 ASP SER PRO LYS ALA HIS VAL THR HIS HIS PRO ARG SER
SEQRES 16 A 276 LYS GLY GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 276 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 A 276 GLU GLU LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 A 276 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 A 276 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG
SEQRES 21 A 276 VAL TYR HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 A 276 TRP GLU PRO
SEQRES 1 B 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 B 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 B 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 B 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 B 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 B 99 ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO LYS
SEQRES 8 B 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 C 9 LYS ALA PRO TYR ASN PHE ALA THR MET
FORMUL 4 HOH *45(H2 O)
HELIX 1 1 ALA A 49 GLU A 53 5 5
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 ASP A 137 SER A 150 1 14
HELIX 4 4 GLY A 151 GLY A 162 1 12
HELIX 5 5 GLY A 162 GLY A 175 1 14
HELIX 6 6 GLY A 175 ARG A 181 1 7
SHEET 1 A 8 TYR A 45 PRO A 47 0
SHEET 2 A 8 LYS A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 A 8 ARG A 21 VAL A 28 -1 N SER A 24 O PHE A 36
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 A 8 THR A 94 LEU A 103 -1 O LEU A 103 N HIS A 3
SHEET 6 A 8 LEU A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 A 8 ARG A 121 LEU A 126 -1 O LEU A 126 N LEU A 114
SHEET 8 A 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 B 4 LYS A 186 PRO A 193 0
SHEET 2 B 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 B 4 PHE A 241 PRO A 250 -1 O VAL A 249 N VAL A 199
SHEET 4 B 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 C 3 THR A 214 LEU A 219 0
SHEET 2 C 3 TYR A 257 TYR A 262 -1 O THR A 258 N GLN A 218
SHEET 3 C 3 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 D 4 GLN B 6 SER B 11 0
SHEET 2 D 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 D 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25
SHEET 4 D 4 GLU B 50 MET B 51 -1 N GLU B 50 O HIS B 67
SHEET 1 E 4 GLN B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25
SHEET 4 E 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 F 4 LYS B 44 LYS B 45 0
SHEET 2 F 4 GLU B 36 LYS B 41 -1 N LYS B 41 O LYS B 44
SHEET 3 F 4 TYR B 78 LYS B 83 -1 O ARG B 81 N GLN B 38
SHEET 4 F 4 LYS B 91 TYR B 94 -1 O LYS B 91 N VAL B 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.04
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.02
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
CISPEP 1 GLY A 1 PRO A 2 0 13.43
CISPEP 2 LYS A 196 GLY A 197 0 -1.20
CISPEP 3 TYR A 209 PRO A 210 0 -1.25
CISPEP 4 HIS B 31 PRO B 32 0 5.57
CRYST1 90.460 108.540 57.390 90.00 122.43 90.00 C 1 2 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 0.011055 0.000000 0.007023 0.00000
SCALE2 0.000000 0.009213 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020644 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
