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1S7R.pdb
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HEADER IMMUNE SYSTEM 30-JAN-04 1S7R
TITLE CRYSTAL STRUCTURES OF THE MURINE CLASS I MAJOR HISTOCOMPATIBILITY
TITLE 2 COMPLEX H-2KB IN COMPLEX WITH LCMV-DERIVED GP33 INDEX PEPTIDE AND
TITLE 3 THREE OF ITS ESCAPE VARIANTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: H-2KB;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 8 CHAIN: B, E;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: GLYCOPROTEIN 9-RESIDUE PEPTIDE;
COMPND 12 CHAIN: C, F;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: H2-K;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-3A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: B2M;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-3A;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED, THE SEQUENCE
SOURCE 24 OF THE PEPTIDE IS NATURALLY FOUND IN LYMPHOCYTIC CHORIOMENINGITIS
SOURCE 25 VIRUS
KEYWDS LCMV, MHC CLASS I, IMMUNE ESCAPE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.VELLOSO,J.MICHAELSSON,H.G.LJUNGGREN,G.SCHNEIDER,A.ACHOUR
REVDAT 3 13-JUL-11 1S7R 1 VERSN
REVDAT 2 24-FEB-09 1S7R 1 VERSN
REVDAT 1 04-MAY-04 1S7R 0
JRNL AUTH L.M.VELLOSO,J.MICHAELSSON,H.G.LJUNGGREN,G.SCHNEIDER,A.ACHOUR
JRNL TITL DETERMINATION OF STRUCTURAL PRINCIPLES UNDERLYING THREE
JRNL TITL 2 DIFFERENT MODES OF LYMPHOCYTIC CHORIOMENINGITIS VIRUS ESCAPE
JRNL TITL 3 FROM CTL RECOGNITION.
JRNL REF J.IMMUNOL. V. 172 5504 2004
JRNL REFN ISSN 0022-1767
JRNL PMID 15100292
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 19684
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) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1041
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) : 2.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1373
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6276
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.19000
REMARK 3 B22 (A**2) : -4.87000
REMARK 3 B33 (A**2) : 0.99000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.505
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.425
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.341
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.870
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.807
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6460 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5588 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8772 ; 1.493 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13038 ; 0.902 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 762 ; 5.788 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 904 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7192 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1354 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1482 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6981 ; 0.247 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3704 ; 0.091 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 170 ; 0.190 ; 0.200
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): 12 ; 0.255 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 67 ; 0.278 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.037 ; 0.200
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): 3836 ; 0.702 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6198 ; 1.339 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2624 ; 1.549 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2574 ; 2.704 ; 4.500
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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 16
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 2 1
REMARK 3 1 D 1 D 2 1
REMARK 3 2 A 4 A 92 1
REMARK 3 2 D 4 D 92 1
REMARK 3 3 A 94 A 144 1
REMARK 3 3 D 94 D 144 1
REMARK 3 4 A 189 A 190 1
REMARK 3 4 D 189 D 190 1
REMARK 3 5 A 193 A 259 1
REMARK 3 5 D 193 D 259 1
REMARK 3 6 A 261 A 262 1
REMARK 3 6 D 261 D 262 1
REMARK 3 7 A 3 A 3 3
REMARK 3 7 D 3 D 3 3
REMARK 3 8 A 93 A 93 3
REMARK 3 8 D 93 D 93 3
REMARK 3 9 A 188 A 188 3
REMARK 3 9 D 188 D 188 3
REMARK 3 10 A 191 A 191 3
REMARK 3 10 D 191 D 191 3
REMARK 3 11 A 260 A 260 3
REMARK 3 11 D 260 D 260 3
REMARK 3 12 A 263 A 263 3
REMARK 3 12 D 263 D 263 3
REMARK 3 13 A 145 A 145 3
REMARK 3 13 D 145 D 145 3
REMARK 3 14 A 192 A 192 3
REMARK 3 14 D 192 D 192 3
REMARK 3 15 A 264 A 276 1
REMARK 3 15 D 264 D 276 1
REMARK 3 16 A 146 A 187 5
REMARK 3 16 D 146 D 187 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3507 ; 0.03 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 248 ; 0.13 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 497 ; 0.19 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 3507 ; 0.06 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 248 ; 0.51 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 497 ; 1.06 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 12 1
REMARK 3 1 E 1 E 12 1
REMARK 3 2 B 35 B 66 1
REMARK 3 2 E 35 E 66 1
REMARK 3 3 B 68 B 83 1
REMARK 3 3 E 68 E 83 1
REMARK 3 4 B 85 B 99 1
REMARK 3 4 E 85 E 99 1
REMARK 3 5 B 34 B 34 3
REMARK 3 5 E 34 E 34 3
REMARK 3 6 B 67 B 67 3
REMARK 3 6 E 67 E 67 3
REMARK 3 7 B 84 B 84 3
REMARK 3 7 E 84 E 84 3
REMARK 3 8 B 13 B 13 3
REMARK 3 8 E 13 E 13 3
REMARK 3 9 B 14 B 30 1
REMARK 3 9 E 14 E 30 1
REMARK 3 10 B 31 B 33 3
REMARK 3 10 E 31 E 33 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 1477 ; 0.03 ; 0.05
REMARK 3 LOOSE POSITIONAL 2 B (A): 68 ; 0.11 ; 5.00
REMARK 3 TIGHT THERMAL 2 B (A**2): 1477 ; 0.07 ; 0.50
REMARK 3 LOOSE THERMAL 2 B (A**2): 68 ; 0.55 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 2 C 9 1
REMARK 3 1 F 2 F 9 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 C (A): 118 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 3 C (A**2): 118 ; 0.06 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 182
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0105 13.9653 49.2604
REMARK 3 T TENSOR
REMARK 3 T11: 0.1152 T22: 0.2051
REMARK 3 T33: 0.2836 T12: 0.0040
REMARK 3 T13: -0.0380 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.5409 L22: 0.4412
REMARK 3 L33: 0.3055 L12: -0.2771
REMARK 3 L13: -0.3165 L23: -0.2004
REMARK 3 S TENSOR
REMARK 3 S11: 0.1452 S12: 0.0397 S13: -0.0077
REMARK 3 S21: -0.0281 S22: -0.1121 S23: 0.0094
REMARK 3 S31: 0.0366 S32: 0.0403 S33: -0.0331
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 183 A 276
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9001 -18.2374 40.4002
REMARK 3 T TENSOR
REMARK 3 T11: 0.2260 T22: 0.2581
REMARK 3 T33: 0.2393 T12: 0.0346
REMARK 3 T13: -0.0137 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.5285 L22: 5.1898
REMARK 3 L33: -0.3190 L12: 1.7757
REMARK 3 L13: 0.7287 L23: -0.1565
REMARK 3 S TENSOR
REMARK 3 S11: 0.0666 S12: 0.1689 S13: -0.1566
REMARK 3 S21: -0.6889 S22: 0.0536 S23: -0.0349
REMARK 3 S31: -0.2184 S32: 0.0027 S33: -0.1202
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 99
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1280 -9.6451 59.3717
REMARK 3 T TENSOR
REMARK 3 T11: 0.0129 T22: 0.1748
REMARK 3 T33: 0.2770 T12: -0.0161
REMARK 3 T13: -0.0553 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 2.9791 L22: 2.6013
REMARK 3 L33: 1.8111 L12: -1.9929
REMARK 3 L13: 0.7499 L23: -1.2791
REMARK 3 S TENSOR
REMARK 3 S11: 0.0829 S12: -0.1208 S13: -0.1201
REMARK 3 S21: -0.0640 S22: -0.0587 S23: 0.1331
REMARK 3 S31: -0.1245 S32: 0.1408 S33: -0.0241
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 9
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7762 20.1543 49.4433
REMARK 3 T TENSOR
REMARK 3 T11: 0.2591 T22: 0.2640
REMARK 3 T33: 0.2735 T12: -0.1111
REMARK 3 T13: 0.1559 T23: 0.0556
REMARK 3 L TENSOR
REMARK 3 L11: 15.5601 L22: 12.7209
REMARK 3 L33: -7.2390 L12: -5.4639
REMARK 3 L13: 23.4192 L23: 1.4726
REMARK 3 S TENSOR
REMARK 3 S11: 1.5630 S12: -0.6539 S13: 1.0553
REMARK 3 S21: 0.4494 S22: -0.9129 S23: -1.3938
REMARK 3 S31: -1.1435 S32: -0.6067 S33: -0.6501
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 182
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7414 -3.2156 9.0581
REMARK 3 T TENSOR
REMARK 3 T11: 0.4814 T22: 0.3501
REMARK 3 T33: 0.2746 T12: 0.0159
REMARK 3 T13: 0.0745 T23: -0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 0.3045 L22: 1.5736
REMARK 3 L33: 1.3801 L12: 0.4607
REMARK 3 L13: -0.3655 L23: 0.1139
REMARK 3 S TENSOR
REMARK 3 S11: -0.0216 S12: 0.0260 S13: -0.0357
REMARK 3 S21: -0.0233 S22: -0.0907 S23: 0.0246
REMARK 3 S31: 0.1494 S32: 0.0278 S33: 0.1123
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 183 D 276
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6062 28.9945 24.6769
REMARK 3 T TENSOR
REMARK 3 T11: 0.2622 T22: 0.3583
REMARK 3 T33: 0.2579 T12: -0.0585
REMARK 3 T13: 0.0232 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 1.1737 L22: 4.3551
REMARK 3 L33: 1.2821 L12: -0.4741
REMARK 3 L13: -0.3484 L23: -0.7891
REMARK 3 S TENSOR
REMARK 3 S11: 0.2276 S12: 0.0106 S13: 0.1823
REMARK 3 S21: 0.0722 S22: -0.1154 S23: 0.3064
REMARK 3 S31: -0.1574 S32: -0.0059 S33: -0.1123
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 99
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8210 20.4153 6.8940
REMARK 3 T TENSOR
REMARK 3 T11: 0.4902 T22: 0.3134
REMARK 3 T33: 0.2719 T12: 0.0747
REMARK 3 T13: 0.0459 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 1.4645 L22: 2.2353
REMARK 3 L33: 2.1925 L12: 1.2913
REMARK 3 L13: -1.0323 L23: 0.0210
REMARK 3 S TENSOR
REMARK 3 S11: -0.0711 S12: 0.0107 S13: 0.0208
REMARK 3 S21: -0.3143 S22: -0.0832 S23: -0.1691
REMARK 3 S31: -0.0252 S32: 0.1327 S33: 0.1543
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 9
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8129 -9.4101 7.5380
REMARK 3 T TENSOR
REMARK 3 T11: 0.3062 T22: 0.3651
REMARK 3 T33: 0.4569 T12: 0.0617
REMARK 3 T13: -0.0078 T23: 0.0833
REMARK 3 L TENSOR
REMARK 3 L11: 11.9024 L22: 12.1528
REMARK 3 L33: 32.5609 L12: -8.0798
REMARK 3 L13: 23.7679 L23: -23.6927
REMARK 3 S TENSOR
REMARK 3 S11: 0.8676 S12: 1.0741 S13: -0.6944
REMARK 3 S21: -0.8491 S22: -0.7281 S23: -0.7899
REMARK 3 S31: 1.8674 S32: 0.9379 S33: -0.1395
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 : 1.40
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 1S7R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-04.
REMARK 100 THE RCSB ID CODE IS RCSB021473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JAN-03
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 : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.097
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20741
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1N59
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM/POTASSIUM PHOSPHATE, METHYL
REMARK 280 PENTANE DIOL, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 44.25950
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: 4560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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: 4550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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 410
REMARK 410 IMGT/3Dstructure-DB annotations
REMARK 410 (http://www.imgt.org)
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1-K1b (H2-K1b)
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Mus musculus (house mouse)
REMARK 410 Chain ID
REMARK 410 1s7r_D,1s7r_E
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1-K1b (H2-K1b)
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Mus musculus (house mouse)
REMARK 410 Chain ID
REMARK 410 1s7r_A,1s7r_B
REMARK 410
REMARK 410 ligand(s)
REMARK 410 Glycoprotein G1 peptide 33-41 (P07399), F6>L C9M
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Lymphocytic choriomeningitis mammarenavirus
REMARK 410 Chain ID
REMARK 410 1s7r_F
REMARK 410
REMARK 410 ligand(s)
REMARK 410 Glycoprotein G1 peptide 33-41 (P07399), F6>L C9>M
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Lymphocytic choriomeningitis mammarenavirus
REMARK 410 Chain ID
REMARK 410 1s7r_C
REMARK 410
REMARK 410
REMARK 410 Chain ID 1s7r_D (1S7RD)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQK
REMARK 410 ][ G-ALPHA
REMARK 410 AKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKT
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLRTDSPKAHVTHHSRPEDK
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQ
REMARK 410 ]
REMARK 410 GLPEPLTLRWEPPPSTVSNMATVAVLVVLGAAIVTGAVVAFVMKMRRRNTGGKGGDYALAPGSQTS
REMARK 410
REMARK 410 DLSLPDCKVMVHDPHSLA
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GPHSLRY.FVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAE
REMARK 410 G-DOMAIN NPRYEPRA.......RWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYN
REMARK 410 G-DOMAIN QSKG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNED..L
REMARK 410 G-DOMAIN KTWTAAD.......MAALITKHKWEQA.GEAERLRAYLEGTCVEWLRRYLKN
REMARK 410 G-DOMAIN GNATLLRT.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DSPKAHVTHHSRPE......DKVTLRCWALGFYP..ADITLTWQL
REMARK 410 C-LIKE-DOMAIN NGEELIQ..DMELVETRPAGD......GTFQKWASVVVPLG.....KEQYYT
REMARK 410 C-LIKE-DOMAIN CHVYHQG..LPEPLTLRW
REMARK 410
REMARK 410 Chain ID 1s7r_E (1S7RE)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (1-99) [D1]
REMARK 410 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILA
REMARK 410 ]
REMARK 410 HTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus B2M*01 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQKTPQIQVYSRHPPEN....GKPNILNCYVTQFHP..PHIEIQMLK
REMARK 410 C-LIKE-DOMAIN NGKKIP...KVEMSDMSFSKD......WSFYILAHTEFTPTE.....TDTYA
REMARK 410 C-LIKE-DOMAIN CRVKHDS..MAEPKTVYWDRDM
REMARK 410
REMARK 410 Chain ID 1s7r_A (1S7RA)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQK
REMARK 410 ][ G-ALPHA
REMARK 410 AKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKT
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLRTDSPKAHVTHHSRPEDK
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQ
REMARK 410 ]
REMARK 410 GLPEPLTLRWEPPPSTVSNMATVAVLVVLGAAIVTGAVVAFVMKMRRRNTGGKGGDYALAPGSQTS
REMARK 410
REMARK 410 DLSLPDCKVMVHDPHSLA
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GPHSLRY.FVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAE
REMARK 410 G-DOMAIN NPRYEPRA.......RWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYN
REMARK 410 G-DOMAIN QSKG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNED..L
REMARK 410 G-DOMAIN KTWTAAD.......MAALITKHKWEQA.GEAERLRAYLEGTCVEWLRRYLKN
REMARK 410 G-DOMAIN GNATLLRT.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DSPKAHVTHHSRPE......DKVTLRCWALGFYP..ADITLTWQL
REMARK 410 C-LIKE-DOMAIN NGEELIQ..DMELVETRPAGD......GTFQKWASVVVPLG.....KEQYYT
REMARK 410 C-LIKE-DOMAIN CHVYHQG..LPEPLTLRW
REMARK 410
REMARK 410 Chain ID 1s7r_B (1S7RB)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (1-99) [D1]
REMARK 410 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILA
REMARK 410 ]
REMARK 410 HTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus B2M*01 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQKTPQIQVYSRHPPEN....GKPNILNCYVTQFHP..PHIEIQMLK
REMARK 410 C-LIKE-DOMAIN NGKKIP...KVEMSDMSFSKD......WSFYILAHTEFTPTE.....TDTYA
REMARK 410 C-LIKE-DOMAIN CRVKHDS..MAEPKTVYWDRDM
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 PRO A 277
REMARK 465 PRO A 278
REMARK 465 SER A 279
REMARK 465 THR A 280
REMARK 465 VAL A 281
REMARK 465 SER A 282
REMARK 465 ASN A 283
REMARK 465 MET A 284
REMARK 465 ALA A 285
REMARK 465 THR A 286
REMARK 465 VAL A 287
REMARK 465 ALA A 288
REMARK 465 VAL A 289
REMARK 465 LEU A 290
REMARK 465 VAL A 291
REMARK 465 VAL A 292
REMARK 465 LEU A 293
REMARK 465 GLY A 294
REMARK 465 ALA A 295
REMARK 465 ALA A 296
REMARK 465 ILE A 297
REMARK 465 VAL A 298
REMARK 465 THR A 299
REMARK 465 GLY A 300
REMARK 465 ALA A 301
REMARK 465 VAL A 302
REMARK 465 VAL A 303
REMARK 465 ALA A 304
REMARK 465 PHE A 305
REMARK 465 VAL A 306
REMARK 465 MET A 307
REMARK 465 LYS A 308
REMARK 465 MET A 309
REMARK 465 ARG A 310
REMARK 465 ARG A 311
REMARK 465 ARG A 312
REMARK 465 ASN A 313
REMARK 465 THR A 314
REMARK 465 GLY A 315
REMARK 465 GLY A 316
REMARK 465 LYS A 317
REMARK 465 GLY A 318
REMARK 465 GLY A 319
REMARK 465 ASP A 320
REMARK 465 TYR A 321
REMARK 465 ALA A 322
REMARK 465 LEU A 323
REMARK 465 ALA A 324
REMARK 465 PRO A 325
REMARK 465 GLY A 326
REMARK 465 SER A 327
REMARK 465 GLN A 328
REMARK 465 THR A 329
REMARK 465 SER A 330
REMARK 465 ASP A 331
REMARK 465 LEU A 332
REMARK 465 SER A 333
REMARK 465 LEU A 334
REMARK 465 PRO A 335
REMARK 465 ASP A 336
REMARK 465 CYS A 337
REMARK 465 LYS A 338
REMARK 465 VAL A 339
REMARK 465 MET A 340
REMARK 465 VAL A 341
REMARK 465 HIS A 342
REMARK 465 ASP A 343
REMARK 465 PRO A 344
REMARK 465 HIS A 345
REMARK 465 SER A 346
REMARK 465 LEU A 347
REMARK 465 ALA A 348
REMARK 465 PRO D 277
REMARK 465 PRO D 278
REMARK 465 SER D 279
REMARK 465 THR D 280
REMARK 465 VAL D 281
REMARK 465 SER D 282
REMARK 465 ASN D 283
REMARK 465 MET D 284
REMARK 465 ALA D 285
REMARK 465 THR D 286
REMARK 465 VAL D 287
REMARK 465 ALA D 288
REMARK 465 VAL D 289
REMARK 465 LEU D 290
REMARK 465 VAL D 291
REMARK 465 VAL D 292
REMARK 465 LEU D 293
REMARK 465 GLY D 294
REMARK 465 ALA D 295
REMARK 465 ALA D 296
REMARK 465 ILE D 297
REMARK 465 VAL D 298
REMARK 465 THR D 299
REMARK 465 GLY D 300
REMARK 465 ALA D 301
REMARK 465 VAL D 302
REMARK 465 VAL D 303
REMARK 465 ALA D 304
REMARK 465 PHE D 305
REMARK 465 VAL D 306
REMARK 465 MET D 307
REMARK 465 LYS D 308
REMARK 465 MET D 309
REMARK 465 ARG D 310
REMARK 465 ARG D 311
REMARK 465 ARG D 312
REMARK 465 ASN D 313
REMARK 465 THR D 314
REMARK 465 GLY D 315
REMARK 465 GLY D 316
REMARK 465 LYS D 317
REMARK 465 GLY D 318
REMARK 465 GLY D 319
REMARK 465 ASP D 320
REMARK 465 TYR D 321
REMARK 465 ALA D 322
REMARK 465 LEU D 323
REMARK 465 ALA D 324
REMARK 465 PRO D 325
REMARK 465 GLY D 326
REMARK 465 SER D 327
REMARK 465 GLN D 328
REMARK 465 THR D 329
REMARK 465 SER D 330
REMARK 465 ASP D 331
REMARK 465 LEU D 332
REMARK 465 SER D 333
REMARK 465 LEU D 334
REMARK 465 PRO D 335
REMARK 465 ASP D 336
REMARK 465 CYS D 337
REMARK 465 LYS D 338
REMARK 465 VAL D 339
REMARK 465 MET D 340
REMARK 465 VAL D 341
REMARK 465 HIS D 342
REMARK 465 ASP D 343
REMARK 465 PRO D 344
REMARK 465 HIS D 345
REMARK 465 SER D 346
REMARK 465 LEU D 347
REMARK 465 ALA D 348
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 NE2 HIS A 191 OE2 GLU A 254 1.94
REMARK 500 NE2 HIS D 191 OE2 GLU D 254 2.03
REMARK 500 O ARG A 194 O HOH A 364 2.16
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 77 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 122 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 137 CB - CG - OD2 ANGL. DEV. = 5.6 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 VAL A 12 108.28 -164.89
REMARK 500 ASP A 29 74.53 51.20
REMARK 500 ALA A 49 131.49 -170.01
REMARK 500 ASN A 86 45.29 39.89
REMARK 500 ARG A 111 144.72 173.23
REMARK 500 LYS A 131 -56.40 -123.52
REMARK 500 GLU A 196 17.59 84.69
REMARK 500 LEU A 219 100.68 -161.21
REMARK 500 GLU A 229 108.55 -165.24
REMARK 500 ASP A 238 30.27 -141.61
REMARK 500 TRP B 60 0.02 96.47
REMARK 500 ALA B 88 -81.26 -38.15
REMARK 500 ALA C 2 -58.06 -162.19
REMARK 500 VAL D 12 107.97 -161.63
REMARK 500 ASP D 29 75.84 50.94
REMARK 500 ALA D 49 134.87 -171.45
REMARK 500 ARG D 111 140.42 171.16
REMARK 500 LYS D 131 -54.99 -123.17
REMARK 500 GLU D 196 14.89 86.21
REMARK 500 GLU D 229 108.19 -167.42
REMARK 500 ASP D 238 27.17 -140.83
REMARK 500 TRP E 60 -3.60 101.80
REMARK 500 ALA E 88 -77.28 -38.82
REMARK 500 ALA F 2 -58.00 -167.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1N59 RELATED DB: PDB
REMARK 900 RELATED ID: 1S7Q RELATED DB: PDB
REMARK 900 RELATED ID: 1S7S RELATED DB: PDB
REMARK 900 RELATED ID: 1S7T RELATED DB: PDB
REMARK 900 RELATED ID: 1S7U RELATED DB: PDB
REMARK 900 RELATED ID: 1S7V RELATED DB: PDB
REMARK 900 RELATED ID: 1S7W RELATED DB: PDB
REMARK 900 RELATED ID: 1S7X RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CYSTEINE IN THE ORIGINAL SEQUENCE IS REPLACED
REMARK 999 INTENTIONALLY BY A METHIONINE TO AVOID OXIDATION OF
REMARK 999 THE PEPTIDE.
DBREF 1S7R A 1 348 UNP P01901 HA1B_MOUSE 22 369
DBREF 1S7R B 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1S7R C 1 9 UNP P07399 VGLY_LYCVW 33 40
DBREF 1S7R D 1 348 UNP P01901 HA1B_MOUSE 22 369
DBREF 1S7R E 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1S7R F 1 9 UNP P07399 VGLY_LYCVW 33 40
SEQADV 1S7R LEU C 6 UNP P07399 PHE 38 ENGINEERED
SEQADV 1S7R MET C 9 UNP P07399 CYS 41 SEE REMARK 999
SEQADV 1S7R LEU F 6 UNP P07399 PHE 38 ENGINEERED
SEQADV 1S7R MET F 9 UNP P07399 CYS 41 SEE REMARK 999
SEQRES 1 A 348 GLY PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER
SEQRES 2 A 348 ARG PRO GLY LEU GLY GLU PRO ARG TYR MET GLU VAL GLY
SEQRES 3 A 348 TYR VAL ASP ASP THR GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 348 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP MET
SEQRES 5 A 348 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 A 348 LYS ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU
SEQRES 7 A 348 ARG THR LEU LEU GLY TYR TYR ASN GLN SER LYS GLY GLY
SEQRES 8 A 348 SER HIS THR ILE GLN VAL ILE SER GLY CYS GLU VAL GLY
SEQRES 9 A 348 SER ASP GLY ARG LEU LEU ARG GLY TYR GLN GLN TYR ALA
SEQRES 10 A 348 TYR ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 A 348 LYS THR TRP THR ALA ALA ASP MET ALA ALA LEU ILE THR
SEQRES 12 A 348 LYS HIS LYS TRP GLU GLN ALA GLY GLU ALA GLU ARG LEU
SEQRES 13 A 348 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 348 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 A 348 ASP SER PRO LYS ALA HIS VAL THR HIS HIS SER ARG PRO
SEQRES 16 A 348 GLU ASP LYS VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 348 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 A 348 GLU GLU LEU ILE GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 A 348 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 A 348 VAL VAL PRO LEU GLY LYS GLU GLN TYR TYR THR CYS HIS
SEQRES 21 A 348 VAL TYR HIS GLN GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 A 348 TRP GLU PRO PRO PRO SER THR VAL SER ASN MET ALA THR
SEQRES 23 A 348 VAL ALA VAL LEU VAL VAL LEU GLY ALA ALA ILE VAL THR
SEQRES 24 A 348 GLY ALA VAL VAL ALA PHE VAL MET LYS MET ARG ARG ARG
SEQRES 25 A 348 ASN THR GLY GLY LYS GLY GLY ASP TYR ALA LEU ALA PRO
SEQRES 26 A 348 GLY SER GLN THR SER ASP LEU SER LEU PRO ASP CYS LYS
SEQRES 27 A 348 VAL MET VAL HIS ASP PRO HIS SER LEU ALA
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 VAL TYR ASN LEU ALA THR MET
SEQRES 1 D 348 GLY PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER
SEQRES 2 D 348 ARG PRO GLY LEU GLY GLU PRO ARG TYR MET GLU VAL GLY
SEQRES 3 D 348 TYR VAL ASP ASP THR GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 D 348 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP MET
SEQRES 5 D 348 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 D 348 LYS ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU
SEQRES 7 D 348 ARG THR LEU LEU GLY TYR TYR ASN GLN SER LYS GLY GLY
SEQRES 8 D 348 SER HIS THR ILE GLN VAL ILE SER GLY CYS GLU VAL GLY
SEQRES 9 D 348 SER ASP GLY ARG LEU LEU ARG GLY TYR GLN GLN TYR ALA
SEQRES 10 D 348 TYR ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 D 348 LYS THR TRP THR ALA ALA ASP MET ALA ALA LEU ILE THR
SEQRES 12 D 348 LYS HIS LYS TRP GLU GLN ALA GLY GLU ALA GLU ARG LEU
SEQRES 13 D 348 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 D 348 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 D 348 ASP SER PRO LYS ALA HIS VAL THR HIS HIS SER ARG PRO
SEQRES 16 D 348 GLU ASP LYS VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 D 348 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 D 348 GLU GLU LEU ILE GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 D 348 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 D 348 VAL VAL PRO LEU GLY LYS GLU GLN TYR TYR THR CYS HIS
SEQRES 21 D 348 VAL TYR HIS GLN GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 D 348 TRP GLU PRO PRO PRO SER THR VAL SER ASN MET ALA THR
SEQRES 23 D 348 VAL ALA VAL LEU VAL VAL LEU GLY ALA ALA ILE VAL THR
SEQRES 24 D 348 GLY ALA VAL VAL ALA PHE VAL MET LYS MET ARG ARG ARG
SEQRES 25 D 348 ASN THR GLY GLY LYS GLY GLY ASP TYR ALA LEU ALA PRO
SEQRES 26 D 348 GLY SER GLN THR SER ASP LEU SER LEU PRO ASP CYS LYS
SEQRES 27 D 348 VAL MET VAL HIS ASP PRO HIS SER LEU ALA
SEQRES 1 E 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 E 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 E 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 E 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 E 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 E 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 E 99 ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO LYS
SEQRES 8 E 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 F 9 LYS ALA VAL TYR ASN LEU ALA THR MET
FORMUL 7 HOH *63(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 ALA A 1051 ALA A 1061A 1 12
HELIX 4 4 GLY A 1062 GLY A 1072A 1 12
HELIX 5 5 GLY A 1072A GLY A 1085 1 14
HELIX 6 6 GLY A 1085 LEU A 1090 1 6
HELIX 7 7 ALA D 49 GLU D 53 5 5
HELIX 8 8 GLY D 56 TYR D 85 1 30