HEADER IMMUNE SYSTEM 06-AUG-15 5D3I
TITLE CRYSTAL STRUCTURE OF THE SSL3-TLR2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLL-LIKE RECEPTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 25-589;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: STAPHYLOCOCCAL SUPERANTIGEN-LIKE PROTEIN 3;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: TLR2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293-EBNA1-S;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN NCTC 8325);
SOURCE 12 ORGANISM_TAXID: 93061;
SOURCE 13 GENE: SAOUHSC_00386;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VARIANT: ROSETTA-GAMI
KEYWDS SUPERANTIGENS, SUPERANTIGEN-LIKE PROTEINS, SSL, SSL3, TOLL-LIKE
KEYWDS 2 RECEPTOR 2, TLR2, TLR6, IMMUNOLOGY, INFLAMMATION, INHIBITION,
KEYWDS 3 LIPOPEPTIDE, PHOSPHATIDYLCHOLINE, PC, IMMUNE EVASION, INNATE
KEYWDS 4 IMMUNITY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.FEITSMA,E.G.HUIZINGA
REVDAT 5 01-MAY-24 5D3I 1 HETSYN
REVDAT 4 29-JUL-20 5D3I 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 09-SEP-15 5D3I 1 JRNL
REVDAT 2 02-SEP-15 5D3I 1 JRNL
REVDAT 1 19-AUG-15 5D3I 0
JRNL AUTH K.J.KOYMANS,L.J.FEITSMA,T.H.BRONDIJK,P.C.AERTS,E.LUKKIEN,
JRNL AUTH 2 P.LOSSL,K.P.VAN KESSEL,C.J.DE HAAS,J.A.VAN STRIJP,
JRNL AUTH 3 E.G.HUIZINGA
JRNL TITL STRUCTURAL BASIS FOR INHIBITION OF TLR2 BY STAPHYLOCOCCAL
JRNL TITL 2 SUPERANTIGEN-LIKE PROTEIN 3 (SSL3).
JRNL REF PROC.NATL.ACAD.SCI.USA V. 112 11018 2015
JRNL REFN ESSN 1091-6490
JRNL PMID 26283364
JRNL DOI 10.1073/PNAS.1502026112
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 14583
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780
REMARK 3 FREE R VALUE TEST SET COUNT : 697
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 52.1059 - 5.4704 0.87 2635 119 0.1836 0.2321
REMARK 3 2 5.4704 - 4.3427 0.93 2780 144 0.1926 0.2167
REMARK 3 3 4.3427 - 3.7939 0.94 2797 145 0.2294 0.2766
REMARK 3 4 3.7939 - 3.4471 0.97 2862 143 0.2912 0.3640
REMARK 3 5 3.4471 - 3.2001 0.95 2812 146 0.3501 0.3570
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.530
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 6092
REMARK 3 ANGLE : 1.199 8225
REMARK 3 CHIRALITY : 0.054 954
REMARK 3 PLANARITY : 0.005 1034
REMARK 3 DIHEDRAL : 13.148 2286
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3749 5.0814 2.0196
REMARK 3 T TENSOR
REMARK 3 T11: 1.0956 T22: 1.0655
REMARK 3 T33: 1.3315 T12: 0.5172
REMARK 3 T13: -0.3441 T23: -0.0650
REMARK 3 L TENSOR
REMARK 3 L11: 3.3166 L22: 1.8609
REMARK 3 L33: 3.8450 L12: -0.2992
REMARK 3 L13: 1.5023 L23: -0.4543
REMARK 3 S TENSOR
REMARK 3 S11: 1.0463 S12: 0.1676 S13: -1.4375
REMARK 3 S21: 0.0904 S22: -0.1604 S23: -1.0305
REMARK 3 S31: 1.5616 S32: 1.2278 S33: 1.9636
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 146 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7567 14.7020 -1.3176
REMARK 3 T TENSOR
REMARK 3 T11: 0.5569 T22: 0.5115
REMARK 3 T33: 0.4939 T12: 0.0262
REMARK 3 T13: -0.0224 T23: 0.1979
REMARK 3 L TENSOR
REMARK 3 L11: 7.5393 L22: 4.8226
REMARK 3 L33: 5.8214 L12: -2.8846
REMARK 3 L13: 2.5419 L23: -2.9106
REMARK 3 S TENSOR
REMARK 3 S11: 0.2760 S12: -0.7359 S13: -0.7356
REMARK 3 S21: 0.1793 S22: 0.3317 S23: -0.1345
REMARK 3 S31: 0.8347 S32: 0.0216 S33: 0.9959
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 344 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4917 29.4781 -14.4205
REMARK 3 T TENSOR
REMARK 3 T11: 0.5038 T22: 0.3955
REMARK 3 T33: 0.3492 T12: -0.0168
REMARK 3 T13: 0.0458 T23: 0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 3.3946 L22: 7.8467
REMARK 3 L33: 6.4492 L12: 0.7791
REMARK 3 L13: -2.4856 L23: -0.1860
REMARK 3 S TENSOR
REMARK 3 S11: -0.1268 S12: -0.1684 S13: 0.5126
REMARK 3 S21: -0.4371 S22: 0.1082 S23: 0.5056
REMARK 3 S31: 0.1323 S32: -0.6880 S33: -0.2664
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 345 THROUGH 538 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9992 47.6699 -25.9604
REMARK 3 T TENSOR
REMARK 3 T11: 0.3873 T22: 0.5171
REMARK 3 T33: 0.5137 T12: 0.0350
REMARK 3 T13: 0.0703 T23: 0.2015
REMARK 3 L TENSOR
REMARK 3 L11: 7.0855 L22: 2.0006
REMARK 3 L33: 3.8754 L12: 1.9653
REMARK 3 L13: 1.6860 L23: 0.1523
REMARK 3 S TENSOR
REMARK 3 S11: -0.2298 S12: 0.6376 S13: 0.3495
REMARK 3 S21: 0.0707 S22: 0.0416 S23: -0.2379
REMARK 3 S31: -0.1182 S32: 0.8733 S33: -0.0654
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 539 THROUGH 575 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1878 42.4780 -15.4302
REMARK 3 T TENSOR
REMARK 3 T11: 0.5819 T22: 1.5403
REMARK 3 T33: 1.4853 T12: -0.0479
REMARK 3 T13: -0.0218 T23: 0.4307
REMARK 3 L TENSOR
REMARK 3 L11: 1.1250 L22: 0.8819
REMARK 3 L33: 1.7342 L12: -0.8578
REMARK 3 L13: 0.8768 L23: -0.0965
REMARK 3 S TENSOR
REMARK 3 S11: -0.1104 S12: -1.3626 S13: -0.7480
REMARK 3 S21: -0.0339 S22: 0.2291 S23: -0.9126
REMARK 3 S31: 0.1488 S32: 1.2800 S33: 0.0159
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.6926 37.8780 -41.8451
REMARK 3 T TENSOR
REMARK 3 T11: 0.6124 T22: 1.1261
REMARK 3 T33: 0.6029 T12: -0.2669
REMARK 3 T13: 0.0115 T23: 0.1412
REMARK 3 L TENSOR
REMARK 3 L11: 5.2608 L22: 3.6948
REMARK 3 L33: 0.8109 L12: -2.9381
REMARK 3 L13: -0.0966 L23: 0.7771
REMARK 3 S TENSOR
REMARK 3 S11: -0.4305 S12: -0.9732 S13: 0.6459
REMARK 3 S21: -0.0228 S22: -0.1189 S23: 1.4883
REMARK 3 S31: 0.4042 S32: -1.8179 S33: -0.1252
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 153 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9680 35.4062 -40.5031
REMARK 3 T TENSOR
REMARK 3 T11: 0.7911 T22: 0.5991
REMARK 3 T33: 0.7550 T12: -0.0002
REMARK 3 T13: -0.3171 T23: 0.0789
REMARK 3 L TENSOR
REMARK 3 L11: 5.1390 L22: 5.2768
REMARK 3 L33: 8.2684 L12: -2.0963
REMARK 3 L13: -2.4696 L23: 6.1079
REMARK 3 S TENSOR
REMARK 3 S11: 0.8217 S12: 1.0036 S13: -0.8974
REMARK 3 S21: 0.4064 S22: -1.9012 S23: 0.9881
REMARK 3 S31: 0.7738 S32: -0.4850 S33: -1.7178
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 168 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2612 37.6539 -40.8185
REMARK 3 T TENSOR
REMARK 3 T11: 0.5456 T22: 0.5891
REMARK 3 T33: 0.5952 T12: -0.0083
REMARK 3 T13: -0.0375 T23: 0.1169
REMARK 3 L TENSOR
REMARK 3 L11: 4.9255 L22: 1.5273
REMARK 3 L33: 1.9162 L12: 0.1129
REMARK 3 L13: 3.3729 L23: 0.3372
REMARK 3 S TENSOR
REMARK 3 S11: -0.0877 S12: 0.5902 S13: -0.2735
REMARK 3 S21: -0.2677 S22: 0.2284 S23: 0.2228
REMARK 3 S31: 0.1007 S32: 0.3280 S33: -0.0016
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 190 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7264 42.9528 -43.5175
REMARK 3 T TENSOR
REMARK 3 T11: 0.5209 T22: 0.5376
REMARK 3 T33: 0.4794 T12: -0.0267
REMARK 3 T13: -0.0007 T23: 0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 5.2204 L22: 7.8314
REMARK 3 L33: 5.8705 L12: -2.3652
REMARK 3 L13: 1.5903 L23: 4.8719
REMARK 3 S TENSOR
REMARK 3 S11: 0.2045 S12: 0.8478 S13: 0.1865
REMARK 3 S21: 0.3084 S22: 0.7210 S23: -1.4464
REMARK 3 S31: 0.0218 S32: 0.7926 S33: 2.2550
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 203 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8625 40.2186 -41.2233
REMARK 3 T TENSOR
REMARK 3 T11: 0.3723 T22: 0.7001
REMARK 3 T33: 0.6045 T12: -0.0984
REMARK 3 T13: -0.0492 T23: 0.0914
REMARK 3 L TENSOR
REMARK 3 L11: 4.1394 L22: 1.4846
REMARK 3 L33: 7.1228 L12: -0.8237
REMARK 3 L13: 2.5091 L23: 0.5212
REMARK 3 S TENSOR
REMARK 3 S11: -0.0775 S12: -0.3717 S13: -0.1686
REMARK 3 S21: -0.6921 S22: 0.0532 S23: 0.2025
REMARK 3 S31: 0.5222 S32: -0.5782 S33: -0.0100
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 229 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.3998 51.1233 -53.0525
REMARK 3 T TENSOR
REMARK 3 T11: 0.4409 T22: 1.2386
REMARK 3 T33: 1.2917 T12: 0.1975
REMARK 3 T13: -0.0539 T23: 0.1942
REMARK 3 L TENSOR
REMARK 3 L11: 7.9190 L22: 0.8937
REMARK 3 L33: 1.9016 L12: 1.3298
REMARK 3 L13: 1.4435 L23: -0.5067
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S12: 0.4710 S13: 0.8800
REMARK 3 S21: 0.7980 S22: 1.1550 S23: 1.9467
REMARK 3 S31: -0.7912 S32: -1.3684 S33: 1.9480
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 244 THROUGH 256 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9903 55.3566 -49.5372
REMARK 3 T TENSOR
REMARK 3 T11: 1.0086 T22: 1.4397
REMARK 3 T33: 0.7923 T12: 0.2407
REMARK 3 T13: -0.0211 T23: -0.1391
REMARK 3 L TENSOR
REMARK 3 L11: 1.0519 L22: 2.5755
REMARK 3 L33: 1.5921 L12: -0.6301
REMARK 3 L13: 1.5028 L23: -0.4365
REMARK 3 S TENSOR
REMARK 3 S11: 0.2839 S12: 1.2834 S13: 0.6232
REMARK 3 S21: 0.0968 S22: -0.7066 S23: 0.4203
REMARK 3 S31: -0.5361 S32: -1.1953 S33: 0.1283
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 257 THROUGH 326 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7343 45.3789 -52.4823
REMARK 3 T TENSOR
REMARK 3 T11: 0.4938 T22: 0.6950
REMARK 3 T33: 0.5128 T12: -0.0132
REMARK 3 T13: 0.0280 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 4.6651 L22: 5.8729
REMARK 3 L33: 6.3674 L12: 2.6183
REMARK 3 L13: -0.1852 L23: -0.8013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0758 S12: -0.2902 S13: 0.1478
REMARK 3 S21: 0.0575 S22: 0.0209 S23: 0.3418
REMARK 3 S31: 0.3322 S32: -0.9304 S33: 0.0004
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5D3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS MARCH 2013
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 1.7.6
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14687
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 52.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.22500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 1.08000
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 2.5.2
REMARK 200 STARTING MODEL: TLR2, SSL3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PCB, PEG1500, PH 5.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.20833
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 102.41667
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 76.81250
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 128.02083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 25.60417
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 GLY A 23
REMARK 465 SER A 24
REMARK 465 GLN A 25
REMARK 465 GLU A 26
REMARK 465 GLN A 576
REMARK 465 ASP A 577
REMARK 465 ALA A 578
REMARK 465 ARG A 579
REMARK 465 PRO A 580
REMARK 465 SER A 581
REMARK 465 VAL A 582
REMARK 465 LEU A 583
REMARK 465 GLU A 584
REMARK 465 CYS A 585
REMARK 465 HIS A 586
REMARK 465 GLN A 587
REMARK 465 ALA A 588
REMARK 465 ALA A 589
REMARK 465 ALA A 590
REMARK 465 GLY B 132
REMARK 465 SER B 133
REMARK 465 MET B 134
REMARK 465 THR B 135
REMARK 465 PRO B 136
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 566 OG
REMARK 470 PRO A 567 CG CD
REMARK 470 PRO A 568 CG CD
REMARK 470 ARG A 569 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 570 CG CD1 CD2
REMARK 470 HIS A 571 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 573 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 574 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 575 CG CD1 CD2
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 NH1 ARG A 257 OD2 ASP A 285 2.15
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 ASN A 62 -158.22 -113.13
REMARK 500 ARG A 87 44.09 -106.27
REMARK 500 LEU A 99 47.72 -93.34
REMARK 500 ASN A 110 -161.96 -109.24
REMARK 500 PRO A 135 34.43 -73.33
REMARK 500 GLN A 192 2.90 82.42
REMARK 500 PRO A 243 106.40 -54.98
REMARK 500 GLU A 246 -73.93 -55.00
REMARK 500 PHE A 295 -32.53 -141.88
REMARK 500 ASN A 296 74.15 30.57
REMARK 500 TYR A 323 -71.26 -117.61
REMARK 500 TYR A 326 -30.09 -145.87
REMARK 500 ASN A 370 -157.54 -122.58
REMARK 500 ALA A 381 52.08 -106.42
REMARK 500 LYS A 383 96.14 -68.25
REMARK 500 TRP A 386 59.51 29.84
REMARK 500 ASN A 397 -152.43 -110.98
REMARK 500 THR A 453 8.81 -63.03
REMARK 500 ASN A 467 -157.57 -127.88
REMARK 500 ARG A 507 -166.10 -72.11
REMARK 500 GLU A 508 43.98 18.12
REMARK 500 ASN A 509 -125.21 -110.13
REMARK 500 ALA A 510 31.17 -152.97
REMARK 500 SER A 512 -30.92 -134.47
REMARK 500 PHE A 514 86.35 -154.56
REMARK 500 GLU A 526 -42.12 -131.48
REMARK 500 TYR A 562 69.39 -100.54
REMARK 500 LYS B 161 101.61 -53.56
REMARK 500 PRO B 162 96.35 -55.99
REMARK 500 ASN B 174 -92.53 -125.55
REMARK 500 LYS B 191 -114.68 -108.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PCW A 804
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5D3D RELATED DB: PDB
REMARK 900 5D3D CONTAINS UNBOUND STAPHYLOCOCCAL SUPERANTIGEN-LIKE PROTEIN 3
REMARK 900 (SSL3)
DBREF 5D3I A 25 589 UNP Q9QUN7 TLR2_MOUSE 25 589
DBREF 5D3I B 134 326 UNP Q2G0X7 Q2G0X7_STAA8 164 356
SEQADV 5D3I GLY A 23 UNP Q9QUN7 EXPRESSION TAG
SEQADV 5D3I SER A 24 UNP Q9QUN7 EXPRESSION TAG
SEQADV 5D3I ALA A 590 UNP Q9QUN7 EXPRESSION TAG
SEQADV 5D3I GLY B 132 UNP Q2G0X7 EXPRESSION TAG
SEQADV 5D3I SER B 133 UNP Q2G0X7 EXPRESSION TAG
SEQRES 1 A 568 GLY SER GLN GLU SER LEU SER CYS ASP ALA SER GLY VAL
SEQRES 2 A 568 CYS ASP GLY ARG SER ARG SER PHE THR SER ILE PRO SER
SEQRES 3 A 568 GLY LEU THR ALA ALA MET LYS SER LEU ASP LEU SER PHE
SEQRES 4 A 568 ASN LYS ILE THR TYR ILE GLY HIS GLY ASP LEU ARG ALA
SEQRES 5 A 568 CYS ALA ASN LEU GLN VAL LEU ILE LEU LYS SER SER ARG
SEQRES 6 A 568 ILE ASN THR ILE GLU GLY ASP ALA PHE TYR SER LEU GLY
SEQRES 7 A 568 SER LEU GLU HIS LEU ASP LEU SER ASP ASN HIS LEU SER
SEQRES 8 A 568 SER LEU SER SER SER TRP PHE GLY PRO LEU SER SER LEU
SEQRES 9 A 568 LYS TYR LEU ASN LEU MET GLY ASN PRO TYR GLN THR LEU
SEQRES 10 A 568 GLY VAL THR SER LEU PHE PRO ASN LEU THR ASN LEU GLN
SEQRES 11 A 568 THR LEU ARG ILE GLY ASN VAL GLU THR PHE SER GLU ILE
SEQRES 12 A 568 ARG ARG ILE ASP PHE ALA GLY LEU THR SER LEU ASN GLU
SEQRES 13 A 568 LEU GLU ILE LYS ALA LEU SER LEU ARG ASN TYR GLN SER
SEQRES 14 A 568 GLN SER LEU LYS SER ILE ARG ASP ILE HIS HIS LEU THR
SEQRES 15 A 568 LEU HIS LEU SER GLU SER ALA PHE LEU LEU GLU ILE PHE
SEQRES 16 A 568 ALA ASP ILE LEU SER SER VAL ARG TYR LEU GLU LEU ARG
SEQRES 17 A 568 ASP THR ASN LEU ALA ARG PHE GLN PHE SER PRO LEU PRO
SEQRES 18 A 568 VAL ASP GLU VAL SER SER PRO MET LYS LYS LEU ALA PHE
SEQRES 19 A 568 ARG GLY SER VAL LEU THR ASP GLU SER PHE ASN GLU LEU
SEQRES 20 A 568 LEU LYS LEU LEU ARG TYR ILE LEU GLU LEU SER GLU VAL
SEQRES 21 A 568 GLU PHE ASP ASP CYS THR LEU ASN GLY LEU GLY ASP PHE
SEQRES 22 A 568 ASN PRO SER GLU SER ASP VAL VAL SER GLU LEU GLY LYS
SEQRES 23 A 568 VAL GLU THR VAL THR ILE ARG ARG LEU HIS ILE PRO GLN
SEQRES 24 A 568 PHE TYR LEU PHE TYR ASP LEU SER THR VAL TYR SER LEU
SEQRES 25 A 568 LEU GLU LYS VAL LYS ARG ILE THR VAL GLU ASN SER LYS
SEQRES 26 A 568 VAL PHE LEU VAL PRO CYS SER PHE SER GLN HIS LEU LYS
SEQRES 27 A 568 SER LEU GLU PHE LEU ASP LEU SER GLU ASN LEU MET VAL
SEQRES 28 A 568 GLU GLU TYR LEU LYS ASN SER ALA CYS LYS GLY ALA TRP
SEQRES 29 A 568 PRO SER LEU GLN THR LEU VAL LEU SER GLN ASN HIS LEU
SEQRES 30 A 568 ARG SER MET GLN LYS THR GLY GLU ILE LEU LEU THR LEU
SEQRES 31 A 568 LYS ASN LEU THR SER LEU ASP ILE SER ARG ASN THR PHE
SEQRES 32 A 568 HIS PRO MET PRO ASP SER CYS GLN TRP PRO GLU LYS MET
SEQRES 33 A 568 ARG PHE LEU ASN LEU SER SER THR GLY ILE ARG VAL VAL
SEQRES 34 A 568 LYS THR CYS ILE PRO GLN THR LEU GLU VAL LEU ASP VAL
SEQRES 35 A 568 SER ASN ASN ASN LEU ASP SER PHE SER LEU PHE LEU PRO
SEQRES 36 A 568 ARG LEU GLN GLU LEU TYR ILE SER ARG ASN LYS LEU LYS
SEQRES 37 A 568 THR LEU PRO ASP ALA SER LEU PHE PRO VAL LEU LEU VAL
SEQRES 38 A 568 MET LYS ILE ARG GLU ASN ALA VAL SER THR PHE SER LYS
SEQRES 39 A 568 ASP GLN LEU GLY SER PHE PRO LYS LEU GLU THR LEU GLU
SEQRES 40 A 568 ALA GLY ASP ASN HIS PHE VAL CYS SER CYS GLU LEU LEU
SEQRES 41 A 568 SER PHE THR MET GLU THR PRO ALA LEU ALA GLN ILE LEU
SEQRES 42 A 568 VAL ASP TRP PRO ASP SER TYR LEU CYS ASP SER PRO PRO
SEQRES 43 A 568 ARG LEU HIS GLY HIS ARG LEU GLN ASP ALA ARG PRO SER
SEQRES 44 A 568 VAL LEU GLU CYS HIS GLN ALA ALA ALA
SEQRES 1 B 195 GLY SER MET THR PRO LYS TYR GLU ASP LEU ARG ALA TYR
SEQRES 2 B 195 TYR THR LYS PRO SER PHE GLU PHE GLU LYS GLN PHE GLY
SEQRES 3 B 195 PHE MET LEU LYS PRO TRP THR THR VAL ARG PHE MET ASN
SEQRES 4 B 195 VAL ILE PRO ASN ARG PHE ILE TYR LYS ILE ALA LEU VAL
SEQRES 5 B 195 GLY LYS ASP GLU LYS LYS TYR LYS ASP GLY PRO TYR ASP
SEQRES 6 B 195 ASN ILE ASP VAL PHE ILE VAL LEU GLU ASP ASN LYS TYR
SEQRES 7 B 195 GLN LEU LYS LYS TYR SER VAL GLY GLY ILE THR LYS THR
SEQRES 8 B 195 ASN SER LYS LYS VAL ASN HIS LYS VAL GLU LEU SER ILE
SEQRES 9 B 195 THR LYS LYS ASP ASN GLN GLY MET ILE SER ARG ASP VAL
SEQRES 10 B 195 SER GLU TYR MET ILE THR LYS GLU GLU ILE SER LEU LYS
SEQRES 11 B 195 GLU LEU ASP PHE LYS LEU ARG LYS GLN LEU ILE GLU LYS
SEQRES 12 B 195 HIS ASN LEU TYR GLY ASN MET GLY SER GLY THR ILE VAL
SEQRES 13 B 195 ILE LYS MET LYS ASN GLY GLY LYS TYR THR PHE GLU LEU
SEQRES 14 B 195 HIS LYS LYS LEU GLN GLU HIS ARG MET ALA ASP VAL ILE
SEQRES 15 B 195 ASP GLY THR ASN ILE ASP ASN ILE GLU VAL ASN ILE LYS
HET NAG C 1 14
HET NAG C 2 14
HET NAG A 801 14
HET PCW A 804 43
HET CL A 805 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
HETNAM CL CHLORIDE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN PCW (Z,Z)-4-HYDROXY-N,N,N-TRIMETHYL-10-OXO-7-[(1-OXO-9-
HETSYN 2 PCW OCTADECENYL)OXY]-3,5,9-TRIOXA-4-PHOSPHAHEPTACOS-18-EN-
HETSYN 3 PCW 1-AMINIUM-4-OXIDE
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 5 PCW C44 H85 N O8 P 1+
FORMUL 6 CL CL 1-
HELIX 1 AA1 PHE A 212 LEU A 221 1 10
HELIX 2 AA2 THR A 262 LYS A 271 1 10
HELIX 3 AA3 LEU A 272 ILE A 276 5 5
HELIX 4 AA4 LEU A 328 LEU A 335 1 8
HELIX 5 AA5 PRO A 352 LEU A 359 1 8
HELIX 6 AA6 VAL A 373 ALA A 381 1 9
HELIX 7 AA7 SER A 401 LEU A 409 1 9
HELIX 8 AA8 LEU A 410 LEU A 412 5 3
HELIX 9 AA9 ASP A 494 PHE A 498 5 5
HELIX 10 AB1 SER A 515 PHE A 522 1 8
HELIX 11 AB2 SER A 538 THR A 548 1 11
HELIX 12 AB3 PRO A 549 ILE A 554 5 6
HELIX 13 AB4 TYR B 138 TYR B 145 1 8
HELIX 14 AB5 GLY B 184 TYR B 190 1 7
HELIX 15 AB6 LEU B 260 ASN B 276 1 17
HELIX 16 AB7 GLN B 305 ALA B 310 5 6
SHEET 1 AA122 SER A 29 CYS A 30 0
SHEET 2 AA122 VAL A 35 ASP A 37 -1 O ASP A 37 N SER A 29
SHEET 3 AA122 SER A 56 ASP A 58 1 O SER A 56 N CYS A 36
SHEET 4 AA122 VAL A 80 ILE A 82 1 O ILE A 82 N LEU A 57
SHEET 5 AA122 HIS A 104 ASP A 106 1 O HIS A 104 N LEU A 81
SHEET 6 AA122 TYR A 128 ASN A 130 1 O TYR A 128 N LEU A 105
SHEET 7 AA122 THR A 153 ASN A 158 1 O ARG A 155 N LEU A 129
SHEET 8 AA122 SER A 175 ALA A 183 1 O LYS A 182 N ILE A 156
SHEET 9 AA122 ASP A 199 HIS A 206 1 O THR A 204 N ILE A 181
SHEET 10 AA122 TYR A 226 ARG A 230 1 O GLU A 228 N LEU A 205
SHEET 11 AA122 LYS A 253 ARG A 257 1 O ARG A 257 N LEU A 229
SHEET 12 AA122 GLU A 281 ASP A 285 1 O ASP A 285 N PHE A 256
SHEET 13 AA122 THR A 311 ARG A 315 1 O THR A 313 N VAL A 282
SHEET 14 AA122 ARG A 340 GLU A 344 1 O THR A 342 N ILE A 314
SHEET 15 AA122 PHE A 364 ASP A 366 1 O ASP A 366 N VAL A 343
SHEET 16 AA122 THR A 391 VAL A 393 1 O VAL A 393 N LEU A 365
SHEET 17 AA122 SER A 417 ASP A 419 1 O SER A 417 N LEU A 392
SHEET 18 AA122 PHE A 440 ASN A 442 1 O PHE A 440 N LEU A 418
SHEET 19 AA122 VAL A 461 ASP A 463 1 O VAL A 461 N LEU A 441
SHEET 20 AA122 GLU A 481 TYR A 483 1 O TYR A 483 N LEU A 462
SHEET 21 AA122 VAL A 503 LYS A 505 1 O VAL A 503 N LEU A 482
SHEET 22 AA122 THR A 527 GLU A 529 1 O THR A 527 N MET A 504
SHEET 1 AA2 2 TYR A 66 ILE A 67 0
SHEET 2 AA2 2 THR A 90 ILE A 91 1 O THR A 90 N ILE A 67
SHEET 1 AA3 2 GLU A 164 ILE A 165 0
SHEET 2 AA3 2 ASN A 188 TYR A 189 1 O ASN A 188 N ILE A 165
SHEET 1 AA4 2 VAL A 260 LEU A 261 0
SHEET 2 AA4 2 THR A 288 LEU A 289 1 O THR A 288 N LEU A 261
SHEET 1 AA5 2 PHE A 535 VAL A 536 0
SHEET 2 AA5 2 CYS A 564 SER A 566 1 O ASP A 565 N PHE A 535
SHEET 1 AA6 3 PHE B 150 GLY B 157 0
SHEET 2 AA6 3 TYR B 195 ILE B 202 -1 O ILE B 202 N PHE B 150
SHEET 3 AA6 3 ILE B 219 LYS B 221 -1 O THR B 220 N ASP B 199
SHEET 1 AA7 3 PHE B 168 VAL B 171 0
SHEET 2 AA7 3 TYR B 178 ALA B 181 -1 O TYR B 178 N VAL B 171
SHEET 3 AA7 3 TYR B 214 VAL B 216 1 O SER B 215 N ALA B 181
SHEET 1 AA8 5 ILE B 244 ILE B 253 0
SHEET 2 AA8 5 HIS B 229 LYS B 238 -1 N ILE B 235 O ASP B 247
SHEET 3 AA8 5 ILE B 318 LYS B 326 1 O VAL B 323 N THR B 236
SHEET 4 AA8 5 SER B 283 MET B 290 -1 N LYS B 289 O ASP B 319
SHEET 5 AA8 5 LYS B 295 GLU B 299 -1 O PHE B 298 N ILE B 286
SHEET 1 AA9 2 GLU B 257 SER B 259 0
SHEET 2 AA9 2 VAL B 312 ASP B 314 -1 O ILE B 313 N ILE B 258
SSBOND 1 CYS A 30 CYS A 36 1555 1555 2.03
SSBOND 2 CYS A 353 CYS A 382 1555 1555 2.03
SSBOND 3 CYS A 432 CYS A 454 1555 1555 2.03
SSBOND 4 CYS A 537 CYS A 564 1555 1555 2.03
LINK ND2 ASN A 414 C1 NAG A 801 1555 1555 1.44
LINK ND2 ASN A 442 C1 NAG C 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
CISPEP 1 TRP A 558 PRO A 559 0 2.32
CISPEP 2 SER A 566 PRO A 567 0 -0.58
CISPEP 3 GLY B 193 PRO B 194 0 -0.57
CRYST1 104.198 104.198 153.625 90.00 90.00 120.00 P 61 6
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 0.009597 0.005541 0.000000 0.00000
SCALE2 0.000000 0.011082 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006509 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
