HEADER IMMUNE SYSTEM 01-AUG-23 8TN5 TITLE THE CRYSTAL STRUCTURE OF A HUMAN MONOCLONAL ANTIBODY (AAB), TERMED TITLE 2 TG10, COMPLEXED WITH A GLCNH2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: TG10, HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TG10, LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS MONOCLONAL ANTIBODY, TG10, GLCNAC, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.LI,A.WLODAWER,S.TEMME,J.GILDERSLEEVE REVDAT 1 04-DEC-24 8TN5 0 JRNL AUTH S.TEMME,M.LI,A.WLODAWER,J.GILDERSLEEVE JRNL TITL AN HUMAN DPNAG-SPECIFIC MONOCLONAL ANTIBODY PROVIDES JRNL TITL 2 PROTECTION FROM A LETHAL S. AUREUS CHANGENGE AND REVEALS JRNL TITL 3 UNIQUE BIOFILM FEATURE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.76 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0405 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) : 1.76 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.40 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 48642 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) : 0.165 REMARK 3 R VALUE (WORKING SET) : 0.164 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1025 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) : 1.76 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2910 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.77 REMARK 3 BIN R VALUE (WORKING SET) : 0.2390 REMARK 3 BIN FREE R VALUE SET COUNT : 60 REMARK 3 BIN FREE R VALUE : 0.2630 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3310 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 53 REMARK 3 SOLVENT ATOMS : 423 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.76 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.05000 REMARK 3 B22 (A**2) : 0.05000 REMARK 3 B33 (A**2) : -0.15000 REMARK 3 B12 (A**2) : 0.02000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.099 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.184 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3478 ; 0.009 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3153 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4745 ; 1.569 ; 1.645 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7323 ; 0.577 ; 1.566 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 448 ; 7.482 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 16 ; 4.471 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 555 ;14.270 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 537 ; 0.074 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4026 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 774 ; 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): 1759 ; 1.969 ; 1.790 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1759 ; 1.964 ; 1.790 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2200 ; 2.884 ; 3.198 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2201 ; 2.883 ; 3.201 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1719 ; 3.113 ; 2.097 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1720 ; 3.112 ; 2.099 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2540 ; 4.589 ; 3.692 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3912 ; 7.983 ;24.430 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3913 ; 7.982 ;24.440 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 : 6 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 : L 1 L 127 REMARK 3 ORIGIN FOR THE GROUP (A): 18.0277 19.8775 101.7358 REMARK 3 T TENSOR REMARK 3 T11: 0.0842 T22: 0.0640 REMARK 3 T33: 0.0631 T12: 0.0088 REMARK 3 T13: -0.0113 T23: -0.0096 REMARK 3 L TENSOR REMARK 3 L11: 0.3856 L22: 0.2731 REMARK 3 L33: 0.4214 L12: -0.1116 REMARK 3 L13: 0.3272 L23: -0.2743 REMARK 3 S TENSOR REMARK 3 S11: -0.0167 S12: -0.0139 S13: -0.0305 REMARK 3 S21: -0.0084 S22: 0.0107 S23: -0.0126 REMARK 3 S31: -0.0291 S32: -0.0242 S33: 0.0061 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 : L 128 L 234 REMARK 3 ORIGIN FOR THE GROUP (A): 25.1828 54.2911 111.1566 REMARK 3 T TENSOR REMARK 3 T11: 0.0948 T22: 0.0614 REMARK 3 T33: 0.1235 T12: 0.0312 REMARK 3 T13: -0.0670 T23: -0.0384 REMARK 3 L TENSOR REMARK 3 L11: 1.1580 L22: 0.7422 REMARK 3 L33: 1.3915 L12: -0.0075 REMARK 3 L13: 1.2687 L23: -0.0115 REMARK 3 S TENSOR REMARK 3 S11: -0.1928 S12: -0.2265 S13: 0.2022 REMARK 3 S21: -0.1216 S22: -0.0305 S23: 0.0046 REMARK 3 S31: -0.2032 S32: -0.2482 S33: 0.2233 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 : H 1 H 128 REMARK 3 ORIGIN FOR THE GROUP (A): 6.3624 29.1690 85.8361 REMARK 3 T TENSOR REMARK 3 T11: 0.0735 T22: 0.0683 REMARK 3 T33: 0.0735 T12: 0.0144 REMARK 3 T13: -0.0090 T23: -0.0125 REMARK 3 L TENSOR REMARK 3 L11: 0.2769 L22: 0.3404 REMARK 3 L33: 0.2609 L12: -0.2908 REMARK 3 L13: 0.1251 L23: -0.0535 REMARK 3 S TENSOR REMARK 3 S11: -0.0115 S12: 0.0224 S13: 0.0250 REMARK 3 S21: 0.0365 S22: -0.0189 S23: -0.0292 REMARK 3 S31: 0.0174 S32: -0.0142 S33: 0.0304 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 : H 129 H 140 REMARK 3 ORIGIN FOR THE GROUP (A): 17.5547 57.4515 93.4799 REMARK 3 T TENSOR REMARK 3 T11: 0.1169 T22: 0.0341 REMARK 3 T33: 0.1535 T12: -0.0511 REMARK 3 T13: -0.0847 T23: 0.0698 REMARK 3 L TENSOR REMARK 3 L11: 6.5296 L22: 0.5880 REMARK 3 L33: 1.6918 L12: 0.2159 REMARK 3 L13: 2.1619 L23: 0.8236 REMARK 3 S TENSOR REMARK 3 S11: -0.3086 S12: 0.1443 S13: 0.3118 REMARK 3 S21: -0.2402 S22: 0.0798 S23: 0.0924 REMARK 3 S31: -0.4057 S32: 0.1487 S33: 0.2287 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 : H 141 H 150 REMARK 3 ORIGIN FOR THE GROUP (A): 38.2296 57.4318 106.0749 REMARK 3 T TENSOR REMARK 3 T11: 0.0637 T22: 0.1035 REMARK 3 T33: 0.1621 T12: -0.0037 REMARK 3 T13: -0.0041 T23: 0.0733 REMARK 3 L TENSOR REMARK 3 L11: 3.8673 L22: 0.9070 REMARK 3 L33: 0.3189 L12: 1.7989 REMARK 3 L13: 1.0598 L23: 0.5375 REMARK 3 S TENSOR REMARK 3 S11: -0.1422 S12: -0.0048 S13: 0.0357 REMARK 3 S21: -0.0794 S22: 0.0675 S23: 0.1145 REMARK 3 S31: -0.0462 S32: 0.0399 S33: 0.0747 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 : H 151 H 231 REMARK 3 ORIGIN FOR THE GROUP (A): 25.8078 52.8123 94.1777 REMARK 3 T TENSOR REMARK 3 T11: 0.1132 T22: 0.2772 REMARK 3 T33: 0.1859 T12: -0.1468 REMARK 3 T13: -0.0655 T23: 0.1133 REMARK 3 L TENSOR REMARK 3 L11: 3.2727 L22: 0.8848 REMARK 3 L33: 2.4052 L12: 1.5118 REMARK 3 L13: 2.6560 L23: 1.4392 REMARK 3 S TENSOR REMARK 3 S11: -0.3732 S12: 0.4042 S13: -0.3032 REMARK 3 S21: -0.2868 S22: 0.4029 S23: 0.0218 REMARK 3 S31: -0.4463 S32: 0.5378 S33: -0.0297 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : 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 8TN5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-23. REMARK 100 THE DEPOSITION ID IS D_1000276245. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-SEP-22 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 : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49758 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760 REMARK 200 RESOLUTION RANGE LOW (A) : 78.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 200 DATA REDUNDANCY : 18.30 REMARK 200 R MERGE (I) : 0.07200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 28.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.63200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: REFMAC REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.76 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M AMMONIUM SULFATE, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 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 138.20000 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 69.10000 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 103.65000 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 34.55000 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 172.75000 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 138.20000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 69.10000 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 34.55000 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 103.65000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 172.75000 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: 5430 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 S SO4 H 303 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 567 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 555 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 601 LIES ON A SPECIAL POSITION. 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 OE2 GLU L 143 O HOH L 401 2.14 REMARK 500 O HOH L 572 O HOH L 574 2.16 REMARK 500 O HOH H 428 O HOH H 529 2.16 REMARK 500 O3 SO4 L 303 O HOH L 402 2.17 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 ARG L 128 NE - CZ - NH1 ANGL. DEV. = 3.0 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 ALA H 100 163.98 177.11 REMARK 500 ASP H 107 125.95 -38.41 REMARK 500 ASP H 116 46.65 -96.78 REMARK 500 ASP H 159 60.98 65.57 REMARK 500 THR H 175 -50.90 -129.23 REMARK 500 ALA L 57 -38.35 74.23 REMARK 500 ALA L 100 174.71 179.60 REMARK 500 ASN L 158 71.47 63.43 REMARK 500 ASP L 171 43.90 34.60 REMARK 500 ASN L 172 -6.34 86.64 REMARK 500 REMARK 500 REMARK: NULL DBREF 8TN5 H 1 231 PDB 8TN5 8TN5 1 231 DBREF 8TN5 L 1 234 PDB 8TN5 8TN5 1 234 SEQRES 1 H 221 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 221 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 H 221 PHE PRO PHE SER SER TYR TRP MET SER TRP VAL ARG GLN SEQRES 4 H 221 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ASN ILE LYS SEQRES 5 H 221 GLU ASP GLY SER GLU LYS TYR TYR VAL ASP SER VAL LYS SEQRES 6 H 221 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 221 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 221 ALA VAL TYR TYR CYS ALA THR ASP PRO ASP VAL GLY LEU SEQRES 9 H 221 SER ASP SER TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY ASP ARG ALA THR HIS SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER ARG SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY GLN THR PRO ARG LEU PHE ILE TYR GLY ALA SEQRES 5 L 215 SER ASN ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR TYR PHE THR LEU THR ILE SER ARG SEQRES 7 L 215 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 215 TYR ASP SER ALA PRO ASP THR PHE GLY GLN GLY THR ARG SEQRES 9 L 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS HET SO4 H 301 5 HET SO4 H 302 5 HET SO4 H 303 5 HET SO4 H 304 5 HET SO4 H 305 5 HET CL H 306 1 HET SO4 L 301 5 HET SO4 L 302 5 HET SO4 L 303 5 HET GCS L 304 12 HETNAM SO4 SULFATE ION HETNAM CL CHLORIDE ION HETNAM GCS 2-AMINO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN GCS BETA-D-GLUCOSAMINE; 2-AMINO-2-DEOXY-BETA-D-GLUCOSE; 2- HETSYN 2 GCS AMINO-2-DEOXY-D-GLUCOSE; 2-AMINO-2-DEOXY-GLUCOSE; D- HETSYN 3 GCS GLUCOSAMINE FORMUL 3 SO4 8(O4 S 2-) FORMUL 8 CL CL 1- FORMUL 12 GCS C6 H13 N O5 FORMUL 13 HOH *423(H2 O) HELIX 1 AA1 PRO H 29 TYR H 37 5 5 HELIX 2 AA2 ASP H 69 LYS H 72 5 4 HELIX 3 AA3 ASN H 82 LYS H 84 5 3 HELIX 4 AA4 ARG H 95 THR H 99 5 5 HELIX 5 AA5 PRO H 108 GLY H 113 5 4 HELIX 6 AA6 SER H 142 LYS H 144 5 3 HELIX 7 AA7 SER H 171 ALA H 173 5 3 HELIX 8 AA8 SER H 202 GLN H 207 1 6 HELIX 9 AA9 LYS H 216 ASN H 219 5 4 HELIX 10 AB1 VAL L 29 SER L 37 5 4 HELIX 11 AB2 GLU L 95 PHE L 99 5 5 HELIX 12 AB3 SER L 141 LYS L 146 1 6 HELIX 13 AB4 LYS L 203 LYS L 208 1 6 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 19 SER H 26 -1 O SER H 26 N GLN H 3 SHEET 3 AA1 4 SER H 86 MET H 91 -1 O MET H 91 N LEU H 19 SHEET 4 AA1 4 PHE H 76 ASP H 81 -1 N ASP H 81 O SER H 86 SHEET 1 AA2 6 GLY H 11 VAL H 13 0 SHEET 2 AA2 6 THR H 122 VAL H 126 1 O THR H 125 N VAL H 13 SHEET 3 AA2 6 ALA H 100 THR H 106 -1 N ALA H 100 O VAL H 124 SHEET 4 AA2 6 MET H 39 GLN H 44 -1 N VAL H 42 O TYR H 103 SHEET 5 AA2 6 LEU H 50 ILE H 56 -1 O GLU H 51 N ARG H 43 SHEET 6 AA2 6 LYS H 65 TYR H 67 -1 O TYR H 66 N ASN H 55 SHEET 1 AA3 4 SER H 135 LEU H 139 0 SHEET 2 AA3 4 THR H 150 TYR H 160 -1 O LEU H 156 N PHE H 137 SHEET 3 AA3 4 TYR H 191 PRO H 200 -1 O LEU H 193 N VAL H 157 SHEET 4 AA3 4 VAL H 178 THR H 180 -1 N HIS H 179 O VAL H 196 SHEET 1 AA4 4 THR H 146 SER H 147 0 SHEET 2 AA4 4 THR H 150 TYR H 160 -1 O THR H 150 N SER H 147 SHEET 3 AA4 4 TYR H 191 PRO H 200 -1 O LEU H 193 N VAL H 157 SHEET 4 AA4 4 VAL H 184 LEU H 185 -1 N VAL H 184 O SER H 192 SHEET 1 AA5 3 THR H 166 TRP H 169 0 SHEET 2 AA5 3 ILE H 210 HIS H 215 -1 O ASN H 212 N SER H 168 SHEET 3 AA5 3 THR H 220 LYS H 225 -1 O THR H 220 N HIS H 215 SHEET 1 AA6 4 LEU L 4 SER L 7 0 SHEET 2 AA6 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA6 4 TYR L 86 ILE L 91 -1 O PHE L 87 N CYS L 23 SHEET 4 AA6 4 PHE L 76 SER L 83 -1 N SER L 77 O THR L 90 SHEET 1 AA7 6 THR L 10 LEU L 13 0 SHEET 2 AA7 6 THR L 122 ILE L 126 1 O GLU L 125 N LEU L 11 SHEET 3 AA7 6 ALA L 100 GLN L 106 -1 N ALA L 100 O LEU L 124 SHEET 4 AA7 6 LEU L 39 GLN L 44 -1 N ALA L 40 O GLN L 105 SHEET 5 AA7 6 ARG L 51 TYR L 55 -1 O PHE L 53 N TRP L 41 SHEET 6 AA7 6 ASN L 66 ARG L 67 -1 O ASN L 66 N TYR L 55 SHEET 1 AA8 4 SER L 134 PHE L 138 0 SHEET 2 AA8 4 THR L 149 PHE L 159 -1 O ASN L 157 N SER L 134 SHEET 3 AA8 4 TYR L 193 SER L 202 -1 O SER L 197 N CYS L 154 SHEET 4 AA8 4 SER L 179 VAL L 183 -1 N GLN L 180 O THR L 198 SHEET 1 AA9 4 ALA L 173 LEU L 174 0 SHEET 2 AA9 4 LYS L 165 VAL L 170 -1 N VAL L 170 O ALA L 173 SHEET 3 AA9 4 VAL L 211 THR L 217 -1 O GLU L 215 N GLN L 167 SHEET 4 AA9 4 VAL L 225 ASN L 230 -1 O VAL L 225 N VAL L 216 SSBOND 1 CYS H 23 CYS H 104 1555 1555 1.97 SSBOND 2 CYS H 155 CYS H 211 1555 1555 2.06 SSBOND 3 CYS L 23 CYS L 104 1555 1555 2.15 SSBOND 4 CYS L 154 CYS L 214 1555 1555 2.06 CISPEP 1 PHE H 161 PRO H 162 0 -13.83 CISPEP 2 GLU H 163 PRO H 164 0 -7.64 CISPEP 3 SER L 7 PRO L 8 0 -5.34 CISPEP 4 ALA L 114 PRO L 115 0 -0.31 CISPEP 5 TYR L 160 PRO L 161 0 3.38 CRYST1 90.524 90.524 207.300 90.00 90.00 120.00 P 65 2 2 12 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 0.011047 0.006378 0.000000 0.00000 SCALE2 0.000000 0.012756 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004824 0.00000