HEADER VIRAL PROTEIN/IMMUNE SYSTEM 26-SEP-24 9DS1 TITLE CRYSTAL STRUCTURE OF 241_2F04 FAB IN COMPLEX WITH H1 HA FROM TITLE 2 A/CALIFORNIA/04/2009(H1N1) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1 CHAI; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMAGGLUTININ HA2 CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 241_2F04, HEAVY CHAIN; COMPND 11 CHAIN: H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 241_2F04, LIGHT CHAIN; COMPND 15 CHAIN: L; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 GENE: HA; SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 9 ORGANISM_TAXID: 11320; SOURCE 10 GENE: HA; SOURCE 11 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS H1N1, ANTIBODY, HEMAGGLUTININ, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX, KEYWDS 2 VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.H.LIN,I.A.WILSON REVDAT 1 19-MAR-25 9DS1 0 JRNL AUTH T.H.LIN,C.D.LEE,M.L.FERNANDEZ-QUINTERO,J.A.FERGUSON,J.HAN, JRNL AUTH 2 X.ZHU,W.YU,J.J.GUTHMILLER,F.KRAMMER,P.C.WILSON,A.B.WARD, JRNL AUTH 3 I.A.WILSON JRNL TITL STRUCTURALLY CONVERGENT ANTIBODIES DERIVED FROM DIFFERENT JRNL TITL 2 VACCINE STRATEGIES TARGET THE INFLUENZA VIRUS HA ANCHOR JRNL TITL 3 EPITOPE WITH A SUBSET OF V H 3 AND V K 3 GENES. JRNL REF NAT COMMUN V. 16 1268 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 39894881 JRNL DOI 10.1038/S41467-025-56496-4 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21RC1_5127: ???) 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) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.43 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 3 NUMBER OF REFLECTIONS : 54191 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110 REMARK 3 FREE R VALUE TEST SET COUNT : 2768 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 39.4300 - 6.5000 0.99 2862 141 0.1874 0.2320 REMARK 3 2 6.5000 - 5.1600 0.99 2738 148 0.1940 0.2029 REMARK 3 3 5.1600 - 4.5100 1.00 2725 136 0.1727 0.1898 REMARK 3 4 4.5100 - 4.1000 1.00 2689 162 0.1705 0.2244 REMARK 3 5 4.1000 - 3.8100 0.99 2676 128 0.1923 0.2655 REMARK 3 6 3.8100 - 3.5800 0.99 2687 133 0.2219 0.2509 REMARK 3 7 3.5800 - 3.4000 0.99 2638 146 0.2300 0.2869 REMARK 3 8 3.4000 - 3.2600 0.98 2626 154 0.2320 0.2641 REMARK 3 9 3.2600 - 3.1300 0.97 2602 142 0.2445 0.3130 REMARK 3 10 3.1300 - 3.0200 0.97 2580 142 0.2520 0.2622 REMARK 3 11 3.0200 - 2.9300 0.96 2564 136 0.2573 0.3076 REMARK 3 12 2.9300 - 2.8400 0.95 2537 146 0.2670 0.3509 REMARK 3 13 2.8400 - 2.7700 0.94 2506 127 0.2591 0.3466 REMARK 3 14 2.7700 - 2.7000 0.94 2530 106 0.2689 0.3281 REMARK 3 15 2.7000 - 2.6400 0.93 2441 149 0.2669 0.2888 REMARK 3 16 2.6400 - 2.5800 0.92 2437 155 0.2860 0.3268 REMARK 3 17 2.5800 - 2.5300 0.92 2438 129 0.2997 0.3281 REMARK 3 18 2.5300 - 2.4800 0.90 2383 125 0.3200 0.3798 REMARK 3 19 2.4800 - 2.4400 0.91 2402 127 0.3445 0.3553 REMARK 3 20 2.4400 - 2.4000 0.90 2362 136 0.3827 0.4665 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.370 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.003 7521 REMARK 3 ANGLE : 0.644 10208 REMARK 3 CHIRALITY : 0.045 1132 REMARK 3 PLANARITY : 0.005 1311 REMARK 3 DIHEDRAL : 17.796 2705 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 9DS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288698. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-NOV-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54268 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 39.430 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 19.00 REMARK 200 R MERGE (I) : 0.18000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.10000 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: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, PH 6.4, 16% REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 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 0.00000 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 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 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 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 64.73300 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 37.37361 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 147.92300 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 64.73300 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 37.37361 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 147.92300 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 64.73300 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 37.37361 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 147.92300 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 64.73300 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 37.37361 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 147.92300 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 64.73300 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 37.37361 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 147.92300 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 64.73300 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 37.37361 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 147.92300 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 74.74723 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 295.84600 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 74.74723 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 295.84600 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 74.74723 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 295.84600 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 74.74723 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 295.84600 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 74.74723 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 295.84600 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 74.74723 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 295.84600 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, 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 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, C REMARK 350 BIOMT1 2 -0.500000 -0.866000 0.000000 -64.73000 REMARK 350 BIOMT2 2 0.866000 -0.500000 0.000000 -112.10000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, C REMARK 350 BIOMT1 3 -0.500000 0.866000 0.000000 64.73000 REMARK 350 BIOMT2 3 -0.866000 -0.500000 0.000000 -122.10000 REMARK 350 BIOMT3 3 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 HOH B 215 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 238 LIES ON A SPECIAL POSITION. 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 CYS L 215 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 OD1 ASP A 190 O HOH A 501 2.19 REMARK 500 REMARK 500 REMARK: NULL 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 514 O HOH B 205 3545 2.05 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 11 140.82 80.03 REMARK 500 ASN A 94 -63.90 -102.85 REMARK 500 GLN A 196 -16.04 70.63 REMARK 500 ASP A 276 51.99 -91.92 REMARK 500 THR A 279 155.24 62.97 REMARK 500 LYS B 127 -124.81 56.14 REMARK 500 PHE H 123 -66.35 -98.02 REMARK 500 ASN H 124 -61.53 127.96 REMARK 500 SER H 171 134.69 -171.33 REMARK 500 SER H 197 48.45 -82.87 REMARK 500 SER L 30 -127.77 56.25 REMARK 500 ALA L 51 -10.52 72.79 REMARK 500 SER L 52 -14.45 -140.64 REMARK 500 REMARK 500 REMARK: NULL DBREF1 9DS1 A 11 325 UNP A0A5B9ZSV0_9INFA DBREF2 9DS1 A A0A5B9ZSV0 18 340 DBREF1 9DS1 B 1 174 UNP A0A6J3XB93_9INFA DBREF2 9DS1 B A0A6J3XB93 345 518 DBREF 9DS1 H 1 226 PDB 9DS1 9DS1 1 226 DBREF 9DS1 L 1 215 PDB 9DS1 9DS1 1 215 SEQADV 9DS1 ALA A 7 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS1 ASP A 8 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS1 PRO A 9 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS1 GLY A 10 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS1 SER A 186 UNP A0A5B9ZSV UNK 200 CONFLICT SEQADV 9DS1 GLY A 206 UNP A0A5B9ZSV SER 220 CONFLICT SEQADV 9DS1 SER B 175 UNP A0A6J3XB9 EXPRESSION TAG SEQRES 1 A 327 ALA ASP PRO GLY ASP THR LEU CYS ILE GLY TYR HIS ALA SEQRES 2 A 327 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS SEQRES 3 A 327 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP SEQRES 4 A 327 LYS HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA SEQRES 5 A 327 PRO LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE SEQRES 6 A 327 LEU GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SEQRES 7 A 327 SER TRP SER TYR ILE VAL GLU THR PRO SER SER ASP ASN SEQRES 8 A 327 GLY THR CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU SEQRES 9 A 327 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG SEQRES 10 A 327 PHE GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS SEQRES 11 A 327 ASP SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA SEQRES 12 A 327 GLY ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL SEQRES 13 A 327 LYS LYS GLY ASN SER TYR PRO LYS LEU SER LYS SER TYR SEQRES 14 A 327 ILE ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY SEQRES 15 A 327 ILE HIS HIS PRO SER THR SER ALA ASP GLN GLN SER LEU SEQRES 16 A 327 TYR GLN ASN ALA ASP THR TYR VAL PHE VAL GLY GLY SER SEQRES 17 A 327 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE ARG SEQRES 18 A 327 PRO LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR SEQRES 19 A 327 TRP THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU SEQRES 20 A 327 ALA THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE ALA SEQRES 21 A 327 MET GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP SEQRES 22 A 327 THR PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO SEQRES 23 A 327 LYS GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE SEQRES 24 A 327 HIS PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SEQRES 25 A 327 SER THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN ILE SEQRES 26 A 327 PRO SER SEQRES 1 B 175 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 B 175 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 B 175 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 B 175 SER THR GLN ASN ALA ILE ASP GLY ILE THR ASN LYS VAL SEQRES 5 B 175 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 B 175 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 B 175 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 B 175 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 B 175 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 B 175 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 B 175 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 B 175 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 B 175 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 B 175 ARG GLU GLU ILE ASP SER SEQRES 1 H 226 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 226 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 H 226 PHE THR PHE SER LYS TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 H 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 H 226 GLY SER GLY ILE SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 226 GLY ARG PHE THR ILE SER ARG ASP THR SER LYS ASN MET SEQRES 7 H 226 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 226 ALA ILE TYR TYR CYS ALA LYS ASP ALA ILE SER GLY GLN SEQRES 9 H 226 ILE TRP LEU GLN GLY THR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 H 226 THR LEU VAL THR VAL PHE ASN GLN ILE LYS GLY PRO SER SEQRES 11 H 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 226 GLU PRO LYS SER CYS SEQRES 1 L 215 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 215 THR ARG ALA THR GLY ILE PRO PRO ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR GLU PHE SER LEU THR ILE SER SER LEU SEQRES 7 L 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 215 ASN ASN TRP PRO PRO ILE 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 NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET NAG A 401 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 3(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 FORMUL 7 HOH *129(H2 O) HELIX 1 AA1 LYS A 53 VAL A 56 5 5 HELIX 2 AA2 ASN A 65 GLY A 72 1 8 HELIX 3 AA3 ASP A 104 SER A 113 1 10 HELIX 4 AA4 THR A 187 GLN A 196 1 10 HELIX 5 AA5 ASP B 37 LYS B 58 1 22 HELIX 6 AA6 GLU B 74 LYS B 127 1 54 HELIX 7 AA7 ASP B 145 ASN B 154 1 10 HELIX 8 AA8 ASP B 158 SER B 175 1 18 HELIX 9 AA9 THR H 28 TYR H 32 5 5 HELIX 10 AB1 ASP H 62 LYS H 65 5 4 HELIX 11 AB2 THR H 74 LYS H 76 5 3 HELIX 12 AB3 ARG H 87 THR H 91 5 5 HELIX 13 AB4 GLN H 104 GLN H 108 5 5 HELIX 14 AB5 SER H 137 THR H 141 5 5 HELIX 15 AB6 HIS H 210 ASN H 214 5 5 HELIX 16 AB7 GLN L 79 PHE L 83 5 5 HELIX 17 AB8 SER L 122 GLY L 129 1 8 HELIX 18 AB9 LYS L 184 GLU L 188 1 5 SHEET 1 AA1 5 GLY B 31 ALA B 36 0 SHEET 2 AA1 5 TYR B 22 ASN B 28 -1 N TYR B 24 O ALA B 35 SHEET 3 AA1 5 THR A 12 TYR A 17 -1 N CYS A 14 O HIS B 25 SHEET 4 AA1 5 CYS B 137 PHE B 140 -1 O PHE B 138 N LEU A 13 SHEET 5 AA1 5 ALA B 130 GLU B 132 -1 N LYS B 131 O GLU B 139 SHEET 1 AA2 2 THR A 25 VAL A 26 0 SHEET 2 AA2 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AA3 2 SER A 39 ASN A 41 0 SHEET 2 AA3 2 ARG A 315 ALA A 317 -1 O LEU A 316 N VAL A 40 SHEET 1 AA4 3 LEU A 43 GLU A 44 0 SHEET 2 AA4 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AA4 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SHEET 1 AA5 3 LEU A 59 HIS A 60 0 SHEET 2 AA5 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AA5 3 ILE A 267 ILE A 269 1 O ILE A 268 N ILE A 87 SHEET 1 AA6 6 SER A 83 TRP A 84 0 SHEET 2 AA6 6 VAL A 115 GLU A 119 -1 O PHE A 116B N SER A 83 SHEET 3 AA6 6 TYR A 256 ARG A 262 -1 O ALA A 259 N GLU A 116C SHEET 4 AA6 6 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 5 AA6 6 LEU A 251 PRO A 254 -1 O VAL A 252 N GLY A 181 SHEET 6 AA6 6 LEU A 151 TRP A 153 -1 N ILE A 152 O VAL A 253 SHEET 1 AA7 5 SER A 83 TRP A 84 0 SHEET 2 AA7 5 VAL A 115 GLU A 119 -1 O PHE A 116B N SER A 83 SHEET 3 AA7 5 TYR A 256 ARG A 262 -1 O ALA A 259 N GLU A 116C SHEET 4 AA7 5 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 5 AA7 5 ARG A 229 VAL A 237 -1 O ARG A 229 N HIS A 184 SHEET 1 AA8 2 THR A 136 HIS A 141 0 SHEET 2 AA8 2 ALA A 144 SER A 146 -1 O ALA A 144 N HIS A 141 SHEET 1 AA9 4 LEU A 164 ILE A 169 0 SHEET 2 AA9 4 LYS A 242 ALA A 247 -1 O ALA A 247 N LEU A 164 SHEET 3 AA9 4 VAL A 202 GLY A 205 -1 N PHE A 203 O GLU A 246 SHEET 4 AA9 4 SER A 210 PHE A 213 -1 O PHE A 213 N VAL A 202 SHEET 1 AB1 3 CYS A 281 GLN A 282 0 SHEET 2 AB1 3 ILE A 302 GLY A 303 -1 O ILE A 302 N GLN A 282 SHEET 3 AB1 3 THR B 64 ALA B 65 -1 O THR B 64 N GLY A 303 SHEET 1 AB2 4 GLN H 3 SER H 7 0 SHEET 2 AB2 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB2 4 MET H 78 MET H 83 -1 O LEU H 79 N CYS H 22 SHEET 4 AB2 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AB3 6 LEU H 11 VAL H 12 0 SHEET 2 AB3 6 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AB3 6 ALA H 92 ASP H 99 -1 N TYR H 94 O THR H 118 SHEET 4 AB3 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB3 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AB3 6 THR H 58 TYR H 60 -1 O TYR H 59 N HIS H 50 SHEET 1 AB4 4 LEU H 11 VAL H 12 0 SHEET 2 AB4 4 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AB4 4 ALA H 92 ASP H 99 -1 N TYR H 94 O THR H 118 SHEET 4 AB4 4 PHE H 111 TRP H 114 -1 O TYR H 113 N LYS H 98 SHEET 1 AB5 4 SER H 130 LEU H 134 0 SHEET 2 AB5 4 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AB5 4 TYR H 186 PRO H 195 -1 O VAL H 194 N ALA H 146 SHEET 4 AB5 4 VAL H 173 THR H 175 -1 N HIS H 174 O VAL H 191 SHEET 1 AB6 4 SER H 130 LEU H 134 0 SHEET 2 AB6 4 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AB6 4 TYR H 186 PRO H 195 -1 O VAL H 194 N ALA H 146 SHEET 4 AB6 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187 SHEET 1 AB7 3 THR H 161 TRP H 164 0 SHEET 2 AB7 3 TYR H 204 ASN H 209 -1 O ASN H 207 N SER H 163 SHEET 3 AB7 3 ASP H 218 VAL H 221 -1 O LYS H 219 N CYS H 206 SHEET 1 AB8 4 MET L 4 THR L 5 0 SHEET 2 AB8 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB8 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AB8 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB9 6 THR L 10 VAL L 13 0 SHEET 2 AB9 6 THR L 103 ILE L 107 1 O ARG L 104 N LEU L 11 SHEET 3 AB9 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 103 SHEET 4 AB9 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AB9 6 ARG L 45 TYR L 49 -1 O ARG L 45 N GLN L 37 SHEET 6 AB9 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AC1 4 THR L 10 VAL L 13 0 SHEET 2 AC1 4 THR L 103 ILE L 107 1 O ARG L 104 N LEU L 11 SHEET 3 AC1 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 103 SHEET 4 AC1 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 90 SHEET 1 AC2 4 SER L 115 PHE L 119 0 SHEET 2 AC2 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AC2 4 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AC2 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AC3 3 LYS L 146 VAL L 151 0 SHEET 2 AC3 3 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 3 AC3 3 VAL L 206 ASN L 211 -1 O LYS L 208 N CYS L 195 SSBOND 1 CYS A 14 CYS B 137 1555 1555 2.04 SSBOND 2 CYS A 52 CYS A 277 1555 1555 2.04 SSBOND 3 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 4 CYS A 97 CYS A 139 1555 1555 2.07 SSBOND 5 CYS A 281 CYS A 305 1555 1555 2.04 SSBOND 6 CYS B 144 CYS B 148 1555 1555 2.04 SSBOND 7 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 8 CYS H 150 CYS H 206 1555 1555 2.03 SSBOND 9 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 10 CYS L 135 CYS L 195 1555 1555 2.03 LINK ND2 ASN A 94 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN A 278 C1 NAG A 401 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 CISPEP 1 PHE H 156 PRO H 157 0 -4.24 CISPEP 2 GLU H 158 PRO H 159 0 -0.09 CISPEP 3 SER L 7 PRO L 8 0 1.73 CISPEP 4 TRP L 94 PRO L 95 0 1.99 CISPEP 5 PRO L 95 PRO L 96 0 1.78 CISPEP 6 TYR L 141 PRO L 142 0 2.18 CRYST1 129.466 129.466 443.769 90.00 90.00 120.00 H 3 2 18 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 0.007724 0.004459 0.000000 0.00000 SCALE2 0.000000 0.008919 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002253 0.00000