HEADER VIRAL PROTEIN/IMMUNE SYSTEM 12-APR-24 8Z2E TITLE CRYSTAL STRUCTURE OF NANOBODY TNB04-1 WITH ANTIBODY 1F11 FAB AND SARS- TITLE 2 COV-2 RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: TNB04-1; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SPIKE PROTEIN S1; COMPND 7 CHAIN: E; COMPND 8 FRAGMENT: RECEPTOR-BINDING DOMAIN (RBD); COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 1F11-H; COMPND 12 CHAIN: H; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: 1F11-L; COMPND 16 CHAIN: L; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 3 ORGANISM_TAXID: 30538; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 9 2; SOURCE 10 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 11 ORGANISM_TAXID: 2697049; SOURCE 12 GENE: S, 2; SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SARS-COV-2, NEUTRALIZING NANOBODY, ANTIBODY, CONSERVED EPITOPE, VIRAL KEYWDS 2 PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR X.Q.WANG,L.Q.ZHANG,J.CHEN,H.D.DONG REVDAT 1 23-APR-25 8Z2E 0 JRNL AUTH X.Q.WANG,L.Q.ZHANG,J.CHEN,H.D.DONG JRNL TITL CRYSTAL STRUCTURE OF NANOBODY TNB04-1 WITH ANTIBODY 1F11 FAB JRNL TITL 2 AND SARS-COV-2 RBD JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.18.2_3874: ???) 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.36 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 45366 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.195 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.380 REMARK 3 FREE R VALUE TEST SET COUNT : 1986 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 73.3600 - 5.5400 0.99 3281 154 0.1920 0.2264 REMARK 3 2 5.5400 - 4.4000 1.00 3184 143 0.1466 0.1813 REMARK 3 3 4.4000 - 3.8400 1.00 3145 148 0.1557 0.1775 REMARK 3 4 3.8400 - 3.4900 1.00 3117 141 0.1833 0.2119 REMARK 3 5 3.4900 - 3.2400 0.94 2937 129 0.2027 0.2463 REMARK 3 6 3.2400 - 3.0500 1.00 3117 139 0.2150 0.2814 REMARK 3 7 3.0500 - 2.9000 1.00 3078 142 0.2185 0.2321 REMARK 3 8 2.9000 - 2.7700 1.00 3099 145 0.2293 0.2788 REMARK 3 9 2.7700 - 2.6600 1.00 3067 138 0.2261 0.2674 REMARK 3 10 2.6600 - 2.5700 1.00 3085 139 0.2314 0.2804 REMARK 3 11 2.5700 - 2.4900 1.00 3062 141 0.2385 0.3156 REMARK 3 12 2.4900 - 2.4200 1.00 3067 137 0.2482 0.2932 REMARK 3 13 2.4200 - 2.3600 1.00 3063 148 0.2591 0.3166 REMARK 3 14 2.3600 - 2.3000 1.00 3078 142 0.2738 0.3438 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) : 0.290 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.730 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 : 0.009 5787 REMARK 3 ANGLE : 1.091 7866 REMARK 3 CHIRALITY : 0.060 874 REMARK 3 PLANARITY : 0.008 1016 REMARK 3 DIHEDRAL : 9.175 814 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 8Z2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 15-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046556. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-SEP-23 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 : SSRF REMARK 200 BEAMLINE : BL18U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45733 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 73.360 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 13.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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 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: 7X2L,7CDI REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM PHOSPHATE DIBASIC 20% REMARK 280 W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 44.07100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.67250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.87350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.67250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.07100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.87350 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, H, L, A 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 ARG E 319 REMARK 465 VAL E 320 REMARK 465 GLN E 321 REMARK 465 PRO E 322 REMARK 465 THR E 323 REMARK 465 GLU E 324 REMARK 465 SER E 325 REMARK 465 ILE E 326 REMARK 465 VAL E 327 REMARK 465 ARG E 328 REMARK 465 PHE E 329 REMARK 465 PRO E 330 REMARK 465 ASN E 331 REMARK 465 ILE E 332 REMARK 465 LYS E 528 REMARK 465 LYS E 529 REMARK 465 HIS E 530 REMARK 465 HIS E 531 REMARK 465 HIS E 532 REMARK 465 HIS E 533 REMARK 465 HIS E 534 REMARK 465 HIS E 535 REMARK 465 GLU H 1 REMARK 465 SER H 132 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 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 O HOH H 398 O HOH H 411 1.91 REMARK 500 O HOH H 331 O HOH H 400 1.94 REMARK 500 O HOH H 357 O HOH H 396 2.00 REMARK 500 O HOH E 640 O HOH E 652 2.14 REMARK 500 O HOH H 389 O HOH H 403 2.14 REMARK 500 O HOH E 660 O HOH E 665 2.18 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 PRO E 337 36.60 -87.52 REMARK 500 ALA E 352 49.97 -108.04 REMARK 500 ALA E 372 -128.56 57.40 REMARK 500 SER E 373 -22.41 74.24 REMARK 500 ASN E 422 -51.88 -129.07 REMARK 500 ASP E 428 33.75 -94.49 REMARK 500 LEU E 518 -94.40 -79.55 REMARK 500 HIS E 519 -128.36 -133.78 REMARK 500 VAL H 100 -84.99 62.49 REMARK 500 ASP H 148 60.43 62.94 REMARK 500 PRO H 151 -169.77 -77.44 REMARK 500 SER L 26 6.55 -69.12 REMARK 500 GLN L 27 149.63 -175.07 REMARK 500 ALA L 52 -31.52 71.63 REMARK 500 ALA L 85 -172.33 -178.28 REMARK 500 ASN L 138 73.60 56.80 REMARK 500 REMARK 500 REMARK: NULL DBREF 8Z2E B 1 116 PDB 8Z2E 8Z2E 1 116 DBREF 8Z2E E 319 529 UNP P0DTC2 SPIKE_SARS2 319 529 DBREF 8Z2E H 1 217 PDB 8Z2E 8Z2E 1 217 DBREF 8Z2E L 1 214 PDB 8Z2E 8Z2E 1 214 SEQADV 8Z2E HIS E 530 UNP P0DTC2 EXPRESSION TAG SEQADV 8Z2E HIS E 531 UNP P0DTC2 EXPRESSION TAG SEQADV 8Z2E HIS E 532 UNP P0DTC2 EXPRESSION TAG SEQADV 8Z2E HIS E 533 UNP P0DTC2 EXPRESSION TAG SEQADV 8Z2E HIS E 534 UNP P0DTC2 EXPRESSION TAG SEQADV 8Z2E HIS E 535 UNP P0DTC2 EXPRESSION TAG SEQRES 1 B 116 GLU VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 116 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 116 SER ILE SER THR LEU ASN VAL MET GLY TRP TYR ARG GLN SEQRES 4 B 116 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ARG ILE THR SEQRES 5 B 116 LEU ASP GLY ARG PRO GLU TYR ALA ASP SER VAL LYS GLY SEQRES 6 B 116 ARG PHE THR ILE THR LYS ASP GLY ALA GLN SER THR LEU SEQRES 7 B 116 TYR LEU GLN MET ASN ASN LEU LYS PRO GLU ASP THR ALA SEQRES 8 B 116 VAL TYR PHE CYS LYS LEU GLU ASN GLY GLY PHE PHE TYR SEQRES 9 B 116 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 E 217 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN SEQRES 2 E 217 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA SEQRES 3 E 217 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 4 E 217 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SEQRES 5 E 217 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER SEQRES 6 E 217 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR SEQRES 7 E 217 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN SEQRES 8 E 217 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN SEQRES 9 E 217 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 10 E 217 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN SEQRES 11 E 217 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU SEQRES 12 E 217 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 13 E 217 ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN SEQRES 14 E 217 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR SEQRES 15 E 217 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 16 E 217 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 17 E 217 PRO LYS LYS HIS HIS HIS HIS HIS HIS SEQRES 1 H 217 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 217 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 217 ILE THR VAL SER SER ASN TYR MET ASN TRP VAL ARG GLN SEQRES 4 H 217 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE TYR SEQRES 5 H 217 SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 H 217 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU SEQRES 7 H 217 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 217 VAL TYR HIS CYS ALA ARG ASP LEU VAL VAL TYR GLY MET SEQRES 9 H 217 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 10 H 217 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 H 217 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 H 217 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 H 217 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 H 217 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 H 217 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 H 217 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 H 217 THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 1 L 214 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 214 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 214 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 214 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 214 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 214 TYR GLY SER SER PRO THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET NAG A 1 14 HET NAG A 2 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 5 NAG 2(C8 H15 N O6) FORMUL 6 HOH *300(H2 O) HELIX 1 AA1 ASP B 61 LYS B 64 5 4 HELIX 2 AA2 LYS B 86 THR B 90 5 5 HELIX 3 AA3 PHE E 338 ASN E 343 1 6 HELIX 4 AA4 SER E 349 TRP E 353 5 5 HELIX 5 AA5 ASP E 364 ASN E 370 1 7 HELIX 6 AA6 SER E 383 ASP E 389 5 7 HELIX 7 AA7 ASP E 405 ILE E 410 5 6 HELIX 8 AA8 GLY E 416 ASN E 422 1 7 HELIX 9 AA9 SER E 438 SER E 443 1 6 HELIX 10 AB1 GLY E 502 TYR E 505 5 4 HELIX 11 AB2 THR H 28 ASN H 32 5 5 HELIX 12 AB3 ASN H 73 LYS H 75 5 3 HELIX 13 AB4 ARG H 86 THR H 90 5 5 HELIX 14 AB5 SER H 160 ALA H 162 5 3 HELIX 15 AB6 SER H 191 THR H 195 5 5 HELIX 16 AB7 LYS H 205 ASN H 208 5 4 HELIX 17 AB8 SER L 30 LEU L 34 5 5 HELIX 18 AB9 GLU L 80 PHE L 84 5 5 HELIX 19 AC1 SER L 121 SER L 127 1 7 HELIX 20 AC2 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 4 VAL B 2 SER B 7 0 SHEET 2 AA1 4 LEU B 18 GLY B 26 -1 O ALA B 23 N GLN B 5 SHEET 3 AA1 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA1 4 PHE B 67 ASP B 72 -1 N THR B 68 O GLN B 81 SHEET 1 AA2 6 GLY B 10 VAL B 12 0 SHEET 2 AA2 6 THR B 110 VAL B 114 1 O THR B 113 N VAL B 12 SHEET 3 AA2 6 ALA B 91 ASN B 99 -1 N TYR B 93 O THR B 110 SHEET 4 AA2 6 ASN B 32 GLN B 39 -1 N TYR B 37 O PHE B 94 SHEET 5 AA2 6 GLU B 46 ILE B 51 -1 O ALA B 49 N TRP B 36 SHEET 6 AA2 6 PRO B 57 TYR B 59 -1 O GLU B 58 N ARG B 50 SHEET 1 AA3 4 GLY B 10 VAL B 12 0 SHEET 2 AA3 4 THR B 110 VAL B 114 1 O THR B 113 N VAL B 12 SHEET 3 AA3 4 ALA B 91 ASN B 99 -1 N TYR B 93 O THR B 110 SHEET 4 AA3 4 PHE B 103 TRP B 106 -1 O PHE B 103 N ASN B 99 SHEET 1 AA4 5 ASN E 354 ILE E 358 0 SHEET 2 AA4 5 ASN E 394 ARG E 403 -1 O VAL E 395 N ILE E 358 SHEET 3 AA4 5 PRO E 507 GLU E 516 -1 O TYR E 508 N ILE E 402 SHEET 4 AA4 5 GLY E 431 ASN E 437 -1 N ILE E 434 O VAL E 511 SHEET 5 AA4 5 THR E 376 TYR E 380 -1 N LYS E 378 O VAL E 433 SHEET 1 AA5 3 CYS E 361 VAL E 362 0 SHEET 2 AA5 3 VAL E 524 CYS E 525 1 O CYS E 525 N CYS E 361 SHEET 3 AA5 3 CYS E 391 PHE E 392 -1 N PHE E 392 O VAL E 524 SHEET 1 AA6 2 LEU E 452 ARG E 454 0 SHEET 2 AA6 2 LEU E 492 SER E 494 -1 O GLN E 493 N TYR E 453 SHEET 1 AA7 2 TYR E 473 GLN E 474 0 SHEET 2 AA7 2 CYS E 488 TYR E 489 -1 O TYR E 489 N TYR E 473 SHEET 1 AA8 4 GLN H 3 SER H 7 0 SHEET 2 AA8 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA8 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA8 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA9 6 LEU H 11 VAL H 12 0 SHEET 2 AA9 6 THR H 111 VAL H 115 1 O THR H 114 N VAL H 12 SHEET 3 AA9 6 ALA H 91 ASP H 98 -1 N TYR H 93 O THR H 111 SHEET 4 AA9 6 TYR H 33 GLN H 39 -1 N VAL H 37 O HIS H 94 SHEET 5 AA9 6 GLU H 46 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA9 6 THR H 57 TYR H 59 -1 O TYR H 58 N LEU H 50 SHEET 1 AB1 4 LEU H 11 VAL H 12 0 SHEET 2 AB1 4 THR H 111 VAL H 115 1 O THR H 114 N VAL H 12 SHEET 3 AB1 4 ALA H 91 ASP H 98 -1 N TYR H 93 O THR H 111 SHEET 4 AB1 4 MET H 104 TRP H 107 -1 O VAL H 106 N ARG H 97 SHEET 1 AB2 4 SER H 124 LEU H 128 0 SHEET 2 AB2 4 THR H 139 TYR H 149 -1 O GLY H 143 N LEU H 128 SHEET 3 AB2 4 TYR H 180 PRO H 189 -1 O LEU H 182 N VAL H 146 SHEET 4 AB2 4 VAL H 167 THR H 169 -1 N HIS H 168 O VAL H 185 SHEET 1 AB3 4 SER H 124 LEU H 128 0 SHEET 2 AB3 4 THR H 139 TYR H 149 -1 O GLY H 143 N LEU H 128 SHEET 3 AB3 4 TYR H 180 PRO H 189 -1 O LEU H 182 N VAL H 146 SHEET 4 AB3 4 VAL H 173 LEU H 174 -1 N VAL H 173 O SER H 181 SHEET 1 AB4 3 THR H 155 TRP H 158 0 SHEET 2 AB4 3 TYR H 198 HIS H 204 -1 O ASN H 201 N SER H 157 SHEET 3 AB4 3 THR H 209 VAL H 215 -1 O VAL H 211 N VAL H 202 SHEET 1 AB5 4 LEU L 4 SER L 7 0 SHEET 2 AB5 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB5 4 ASP L 71 ILE L 76 -1 O LEU L 74 N LEU L 21 SHEET 4 AB5 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AB6 6 THR L 10 LEU L 13 0 SHEET 2 AB6 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB6 6 VAL L 86 TYR L 92 -1 N TYR L 87 O THR L 102 SHEET 4 AB6 6 ALA L 35 GLN L 39 -1 N GLN L 39 O VAL L 86 SHEET 5 AB6 6 ARG L 46 TYR L 50 -1 O LEU L 48 N TRP L 36 SHEET 6 AB6 6 SER L 54 ARG L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AB7 4 THR L 10 LEU L 13 0 SHEET 2 AB7 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB7 4 VAL L 86 TYR L 92 -1 N TYR L 87 O THR L 102 SHEET 4 AB7 4 PRO L 96 PHE L 98 -1 O THR L 97 N GLN L 91 SHEET 1 AB8 4 SER L 114 PHE L 118 0 SHEET 2 AB8 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB8 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB8 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB9 4 ALA L 153 GLN L 155 0 SHEET 2 AB9 4 LYS L 145 VAL L 150 -1 N TRP L 148 O GLN L 155 SHEET 3 AB9 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB9 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS B 22 CYS B 95 1555 1555 2.04 SSBOND 2 CYS E 336 CYS E 361 1555 1555 2.01 SSBOND 3 CYS E 379 CYS E 432 1555 1555 2.07 SSBOND 4 CYS E 391 CYS E 525 1555 1555 2.05 SSBOND 5 CYS E 480 CYS E 488 1555 1555 2.07 SSBOND 6 CYS H 22 CYS H 95 1555 1555 2.05 SSBOND 7 CYS H 144 CYS H 200 1555 1555 2.06 SSBOND 8 CYS L 23 CYS L 89 1555 1555 2.08 SSBOND 9 CYS L 134 CYS L 194 1555 1555 2.02 LINK ND2 ASN E 343 C1 NAG A 1 1555 1555 1.45 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.43 CISPEP 1 ALA E 520 PRO E 521 0 -15.53 CISPEP 2 PHE H 150 PRO H 151 0 -13.45 CISPEP 3 GLU H 152 PRO H 153 0 5.14 CISPEP 4 SER L 7 PRO L 8 0 -8.60 CISPEP 5 TYR L 140 PRO L 141 0 -1.46 CRYST1 88.142 89.747 127.345 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011345 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011142 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007853 0.00000