HEADER ANTIVIRAL PROTEIN 11-JAN-25 9LH2 TITLE CRYSTAL STRUCTURE OF SARS-COV-2 SPIKE RECEPTOR-BINDING DOMAIN (DELTA) TITLE 2 IN COMPLEX WITH PH-DEPENDENT NANOBODY MNB-11. COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A, C; COMPND 4 FRAGMENT: RECEPTOR-BINDING DOMAIN (RBD); COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MNB-11; COMPND 8 CHAIN: B, D; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 11 ORGANISM_TAXID: 30538; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COMPLEX, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR X.D.ZHANG,G.W.LU REVDAT 1 14-JAN-26 9LH2 0 JRNL AUTH X.D.ZHANG,Z.M.CHEN,S.LIN,F.L.YANG,L.Y.GUO,J.YANG,L.L.WANG, JRNL AUTH 2 X.YUAN,P.L.XU,B.HE,Y.CAO,J.LI,Q.ZHAO,J.LI,L.YANG,W.WANG, JRNL AUTH 3 Z.L.WANG,J.L.YANG,J.Y.YANG,G.B.SHEN,X.W.WEI,G.W.LU JRNL TITL MODIFICATION OF A SARS-COV-2 SPIKE-RBD TARGETING NANOBODY JRNL TITL 2 FOR PH-DEPENDENT BINDING AND ITS CHROMATOGRAPHIC ENGINEERING JRNL TITL 3 FOR PURIFICATION OF WT AND VARIANT S-RBDS WITH MILD ELUTION JRNL TITL 4 CONDITIONS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) 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) : 49.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 3 NUMBER OF REFLECTIONS : 44837 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.209 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2228 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 2.3830 - 2.3000 0.00 0 0 0.0000 0.0000 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) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL 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 9LH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 18-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1300055581. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-APR-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 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 PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45744 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 49.900 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 13.20 REMARK 200 R MERGE (I) : 0.13800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.0000 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) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 13.00 REMARK 200 R MERGE FOR SHELL (I) : 0.80000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.500 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: 8CYJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.09M NPS, 0.1M TRIS (BASE), 0.1M REMARK 280 BICINE, PH 8.5, 20% V/V PEG 500* MME, 10 % W/V PEG 20000, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 146.30750 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.06750 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.06750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.15375 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.06750 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.06750 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 219.46125 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.06750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.06750 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 73.15375 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.06750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.06750 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 219.46125 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 146.30750 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 VAL A 320 REMARK 465 GLN A 321 REMARK 465 PRO A 322 REMARK 465 THR A 323 REMARK 465 GLU A 324 REMARK 465 SER A 325 REMARK 465 ILE A 326 REMARK 465 VAL A 327 REMARK 465 ARG A 328 REMARK 465 PHE A 329 REMARK 465 PRO A 330 REMARK 465 ASN A 331 REMARK 465 ILE A 332 REMARK 465 THR A 333 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 ASN A 532 REMARK 465 LEU A 533 REMARK 465 VAL A 534 REMARK 465 LYS A 535 REMARK 465 ASN A 536 REMARK 465 LYS A 537 REMARK 465 HIS B 133 REMARK 465 HIS B 134 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 HIS D 133 REMARK 465 HIS D 134 REMARK 465 VAL C 320 REMARK 465 GLN C 321 REMARK 465 PRO C 322 REMARK 465 THR C 323 REMARK 465 GLU C 324 REMARK 465 SER C 325 REMARK 465 ILE C 326 REMARK 465 VAL C 327 REMARK 465 ARG C 328 REMARK 465 PHE C 329 REMARK 465 PRO C 330 REMARK 465 ASN C 331 REMARK 465 ILE C 332 REMARK 465 THR C 333 REMARK 465 LYS C 528 REMARK 465 LYS C 529 REMARK 465 SER C 530 REMARK 465 THR C 531 REMARK 465 ASN C 532 REMARK 465 LEU C 533 REMARK 465 VAL C 534 REMARK 465 LYS C 535 REMARK 465 ASN C 536 REMARK 465 LYS C 537 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 D 245 O HOH D 246 1.82 REMARK 500 O HOH C 763 O HOH C 769 1.96 REMARK 500 O HOH D 216 O HOH D 248 1.97 REMARK 500 O HOH D 247 O HOH D 258 2.09 REMARK 500 O HOH D 250 O HOH D 256 2.09 REMARK 500 O HOH A 774 O HOH A 790 2.16 REMARK 500 O HOH A 791 O HOH A 805 2.17 REMARK 500 O HOH D 206 O HOH D 244 2.17 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 804 O HOH D 261 4444 2.04 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 CYS B 96 CA - CB - SG ANGL. DEV. = 11.2 DEGREES REMARK 500 CYS D 96 CA - CB - SG ANGL. DEV. = 12.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PHE A 377 85.10 -152.68 REMARK 500 ASN A 422 -57.48 -126.61 REMARK 500 ASP A 428 37.60 -94.44 REMARK 500 ASN B 108 143.25 -170.24 REMARK 500 PHE C 377 85.90 -150.36 REMARK 500 LYS C 386 35.62 -83.93 REMARK 500 ASN C 388 5.10 -69.87 REMARK 500 ASN C 422 -52.08 -129.21 REMARK 500 REMARK 500 REMARK: NULL DBREF 9LH2 A 320 537 UNP P0DTC2 SPIKE_SARS2 320 537 DBREF 9LH2 B 1 134 PDB 9LH2 9LH2 1 134 DBREF 9LH2 D 1 134 PDB 9LH2 9LH2 1 134 DBREF 9LH2 C 320 537 UNP P0DTC2 SPIKE_SARS2 320 537 SEQADV 9LH2 ARG A 452 UNP P0DTC2 LEU 452 VARIANT SEQADV 9LH2 LYS A 478 UNP P0DTC2 THR 478 VARIANT SEQADV 9LH2 ARG C 452 UNP P0DTC2 LEU 452 VARIANT SEQADV 9LH2 LYS C 478 UNP P0DTC2 THR 478 VARIANT SEQRES 1 A 218 VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN ILE SEQRES 2 A 218 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 3 A 218 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 4 A 218 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 5 A 218 ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO SEQRES 6 A 218 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 7 A 218 ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE SEQRES 8 A 218 ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR SEQRES 9 A 218 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 10 A 218 ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR SEQRES 11 A 218 ASN TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU LYS SEQRES 12 A 218 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 13 A 218 GLY SER LYS PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS SEQRES 14 A 218 TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN SEQRES 15 A 218 GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 16 A 218 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 17 A 218 LYS LYS SER THR ASN LEU VAL LYS ASN LYS SEQRES 1 B 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 134 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 134 PHE THR PHE ASN ARG TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 B 134 ALA PRO GLY LYS GLY ARG GLU TRP VAL SER GLY ILE TYR SEQRES 5 B 134 SER ASP GLY SER GLU THR TYR TYR THR GLU SER VAL LYS SEQRES 6 B 134 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN MET SEQRES 7 B 134 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 B 134 ALA LEU TYR TYR CYS ALA LYS ASP HIS HIS ALA HIS GLU SEQRES 9 B 134 ASP HIS PHE ASN SER GLY PHE ASP ARG LYS TYR ASP TYR SEQRES 10 B 134 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS HIS SEQRES 11 B 134 HIS HIS HIS HIS SEQRES 1 D 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 134 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 134 PHE THR PHE ASN ARG TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 D 134 ALA PRO GLY LYS GLY ARG GLU TRP VAL SER GLY ILE TYR SEQRES 5 D 134 SER ASP GLY SER GLU THR TYR TYR THR GLU SER VAL LYS SEQRES 6 D 134 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN MET SEQRES 7 D 134 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 D 134 ALA LEU TYR TYR CYS ALA LYS ASP HIS HIS ALA HIS GLU SEQRES 9 D 134 ASP HIS PHE ASN SER GLY PHE ASP ARG LYS TYR ASP TYR SEQRES 10 D 134 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS HIS SEQRES 11 D 134 HIS HIS HIS HIS SEQRES 1 C 218 VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN ILE SEQRES 2 C 218 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 3 C 218 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 4 C 218 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 5 C 218 ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO SEQRES 6 C 218 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 7 C 218 ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE SEQRES 8 C 218 ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR SEQRES 9 C 218 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 10 C 218 ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR SEQRES 11 C 218 ASN TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU LYS SEQRES 12 C 218 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 13 C 218 GLY SER LYS PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS SEQRES 14 C 218 TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN SEQRES 15 C 218 GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 16 C 218 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 17 C 218 LYS LYS SER THR ASN LEU VAL LYS ASN LYS HET NAG A 601 28 HET NAG C 601 28 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 7 HOH *290(H2 O) HELIX 1 AA1 PRO A 337 ASN A 343 1 7 HELIX 2 AA2 SER A 349 TRP A 353 5 5 HELIX 3 AA3 ASP A 364 ASN A 370 1 7 HELIX 4 AA4 SER A 383 ASP A 389 5 7 HELIX 5 AA5 ASP A 405 ILE A 410 5 6 HELIX 6 AA6 GLY A 416 ASN A 422 1 7 HELIX 7 AA7 SER A 438 SER A 443 1 6 HELIX 8 AA8 GLY A 502 TYR A 505 5 4 HELIX 9 AA9 THR B 28 TYR B 32 5 5 HELIX 10 AB1 GLU B 62 LYS B 65 5 4 HELIX 11 AB2 LYS B 87 THR B 91 5 5 HELIX 12 AB3 THR D 28 TYR D 32 5 5 HELIX 13 AB4 GLU D 62 LYS D 65 5 4 HELIX 14 AB5 LYS D 87 THR D 91 5 5 HELIX 15 AB6 PRO C 337 ASN C 343 1 7 HELIX 16 AB7 SER C 349 TRP C 353 5 5 HELIX 17 AB8 TYR C 365 ASN C 370 1 6 HELIX 18 AB9 THR C 385 ASP C 389 5 5 HELIX 19 AC1 ASP C 405 ILE C 410 5 6 HELIX 20 AC2 GLY C 416 ASN C 422 1 7 HELIX 21 AC3 SER C 438 SER C 443 1 6 HELIX 22 AC4 GLY C 502 TYR C 505 5 4 SHEET 1 AA1 5 ASN A 354 ILE A 358 0 SHEET 2 AA1 5 ASN A 394 ARG A 403 -1 O VAL A 395 N ILE A 358 SHEET 3 AA1 5 PRO A 507 GLU A 516 -1 O TYR A 508 N ILE A 402 SHEET 4 AA1 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA1 5 THR A 376 TYR A 380 -1 N TYR A 380 O GLY A 431 SHEET 1 AA2 3 CYS A 361 VAL A 362 0 SHEET 2 AA2 3 VAL A 524 CYS A 525 1 O CYS A 525 N CYS A 361 SHEET 3 AA2 3 CYS A 391 PHE A 392 -1 N PHE A 392 O VAL A 524 SHEET 1 AA3 2 ARG A 452 ARG A 454 0 SHEET 2 AA3 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA4 2 TYR A 473 GLN A 474 0 SHEET 2 AA4 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA5 4 GLN B 3 SER B 7 0 SHEET 2 AA5 4 LEU B 18 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AA5 4 MET B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA5 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA6 6 LEU B 11 VAL B 12 0 SHEET 2 AA6 6 THR B 122 VAL B 126 1 O THR B 125 N VAL B 12 SHEET 3 AA6 6 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 122 SHEET 4 AA6 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA6 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA6 6 THR B 58 TYR B 60 -1 O TYR B 59 N GLY B 50 SHEET 1 AA7 4 LEU B 11 VAL B 12 0 SHEET 2 AA7 4 THR B 122 VAL B 126 1 O THR B 125 N VAL B 12 SHEET 3 AA7 4 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 122 SHEET 4 AA7 4 TYR B 115 TRP B 118 -1 O TYR B 117 N LYS B 98 SHEET 1 AA8 4 GLN D 3 SER D 7 0 SHEET 2 AA8 4 LEU D 18 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 3 AA8 4 MET D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AA8 4 PHE D 68 ASP D 73 -1 N THR D 69 O GLN D 82 SHEET 1 AA9 6 GLY D 10 VAL D 12 0 SHEET 2 AA9 6 THR D 122 VAL D 126 1 O THR D 125 N GLY D 10 SHEET 3 AA9 6 ALA D 92 ASP D 99 -1 N TYR D 94 O THR D 122 SHEET 4 AA9 6 MET D 34 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AA9 6 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AA9 6 THR D 58 TYR D 60 -1 O TYR D 59 N GLY D 50 SHEET 1 AB1 4 GLY D 10 VAL D 12 0 SHEET 2 AB1 4 THR D 122 VAL D 126 1 O THR D 125 N GLY D 10 SHEET 3 AB1 4 ALA D 92 ASP D 99 -1 N TYR D 94 O THR D 122 SHEET 4 AB1 4 TYR D 115 TRP D 118 -1 O TYR D 117 N LYS D 98 SHEET 1 AB2 5 ASN C 354 ILE C 358 0 SHEET 2 AB2 5 ASN C 394 ARG C 403 -1 O VAL C 395 N ILE C 358 SHEET 3 AB2 5 PRO C 507 GLU C 516 -1 O VAL C 512 N ASP C 398 SHEET 4 AB2 5 GLY C 431 ASN C 437 -1 N ILE C 434 O VAL C 511 SHEET 5 AB2 5 THR C 376 TYR C 380 -1 N TYR C 380 O GLY C 431 SHEET 1 AB3 3 CYS C 361 VAL C 362 0 SHEET 2 AB3 3 VAL C 524 CYS C 525 1 O CYS C 525 N CYS C 361 SHEET 3 AB3 3 CYS C 391 PHE C 392 -1 N PHE C 392 O VAL C 524 SHEET 1 AB4 2 ARG C 452 ARG C 454 0 SHEET 2 AB4 2 LEU C 492 SER C 494 -1 O GLN C 493 N TYR C 453 SHEET 1 AB5 2 TYR C 473 GLN C 474 0 SHEET 2 AB5 2 CYS C 488 TYR C 489 -1 O TYR C 489 N TYR C 473 SSBOND 1 CYS A 336 CYS A 361 1555 1555 2.03 SSBOND 2 CYS A 379 CYS A 432 1555 1555 2.04 SSBOND 3 CYS A 391 CYS A 525 1555 1555 2.03 SSBOND 4 CYS A 480 CYS A 488 1555 1555 2.04 SSBOND 5 CYS B 22 CYS B 96 1555 1555 2.07 SSBOND 6 CYS D 22 CYS D 96 1555 1555 2.08 SSBOND 7 CYS C 336 CYS C 361 1555 1555 2.04 SSBOND 8 CYS C 379 CYS C 432 1555 1555 2.03 SSBOND 9 CYS C 391 CYS C 525 1555 1555 2.02 SSBOND 10 CYS C 480 CYS C 488 1555 1555 2.03 LINK ND2 ASN A 343 C1 NAG A 601 1555 1555 1.45 LINK ND2 ASN C 343 C1 NAG C 601 1555 1555 1.45 CRYST1 82.135 82.135 292.615 90.00 90.00 90.00 P 41 21 2 16 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 0.012175 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012175 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003417 0.00000