HEADER VIRAL PROTEIN/IMMUNE SYSTEM 08-FEB-25 9LUE TITLE CRYO-EM STRUCTURE OF THE NIPAH G HEAD DOMAIN IN COMPLEX WITH THREE TITLE 2 FABS COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLYCOPROTEIN G; COMPND 3 CHAIN: G; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NIV LN3D3 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NIV S2B10 FAB HEAVY CHAIN; COMPND 11 CHAIN: A; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: NIV S2B10 FAB LIGHT CHAIN; COMPND 15 CHAIN: B; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: NIV S1E2 FAB HEAVY CHAIN; COMPND 19 CHAIN: C; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: NIV S1E2 FAB LIGHT CHAIN; COMPND 23 CHAIN: D; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: NIV LN3D3 FAB HEAVY CHAIN; COMPND 27 CHAIN: H; COMPND 28 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HENIPAVIRUS NIPAHENSE; SOURCE 3 ORGANISM_TAXID: 3052225; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MESOCRICETUS AURATUS; SOURCE 8 ORGANISM_TAXID: 10036; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MESOCRICETUS AURATUS; SOURCE 13 ORGANISM_TAXID: 10036; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: MESOCRICETUS AURATUS; SOURCE 18 ORGANISM_TAXID: 10036; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 5; SOURCE 22 ORGANISM_SCIENTIFIC: MESOCRICETUS AURATUS; SOURCE 23 ORGANISM_TAXID: 10036; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 MOL_ID: 6; SOURCE 27 ORGANISM_SCIENTIFIC: MESOCRICETUS AURATUS; SOURCE 28 ORGANISM_TAXID: 10036; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 31 MOL_ID: 7; SOURCE 32 ORGANISM_SCIENTIFIC: MESOCRICETUS AURATUS; SOURCE 33 ORGANISM_TAXID: 10036; SOURCE 34 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NIPAH G PROTEIN, ANTIBODIES, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Y.WANG,Z.DENG,H.ZHAO REVDAT 1 26-NOV-25 9LUE 0 JRNL AUTH Y.WANG,Z.DENG,H.ZHAO JRNL TITL CRYO-EM STRUCTURE OF THE NIPAH G HEAD DOMAIN IN COMPLEX WITH JRNL TITL 2 THREE FABS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.03 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, COOT REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.030 REMARK 3 NUMBER OF PARTICLES : 145635 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9LUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 12-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300054266. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : THE QUATERNARY COMPLEX OF NIPAH REMARK 245 VIRUS G PROTEIN WITH LN3D3, REMARK 245 S2B10, AND S1E2 ANTIBODY FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : JEOL CRYO ARM 300 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: HEPTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, L, A, B, C, D, H 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 LEU L 104 REMARK 465 GLU L 105 REMARK 465 ILE L 106 REMARK 465 LYS L 107 REMARK 465 ALA A 113 REMARK 465 GLU B 105 REMARK 465 ILE B 106 REMARK 465 LYS B 107 REMARK 465 LYS D 107 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 H 6 SG CYS H 92 1.36 REMARK 500 OE2 GLU A 6 SG CYS A 92 1.54 REMARK 500 OE2 GLU A 6 CB CYS A 92 2.12 REMARK 500 OE2 GLU A 6 N CYS A 92 2.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 SER D 14 C PRO D 15 N 0.169 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 LEU L 33 CA - CB - CG ANGL. DEV. = 14.7 DEGREES REMARK 500 PRO D 15 C - N - CA ANGL. DEV. = 10.6 DEGREES REMARK 500 PRO H 98 C - N - CD ANGL. DEV. = -14.0 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 ASN G 287 113.78 -160.28 REMARK 500 ASN G 288 70.44 57.67 REMARK 500 GLU G 289 15.54 57.71 REMARK 500 PRO G 303 0.16 -69.15 REMARK 500 SER G 457 74.83 -100.32 REMARK 500 PHE G 458 48.91 -92.38 REMARK 500 GLN G 490 -164.79 -128.65 REMARK 500 GLN G 492 -11.69 74.55 REMARK 500 ASN G 534 72.57 59.08 REMARK 500 ASN G 570 41.76 35.74 REMARK 500 TYR G 581 74.41 -103.70 REMARK 500 ALA L 51 -5.24 67.74 REMARK 500 SER L 91 33.90 -141.37 REMARK 500 THR A 30 47.60 -89.12 REMARK 500 TYR A 32 176.34 64.85 REMARK 500 TRP A 99 -6.12 72.34 REMARK 500 TYR B 30B 60.01 -109.04 REMARK 500 ALA B 51 -5.64 67.16 REMARK 500 ARG B 68 -115.58 60.22 REMARK 500 ALA B 80 45.87 -89.64 REMARK 500 SER D 50 -118.79 57.02 REMARK 500 PRO H 9 129.46 -37.21 REMARK 500 TYR H 97 84.88 56.13 REMARK 500 PRO H 98 -126.58 38.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TYR H 97 PRO H 98 -134.25 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63395 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE NIPAH G HEAD DOMAIN IN COMPLEX WITH THREE REMARK 900 FABS DBREF 9LUE G 177 602 UNP Q9IH62 GLYCP_NIPAV 177 602 DBREF 9LUE L 1 107 PDB 9LUE 9LUE 1 107 DBREF 9LUE A 1 113 PDB 9LUE 9LUE 1 113 DBREF 9LUE B 1 107 PDB 9LUE 9LUE 1 107 DBREF 9LUE C 1 113 PDB 9LUE 9LUE 1 113 DBREF 9LUE D 1 107 PDB 9LUE 9LUE 1 107 DBREF 9LUE H 1 113 PDB 9LUE 9LUE 1 113 SEQRES 1 G 426 GLY VAL SER ASN LEU VAL GLY LEU PRO ASN ASN ILE CYS SEQRES 2 G 426 LEU GLN LYS THR SER ASN GLN ILE LEU LYS PRO LYS LEU SEQRES 3 G 426 ILE SER TYR THR LEU PRO VAL VAL GLY GLN SER GLY THR SEQRES 4 G 426 CYS ILE THR ASP PRO LEU LEU ALA MET ASP GLU GLY TYR SEQRES 5 G 426 PHE ALA TYR SER HIS LEU GLU ARG ILE GLY SER CYS SER SEQRES 6 G 426 ARG GLY VAL SER LYS GLN ARG ILE ILE GLY VAL GLY GLU SEQRES 7 G 426 VAL LEU ASP ARG GLY ASP GLU VAL PRO SER LEU PHE MET SEQRES 8 G 426 THR ASN VAL TRP THR PRO PRO ASN PRO ASN THR VAL TYR SEQRES 9 G 426 HIS CYS SER ALA VAL TYR ASN ASN GLU PHE TYR TYR VAL SEQRES 10 G 426 LEU CYS ALA VAL SER THR VAL GLY ASP PRO ILE LEU ASN SEQRES 11 G 426 SER THR TYR TRP SER GLY SER LEU MET MET THR ARG LEU SEQRES 12 G 426 ALA VAL LYS PRO LYS SER ASN GLY GLY GLY TYR ASN GLN SEQRES 13 G 426 HIS GLN LEU ALA LEU ARG SER ILE GLU LYS GLY ARG TYR SEQRES 14 G 426 ASP LYS VAL MET PRO TYR GLY PRO SER GLY ILE LYS GLN SEQRES 15 G 426 GLY ASP THR LEU TYR PHE PRO ALA VAL GLY PHE LEU VAL SEQRES 16 G 426 ARG THR GLU PHE LYS TYR ASN ASP SER ASN CYS PRO ILE SEQRES 17 G 426 THR LYS CYS GLN TYR SER LYS PRO GLU ASN CYS ARG LEU SEQRES 18 G 426 SER MET GLY ILE ARG PRO ASN SER HIS TYR ILE LEU ARG SEQRES 19 G 426 SER GLY LEU LEU LYS TYR ASN LEU SER ASP GLY GLU ASN SEQRES 20 G 426 PRO LYS VAL VAL PHE ILE GLU ILE SER ASP GLN ARG LEU SEQRES 21 G 426 SER ILE GLY SER PRO SER LYS ILE TYR ASP SER LEU GLY SEQRES 22 G 426 GLN PRO VAL PHE TYR GLN ALA SER PHE SER TRP ASP THR SEQRES 23 G 426 MET ILE LYS PHE GLY ASP VAL LEU THR VAL ASN PRO LEU SEQRES 24 G 426 VAL VAL ASN TRP ARG ASN ASN THR VAL ILE SER ARG PRO SEQRES 25 G 426 GLY GLN SER GLN CYS PRO ARG PHE ASN THR CYS PRO GLU SEQRES 26 G 426 ILE CYS TRP GLU GLY VAL TYR ASN ASP ALA PHE LEU ILE SEQRES 27 G 426 ASP ARG ILE ASN TRP ILE SER ALA GLY VAL PHE LEU ASP SEQRES 28 G 426 SER ASN GLN THR ALA GLU ASN PRO VAL PHE THR VAL PHE SEQRES 29 G 426 LYS ASP ASN GLU ILE LEU TYR ARG ALA GLN LEU ALA SER SEQRES 30 G 426 GLU ASP THR ASN ALA GLN LYS THR ILE THR ASN CYS PHE SEQRES 31 G 426 LEU LEU LYS ASN LYS ILE TRP CYS ILE SER LEU VAL GLU SEQRES 32 G 426 ILE TYR ASP THR GLY ASP ASN VAL ILE ARG PRO LYS LEU SEQRES 33 G 426 PHE ALA VAL LYS ILE PRO GLU GLN CYS THR SEQRES 1 L 107 GLU ILE GLN MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 107 THR PRO GLY ASP SER VAL SER LEU SER CYS ARG ALA SER SEQRES 3 L 107 GLN SER ILE SER ASN ASN LEU HIS TRP TYR GLN GLN LYS SEQRES 4 L 107 SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA SER SEQRES 5 L 107 GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN ASN LEU SEQRES 7 L 107 GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN HIS SER SEQRES 8 L 107 ASP SER TRP PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 L 107 GLU ILE LYS SEQRES 1 A 119 GLN MET GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 A 119 PRO SER GLN SER LEU SER LEU THR CYS THR VAL THR GLY SEQRES 3 A 119 TYR SER ILE THR SER ASP TYR ALA TRP ASN TRP ILE ARG SEQRES 4 A 119 GLN PHE PRO ARG ASN LYS LEU GLU TRP MET GLY PHE ILE SEQRES 5 A 119 THR TYR SER GLY SER THR SER TYR ASN PRO SER LEU LYS SEQRES 6 A 119 SER ARG ILE SER LEU THR ARG ASP THR SER LYS ASN GLN SEQRES 7 A 119 PHE PHE LEU GLN LEU SER SER VAL THR THR GLU ASP THR SEQRES 8 A 119 ALA THR TYR TYR CYS ALA ARG SER GLY ALA ASN TRP ASP SEQRES 9 A 119 TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 A 119 SER ALA SEQRES 1 B 111 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 B 111 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 B 111 GLU SER VAL ASP ASN TYR GLY ASN SER PHE MET HIS TRP SEQRES 4 B 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 B 111 TYR ARG ALA SER LYS LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6 B 111 PHE SER GLY SER GLY SER ARG THR ASP PHE THR LEU THR SEQRES 7 B 111 ILE ASN PRO VAL GLU ALA ASP ASP VAL ALA THR TYR HIS SEQRES 8 B 111 CYS GLN GLN SER ASN GLU ASP PRO TRP THR PHE GLY GLY SEQRES 9 B 111 GLY THR LYS LEU GLU ILE LYS SEQRES 1 C 120 GLN MET GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 C 120 PRO SER GLN SER LEU SER LEU THR CYS SER VAL THR GLY SEQRES 3 C 120 TYR SER ILE THR SER GLY TYR TYR TRP ASN TRP ILE ARG SEQRES 4 C 120 GLN PHE SER GLY ASN LYS LEU GLU TRP MET GLY TYR ILE SEQRES 5 C 120 ASN HIS ASP GLY SER LYS ASN TYR ASN PRO SER LEU LYS SEQRES 6 C 120 ASN ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN SEQRES 7 C 120 PHE PHE LEU LYS LEU ASN SER VAL THR THR GLU ASP THR SEQRES 8 C 120 ALA THR TYR TYR CYS ALA ARG ASP TYR GLY SER TYR TYR SEQRES 9 C 120 TYR PRO MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 C 120 VAL SER SER SEQRES 1 D 106 GLU ILE VAL LEU THR GLN SER PRO PRO ILE MET SER ALA SEQRES 2 D 106 SER PRO GLY GLU LYS VAL THR ILE THR CYS SER ALA SER SEQRES 3 D 106 SER SER VAL THR PHE MET HIS TRP PHE GLN GLN LYS PRO SEQRES 4 D 106 GLY THR SER PRO LYS LEU TRP ILE PHE SER THR SER ASN SEQRES 5 D 106 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 D 106 SER GLY THR SER TYR SER LEU THR ILE SER ARG MET GLU SEQRES 7 D 106 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN ARG SER SEQRES 8 D 106 SER TYR PRO PHE THR PHE GLY SER GLY THR LYS LEU GLU SEQRES 9 D 106 ILE LYS SEQRES 1 H 119 GLU VAL LYS LEU GLU GLU SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 119 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 H 119 TYR THR PHE THR ASN TYR VAL MET HIS TRP VAL LYS GLN SEQRES 4 H 119 LYS PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR VAL ASN SEQRES 5 H 119 PRO TYR ASN ASP GLY THR GLN TYR ASN GLU LYS PHE ARG SEQRES 6 H 119 ASP LYS ALA THR LEU THR SER ASP LYS SER SER SER THR SEQRES 7 H 119 VAL TYR MET GLU LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 H 119 ALA VAL TYR TYR CYS THR ARG GLY ASP TYR PRO TYR TRP SEQRES 9 H 119 VAL PHE GLU VAL TRP GLY ALA GLY THR THR VAL THR VAL SEQRES 10 H 119 SER SER HET NAG G1605 14 HET NAG G1606 14 HET NAG G1607 14 HET NAG G1608 14 HET NAG G1701 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 8 NAG 5(C8 H15 N O6) HELIX 1 AA1 ASN G 306 TRP G 310 5 5 HELIX 2 AA2 GLU G 393 SER G 398 1 6 HELIX 3 AA3 GLU L 79 PHE L 83 5 5 HELIX 4 AA4 PRO A 61 LYS A 64 5 4 HELIX 5 AA5 THR A 83 THR A 87 5 5 HELIX 6 AA6 THR C 83 ASP C 86 5 4 HELIX 7 AA7 GLU D 79 ALA D 83 5 5 HELIX 8 AA8 THR H 28 TYR H 32 5 5 HELIX 9 AA9 THR H 83 SER H 87 5 5 SHEET 1 AA1 5 VAL G 178 SER G 179 0 SHEET 2 AA1 5 ASN G 557 LEU G 568 -1 O LEU G 567 N SER G 179 SHEET 3 AA1 5 LYS G 571 TYR G 581 -1 O ILE G 575 N ASN G 564 SHEET 4 AA1 5 LYS G 591 LYS G 596 -1 O VAL G 595 N CYS G 574 SHEET 5 AA1 5 PRO G 200 ILE G 203 -1 N LYS G 201 O ALA G 594 SHEET 1 AA2 4 THR G 215 ASP G 225 0 SHEET 2 AA2 4 TYR G 228 ILE G 237 -1 O ARG G 236 N CYS G 216 SHEET 3 AA2 4 VAL G 244 ASP G 257 -1 O VAL G 244 N ILE G 237 SHEET 4 AA2 4 PRO G 263 TRP G 271 -1 O TRP G 271 N ILE G 250 SHEET 1 AA3 4 VAL G 279 ASN G 287 0 SHEET 2 AA3 4 PHE G 290 VAL G 297 -1 O LEU G 294 N SER G 283 SHEET 3 AA3 4 LEU G 314 ALA G 320 -1 O THR G 317 N VAL G 293 SHEET 4 AA3 4 GLN G 332 LEU G 335 -1 O HIS G 333 N ARG G 318 SHEET 1 AA4 5 SER G 339 GLU G 341 0 SHEET 2 AA4 5 LYS G 425 GLU G 430 1 O PHE G 428 N GLU G 341 SHEET 3 AA4 5 TYR G 407 ASN G 417 -1 N LYS G 415 O VAL G 427 SHEET 4 AA4 5 THR G 361 VAL G 371 -1 N ALA G 366 O GLY G 412 SHEET 5 AA4 5 LYS G 347 PRO G 350 -1 N MET G 349 O VAL G 367 SHEET 1 AA5 5 SER G 339 GLU G 341 0 SHEET 2 AA5 5 LYS G 425 GLU G 430 1 O PHE G 428 N GLU G 341 SHEET 3 AA5 5 TYR G 407 ASN G 417 -1 N LYS G 415 O VAL G 427 SHEET 4 AA5 5 THR G 361 VAL G 371 -1 N ALA G 366 O GLY G 412 SHEET 5 AA5 5 ILE G 356 GLN G 358 -1 N ILE G 356 O TYR G 363 SHEET 1 AA6 4 SER G 442 SER G 447 0 SHEET 2 AA6 4 GLN G 450 GLN G 455 -1 O TYR G 454 N LYS G 443 SHEET 3 AA6 4 LYS G 465 THR G 471 -1 O GLY G 467 N PHE G 453 SHEET 4 AA6 4 VAL G 476 TRP G 479 -1 O ASN G 478 N ASP G 468 SHEET 1 AA7 4 PHE G 512 ASP G 515 0 SHEET 2 AA7 4 ILE G 520 LEU G 526 -1 O ALA G 522 N PHE G 512 SHEET 3 AA7 4 PRO G 535 PHE G 540 -1 O THR G 538 N GLY G 523 SHEET 4 AA7 4 ILE G 545 GLN G 550 -1 O TYR G 547 N VAL G 539 SHEET 1 AA8 4 MET L 4 SER L 7 0 SHEET 2 AA8 4 VAL L 19 ILE L 29 -1 O SER L 22 N SER L 7 SHEET 3 AA8 4 GLY L 68 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA8 4 SER L 63 GLY L 66 -1 N SER L 63 O SER L 74 SHEET 1 AA9 4 GLN L 53 SER L 54 0 SHEET 2 AA9 4 ARG L 45 LYS L 49 -1 N LYS L 49 O GLN L 53 SHEET 3 AA9 4 LEU L 33 GLN L 38 -1 N GLN L 37 O ARG L 45 SHEET 4 AA9 4 MET L 85 HIS L 90 -1 O MET L 85 N GLN L 38 SHEET 1 AB1 4 GLN A 3 SER A 7 0 SHEET 2 AB1 4 SER A 17 THR A 25 -1 O THR A 23 N GLN A 5 SHEET 3 AB1 4 GLN A 77 SER A 82A-1 O LEU A 80 N LEU A 20 SHEET 4 AB1 4 ILE A 67 ASP A 72 -1 N THR A 70 O PHE A 79 SHEET 1 AB2 6 LEU A 11 VAL A 12 0 SHEET 2 AB2 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB2 6 ALA A 88 SER A 95 -1 N ALA A 88 O VAL A 109 SHEET 4 AB2 6 ALA A 33 GLN A 39 -1 N ALA A 33 O SER A 95 SHEET 5 AB2 6 LEU A 45 THR A 52 -1 O GLU A 46 N ARG A 38 SHEET 6 AB2 6 THR A 57 TYR A 59 -1 O SER A 58 N PHE A 50 SHEET 1 AB3 4 LEU A 11 VAL A 12 0 SHEET 2 AB3 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB3 4 ALA A 88 SER A 95 -1 N ALA A 88 O VAL A 109 SHEET 4 AB3 4 PHE A 100B TRP A 103 -1 O TYR A 102 N ARG A 94 SHEET 1 AB4 4 MET B 4 SER B 7 0 SHEET 2 AB4 4 ALA B 19 ALA B 25 -1 O SER B 22 N SER B 7 SHEET 3 AB4 4 ASP B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AB4 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AB5 4 LYS B 53 LEU B 54 0 SHEET 2 AB5 4 PRO B 44 TYR B 49 -1 N TYR B 49 O LYS B 53 SHEET 3 AB5 4 MET B 33 GLN B 38 -1 N GLN B 37 O LYS B 45 SHEET 4 AB5 4 THR B 85 GLN B 90 -1 O GLN B 89 N HIS B 34 SHEET 1 AB6 4 GLN C 3 SER C 7 0 SHEET 2 AB6 4 LEU C 18 THR C 25 -1 O SER C 23 N GLN C 5 SHEET 3 AB6 4 GLN C 77 LEU C 82 -1 O PHE C 78 N CYS C 22 SHEET 4 AB6 4 ILE C 67 ASP C 72 -1 N ASP C 72 O GLN C 77 SHEET 1 AB7 6 LEU C 11 VAL C 12 0 SHEET 2 AB7 6 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AB7 6 ALA C 88 ASP C 95 -1 N TYR C 90 O THR C 107 SHEET 4 AB7 6 TYR C 33 PHE C 40 -1 N TYR C 33 O ASP C 95 SHEET 5 AB7 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB7 6 LYS C 57 TYR C 59 -1 O ASN C 58 N TYR C 50 SHEET 1 AB8 4 LEU C 11 VAL C 12 0 SHEET 2 AB8 4 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AB8 4 ALA C 88 ASP C 95 -1 N TYR C 90 O THR C 107 SHEET 4 AB8 4 TYR C 102 TRP C 103 -1 O TYR C 102 N ARG C 94 SHEET 1 AB9 4 THR D 5 GLN D 6 0 SHEET 2 AB9 4 VAL D 19 SER D 24 -1 O SER D 24 N THR D 5 SHEET 3 AB9 4 SER D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AB9 4 PHE D 62 SER D 67 -1 N SER D 65 O SER D 72 SHEET 1 AC1 4 ASN D 53 LEU D 54 0 SHEET 2 AC1 4 LYS D 45 PHE D 49 -1 N PHE D 49 O ASN D 53 SHEET 3 AC1 4 HIS D 34 GLN D 38 -1 N GLN D 37 O LYS D 45 SHEET 4 AC1 4 THR D 85 GLN D 89 -1 O GLN D 89 N HIS D 34 SHEET 1 AC2 4 LYS H 3 GLU H 6 0 SHEET 2 AC2 4 SER H 17 SER H 25 -1 O LYS H 23 N GLU H 5 SHEET 3 AC2 4 THR H 77 ASN H 82A-1 O VAL H 78 N CYS H 22 SHEET 4 AC2 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AC3 5 GLY H 56 TYR H 59 0 SHEET 2 AC3 5 LEU H 45 ASN H 52 -1 N TYR H 50 O GLN H 58 SHEET 3 AC3 5 MET H 34 GLN H 39 -1 N LYS H 38 O GLU H 46 SHEET 4 AC3 5 ALA H 88 ASP H 96 -1 O TYR H 91 N VAL H 37 SHEET 5 AC3 5 VAL H 100A TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AC4 5 GLY H 56 TYR H 59 0 SHEET 2 AC4 5 LEU H 45 ASN H 52 -1 N TYR H 50 O GLN H 58 SHEET 3 AC4 5 MET H 34 GLN H 39 -1 N LYS H 38 O GLU H 46 SHEET 4 AC4 5 ALA H 88 ASP H 96 -1 O TYR H 91 N VAL H 37 SHEET 5 AC4 5 THR H 107 VAL H 109 -1 O VAL H 109 N ALA H 88 SSBOND 1 CYS G 189 CYS G 601 1555 1555 2.04 SSBOND 2 CYS G 216 CYS G 240 1555 1555 2.03 SSBOND 3 CYS G 282 CYS G 295 1555 1555 2.03 SSBOND 4 CYS G 382 CYS G 395 1555 1555 2.03 SSBOND 5 CYS G 387 CYS G 499 1555 1555 2.03 SSBOND 6 CYS G 493 CYS G 503 1555 1555 2.04 SSBOND 7 CYS G 565 CYS G 574 1555 1555 2.03 SSBOND 8 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 9 CYS A 22 CYS A 92 1555 1555 2.03 SSBOND 10 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 11 CYS C 22 CYS C 92 1555 1555 2.03 SSBOND 12 CYS D 23 CYS D 88 1555 1555 2.03 SSBOND 13 CYS H 22 CYS H 92 1555 1555 2.03 LINK ND2 ASN G 306 C1 NAG G1608 1555 1555 1.44 LINK ND2 ASN G 378 C1 NAG G1701 1555 1555 1.45 LINK ND2 ASN G 417 C1 NAG G1605 1555 1555 1.44 LINK ND2 ASN G 481 C1 NAG G1607 1555 1555 1.44 LINK ND2 ASN G 529 C1 NAG G1606 1555 1555 1.45 CISPEP 1 ASN G 473 PRO G 474 0 -1.39 CISPEP 2 SER L 7 PRO L 8 0 -8.33 CISPEP 3 SER B 7 PRO B 8 0 -7.06 CISPEP 4 ASN B 76 PRO B 77 0 -3.40 CISPEP 5 ASP B 94 PRO B 95 0 -7.65 CISPEP 6 TYR D 94 PRO D 95 0 2.14 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000