HEADER SIGNALING PROTEIN/IMMUNE SYSTEM 06-JUL-24 9IND TITLE INTEGRIN ALPHA-V BETA-8 IN COMPLEX WITH THE FAB OF 130H2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTEGRIN ALPHA-V HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: THE HEAVY CHAIN OF 130H2-FAB; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: THE LIGHT CHAIN OF 130H2-FAB; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: INTEGRIN BETA-8; COMPND 15 CHAIN: B; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ITGAV, MSK8, VNRA, VTNR; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_TAXID: 10090; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 GENE: ITGB8; SOURCE 23 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CRYO-EM, INTEGRIN, COMPLEX, SIGNALING PROTEIN/IMMUNE SYSTEM, KEYWDS 2 SIGNALING PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR H.SUN,Q.ZHENG,X.GUI REVDAT 1 22-JAN-25 9IND 0 JRNL AUTH C.GUO,H.SUN,Y.DU,X.DAI,Y.PANG,Z.HAN,X.XIONG,S.LI,J.ZHANG, JRNL AUTH 2 Q.ZHENG,X.GUI JRNL TITL SPECIFICALLY BLOCKING ALPHA V BETA 8-MEDIATED TGF-BETA JRNL TITL 2 SIGNALING TO REVERSE IMMUNOSUPPRESSION BY MODULATING JRNL TITL 3 MACROPHAGE POLARIZATION. JRNL REF J EXP CLIN CANCER RES V. 44 1 2025 JRNL REFN ISSN 1756-9966 JRNL PMID 39743547 JRNL DOI 10.1186/S13046-024-03250-1 REMARK 2 REMARK 2 RESOLUTION. 2.88 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 2.880 REMARK 3 NUMBER OF PARTICLES : 96290 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9IND COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049218. 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 : INTEGRIN ALPHA-V BETA-8 REMARK 245 COMPLEXED WITH ANTIBODY FAB REMARK 245 FRAGMENT OF 130H2; INTEGRIN REMARK 245 ALPHA-V BETA-8; 130H2-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 : 7.40 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 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) : 4800.00 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, B, 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 B 399 REMARK 465 THR B 400 REMARK 465 GLY B 401 REMARK 465 GLY B 402 REMARK 465 LYS B 403 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASP A 60 CG OD1 OD2 REMARK 470 ARG A 65 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 66 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 82 CG CD CE NZ REMARK 470 ASP A 83 CG OD1 OD2 REMARK 470 GLU A 117 CG CD OE1 OE2 REMARK 470 LYS A 119 CG CD CE NZ REMARK 470 GLU A 121 CG CD OE1 OE2 REMARK 470 THR A 134 OG1 CG2 REMARK 470 GLU A 138 CG CD OE1 OE2 REMARK 470 GLN A 145 CG CD OE1 NE2 REMARK 470 ASP A 146 CG OD1 OD2 REMARK 470 ASP A 148 CG OD1 OD2 REMARK 470 ASP A 167 CG OD1 OD2 REMARK 470 ASN A 198 CG OD1 ND2 REMARK 470 LYS A 259 CG CD CE NZ REMARK 470 TYR A 265 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 270 CG CD OE1 OE2 REMARK 470 ASP A 289 CG OD1 OD2 REMARK 470 ASP A 325 CG OD1 OD2 REMARK 470 GLU A 335 CG CD OE1 OE2 REMARK 470 GLN A 352 CG CD OE1 NE2 REMARK 470 ASP A 353 CG OD1 OD2 REMARK 470 GLU A 367 CG CD OE1 OE2 REMARK 470 ASP A 368 CG OD1 OD2 REMARK 470 LYS A 369 CG CD CE NZ REMARK 470 ARG A 379 CG CD NE CZ NH1 NH2 REMARK 470 THR A 381 OG1 CG2 REMARK 470 ARG A 398 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 416 CG CD CE NZ REMARK 470 LYS H 12 CG CD CE NZ REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 TYR H 27 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS H 63 CG CD CE NZ REMARK 470 ARG L 18 CG CD NE CZ NH1 NH2 REMARK 470 ASP L 70 CG OD1 OD2 REMARK 470 GLU L 79 CG CD OE1 OE2 REMARK 470 LYS L 103 CG CD CE NZ REMARK 470 ASN B 70 CG OD1 ND2 REMARK 470 GLU B 71 CG CD OE1 OE2 REMARK 470 GLU B 80 CG CD OE1 OE2 REMARK 470 GLN B 84 CG CD OE1 NE2 REMARK 470 ARG B 86 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 90 CG CD OE1 OE2 REMARK 470 LYS B 96 CG CD CE NZ REMARK 470 LYS B 101 CG CD CE NZ REMARK 470 LYS B 123 CG CD CE NZ REMARK 470 ASN B 129 CG OD1 ND2 REMARK 470 ASP B 130 CG OD1 OD2 REMARK 470 ARG B 133 CG CD NE CZ NH1 NH2 REMARK 470 PHE B 137 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU B 163 CG CD OE1 OE2 REMARK 470 ARG B 164 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 168 CG CD OE1 NE2 REMARK 470 ASP B 171 CG OD1 OD2 REMARK 470 GLU B 190 CG CD OE1 OE2 REMARK 470 GLU B 196 CG CD OE1 OE2 REMARK 470 LYS B 268 CG CD CE NZ REMARK 470 GLU B 288 CG CD OE1 OE2 REMARK 470 ASP B 292 CG OD1 OD2 REMARK 470 LYS B 304 CG CD CE NZ REMARK 470 GLU B 325 CG CD OE1 OE2 REMARK 470 LYS B 327 CG CD CE NZ REMARK 470 LYS B 341 CG CD CE NZ REMARK 470 GLU B 345 CG CD OE1 OE2 REMARK 470 GLU B 351 CG CD OE1 OE2 REMARK 470 GLN B 353 CG CD OE1 NE2 REMARK 470 GLN B 355 CG CD OE1 NE2 REMARK 470 ARG B 378 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 385 CG CD OE1 OE2 REMARK 470 LYS B 395 CG CD CE NZ REMARK 470 LYS B 396 CG CD CE NZ REMARK 470 TYR B 405 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU B 415 CG CD OE1 OE2 REMARK 470 LYS B 418 CG CD CE NZ REMARK 470 HIS B 420 CG ND1 CD2 CE1 NE2 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 ASN B 167 O - C - N ANGL. DEV. = 10.7 DEGREES REMARK 500 GLN B 168 O - C - N ANGL. DEV. = -11.1 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 GLN A 102 -19.86 72.76 REMARK 500 ASP A 103 -17.59 -147.53 REMARK 500 ASP A 148 -172.48 -171.94 REMARK 500 ALA A 166 30.77 -92.19 REMARK 500 ARG A 211 -169.51 -117.32 REMARK 500 ALA A 213 -169.14 -124.15 REMARK 500 ASN A 232 26.74 -140.76 REMARK 500 ASN A 260 15.03 -141.92 REMARK 500 ARG A 339 61.22 61.63 REMARK 500 ALA H 16 -166.08 -117.60 REMARK 500 THR H 30 -6.98 73.37 REMARK 500 ARG H 104 50.99 -93.23 REMARK 500 CYS L 23 113.59 -161.19 REMARK 500 ALA L 51 -11.53 71.37 REMARK 500 SER L 52 -0.80 -147.60 REMARK 500 ILE B 72 -51.98 -126.33 REMARK 500 LYS B 102 71.48 60.17 REMARK 500 ASN B 129 -62.14 -93.18 REMARK 500 VAL B 150 -68.28 -121.13 REMARK 500 THR B 153 56.36 -94.66 REMARK 500 VAL B 185 -60.72 -96.00 REMARK 500 LYS B 203 -166.92 -118.47 REMARK 500 SER B 205 -158.63 -138.61 REMARK 500 GLU B 233 47.53 -94.65 REMARK 500 GLU B 325 -167.15 -76.52 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 ASN H 99 TYR H 100 148.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60703 RELATED DB: EMDB REMARK 900 INTEGRIN ALPHA-V BETA-8 IN COMPLEX WITH THE FAB OF 130H2 DBREF 9IND A 1 440 UNP P06756 ITAV_HUMAN 31 470 DBREF 9IND H 1 119 PDB 9IND 9IND 1 119 DBREF 9IND L 1 104 PDB 9IND 9IND 1 104 DBREF 9IND B 70 421 UNP P26012 ITB8_HUMAN 112 463 SEQADV 9IND TRP A 419 UNP P06756 TYR 449 CONFLICT SEQRES 1 A 440 PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY SEQRES 2 A 440 PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE SEQRES 3 A 440 VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY SEQRES 4 A 440 ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU SEQRES 5 A 440 GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG SEQRES 6 A 440 ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG SEQRES 7 A 440 ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS SEQRES 8 A 440 GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS SEQRES 9 A 440 ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU SEQRES 10 A 440 MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU SEQRES 11 A 440 GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG SEQRES 12 A 440 SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN SEQRES 13 A 440 GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL SEQRES 14 A 440 LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN SEQRES 15 A 440 LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR SEQRES 16 A 440 ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU SEQRES 17 A 440 ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR SEQRES 18 A 440 LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP SEQRES 19 A 440 GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA SEQRES 20 A 440 ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN SEQRES 21 A 440 MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA SEQRES 22 A 440 ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN SEQRES 23 A 440 GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU SEQRES 24 A 440 PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL SEQRES 25 A 440 GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP SEQRES 26 A 440 PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA SEQRES 27 A 440 ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP SEQRES 28 A 440 GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR SEQRES 29 A 440 GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN SEQRES 30 A 440 GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE SEQRES 31 A 440 LEU GLU GLY GLN TRP ALA ALA ARG SER MET PRO PRO SER SEQRES 32 A 440 PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS SEQRES 33 A 440 ASN GLY TRP PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL SEQRES 34 A 440 ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL SEQRES 1 H 119 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 119 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 119 TYR THR PHE THR ASN TYR GLY ILE ASN TRP VAL ARG GLN SEQRES 4 H 119 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TYR PHE TYR SEQRES 5 H 119 ILE GLY ASN GLY TYR THR GLU TYR ASN GLU LYS PHE LYS SEQRES 6 H 119 GLY ARG VAL THR MET THR SER ASP THR SER THR SER THR SEQRES 7 H 119 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 119 ALA VAL TYR TYR CYS ALA LEU ASN TYR PHE GLY SER ARG SEQRES 9 H 119 LYS PHE ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SEQRES 10 H 119 SER SER SEQRES 1 L 104 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 L 104 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 104 GLN ASN ILE ILE THR ASN LEU HIS TRP TYR GLN GLN LYS SEQRES 4 L 104 PRO GLY GLN ALA PRO ARG LEU LEU ILE LYS TYR ALA SER SEQRES 5 L 104 GLN SER ILE SER GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 104 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 104 GLU PRO GLU ASP PHE ALA VAL TYR PHE CYS GLN GLN SER SEQRES 8 L 104 ASP ASP TRP PRO LEU THR PHE GLY GLN GLY THR LYS LEU SEQRES 1 B 352 ASN GLU ILE ASN THR GLN VAL THR PRO GLY GLU VAL SER SEQRES 2 B 352 ILE GLN LEU ARG PRO GLY ALA GLU ALA ASN PHE MET LEU SEQRES 3 B 352 LYS VAL HIS PRO LEU LYS LYS TYR PRO VAL ASP LEU TYR SEQRES 4 B 352 TYR LEU VAL ASP VAL SER ALA SER MET HIS ASN ASN ILE SEQRES 5 B 352 GLU LYS LEU ASN SER VAL GLY ASN ASP LEU SER ARG LYS SEQRES 6 B 352 MET ALA PHE PHE SER ARG ASP PHE ARG LEU GLY PHE GLY SEQRES 7 B 352 SER TYR VAL ASP LYS THR VAL SER PRO TYR ILE SER ILE SEQRES 8 B 352 HIS PRO GLU ARG ILE HIS ASN GLN CYS SER ASP TYR ASN SEQRES 9 B 352 LEU ASP CYS MET PRO PRO HIS GLY TYR ILE HIS VAL LEU SEQRES 10 B 352 SER LEU THR GLU ASN ILE THR GLU PHE GLU LYS ALA VAL SEQRES 11 B 352 HIS ARG GLN LYS ILE SER GLY ASN ILE ASP THR PRO GLU SEQRES 12 B 352 GLY GLY PHE ASP ALA MET LEU GLN ALA ALA VAL CYS GLU SEQRES 13 B 352 SER HIS ILE GLY TRP ARG LYS GLU ALA LYS ARG LEU LEU SEQRES 14 B 352 LEU VAL MET THR ASP GLN THR SER HIS LEU ALA LEU ASP SEQRES 15 B 352 SER LYS LEU ALA GLY ILE VAL VAL PRO ASN ASP GLY ASN SEQRES 16 B 352 CYS HIS LEU LYS ASN ASN VAL TYR VAL LYS SER THR THR SEQRES 17 B 352 MET GLU HIS PRO SER LEU GLY GLN LEU SER GLU LYS LEU SEQRES 18 B 352 ILE ASP ASN ASN ILE ASN VAL ILE PHE ALA VAL GLN GLY SEQRES 19 B 352 LYS GLN PHE HIS TRP TYR LYS ASP LEU LEU PRO LEU LEU SEQRES 20 B 352 PRO GLY THR ILE ALA GLY GLU ILE GLU SER LYS ALA ALA SEQRES 21 B 352 ASN LEU ASN ASN LEU VAL VAL GLU ALA TYR GLN LYS LEU SEQRES 22 B 352 ILE SER GLU VAL LYS VAL GLN VAL GLU ASN GLN VAL GLN SEQRES 23 B 352 GLY ILE TYR PHE ASN ILE THR ALA ILE CYS PRO ASP GLY SEQRES 24 B 352 SER ARG LYS PRO GLY MET GLU GLY CYS ARG ASN VAL THR SEQRES 25 B 352 SER ASN ASP GLU VAL LEU PHE ASN VAL THR VAL THR MET SEQRES 26 B 352 LYS LYS CYS ASP VAL THR GLY GLY LYS ASN TYR ALA ILE SEQRES 27 B 352 ILE LYS PRO ILE GLY PHE ASN GLU THR ALA LYS ILE HIS SEQRES 28 B 352 ILE HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET MAN C 4 11 HET MAN C 5 11 HET NAG A 501 14 HET NAG A 502 14 HET NAG B 501 14 HET NAG B 502 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-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 HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 6(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 FORMUL 5 MAN 2(C6 H12 O6) HELIX 1 AA1 GLY A 175 GLN A 180 1 6 HELIX 2 AA2 VAL A 188 LYS A 194 1 7 HELIX 3 AA3 GLN A 214 ASP A 218 5 5 HELIX 4 AA4 ARG A 245 LEU A 250 1 6 HELIX 5 AA5 GLY A 366 LYS A 370 5 5 HELIX 6 AA6 ARG H 87 THR H 91 5 5 HELIX 7 AA7 GLU L 79 PHE L 83 5 5 HELIX 8 AA8 SER B 114 SER B 116 5 3 HELIX 9 AA9 MET B 117 LYS B 123 1 7 HELIX 10 AB1 SER B 126 MET B 135 1 10 HELIX 11 AB2 HIS B 161 TYR B 172 1 12 HELIX 12 AB3 ASN B 191 GLN B 202 1 12 HELIX 13 AB4 GLY B 213 CYS B 224 1 12 HELIX 14 AB5 CYS B 224 GLY B 229 1 6 HELIX 15 AB6 LEU B 250 GLY B 256 5 7 HELIX 16 AB7 SER B 282 ASN B 293 1 12 HELIX 17 AB8 GLN B 305 LEU B 313 1 9 HELIX 18 AB9 ASN B 330 GLU B 345 1 16 SHEET 1 AA1 4 ALA A 9 SER A 12 0 SHEET 2 AA1 4 ARG A 431 TYR A 435 -1 O LEU A 434 N ALA A 9 SHEET 3 AA1 4 ASP A 421 ALA A 426 -1 N LEU A 422 O TYR A 435 SHEET 4 AA1 4 SER A 407 THR A 412 -1 N SER A 407 O GLY A 425 SHEET 1 AA2 4 VAL A 23 PHE A 26 0 SHEET 2 AA2 4 PHE A 35 ALA A 40 -1 O PHE A 35 N PHE A 26 SHEET 3 AA2 4 GLN A 55 ASP A 60 -1 O CYS A 59 N LEU A 36 SHEET 4 AA2 4 CYS A 67 PRO A 69 -1 O GLN A 68 N LYS A 58 SHEET 1 AA3 2 ASP A 79 ALA A 81 0 SHEET 2 AA3 2 ASP A 84 PRO A 85 -1 O ASP A 84 N TYR A 80 SHEET 1 AA4 3 GLU A 87 PHE A 88 0 SHEET 2 AA4 3 HIS A 113 TRP A 114 -1 O HIS A 113 N PHE A 88 SHEET 3 AA4 3 GLU A 123 PRO A 124 -1 O GLU A 123 N TRP A 114 SHEET 1 AA5 4 VAL A 98 LYS A 101 0 SHEET 2 AA5 4 LYS A 104 ALA A 109 -1 O LEU A 106 N ARG A 99 SHEET 3 AA5 4 THR A 127 ASP A 132 -1 O PHE A 129 N ALA A 107 SHEET 4 AA5 4 LYS A 135 TYR A 139 -1 O TYR A 139 N CYS A 128 SHEET 1 AA6 4 SER A 160 PHE A 163 0 SHEET 2 AA6 4 ARG A 168 GLY A 173 -1 O LEU A 170 N ASP A 162 SHEET 3 AA6 4 GLN A 182 GLN A 187 -1 O ILE A 184 N LEU A 171 SHEET 4 AA6 4 LEU A 208 ALA A 209 -1 O LEU A 208 N SER A 185 SHEET 1 AA7 4 SER A 225 GLY A 229 0 SHEET 2 AA7 4 ASP A 238 VAL A 243 -1 O GLY A 242 N SER A 225 SHEET 3 AA7 4 MET A 252 TYR A 256 -1 O TYR A 256 N PHE A 239 SHEET 4 AA7 4 SER A 263 THR A 268 -1 O LEU A 264 N ILE A 255 SHEET 1 AA8 4 VAL A 280 THR A 283 0 SHEET 2 AA8 4 ASP A 292 ALA A 297 -1 O ASP A 292 N THR A 283 SHEET 3 AA8 4 GLN A 314 GLN A 320 -1 O SER A 316 N ILE A 295 SHEET 4 AA8 4 PHE A 326 ASN A 332 -1 O THR A 329 N VAL A 317 SHEET 1 AA9 2 MET A 301 ARG A 303 0 SHEET 2 AA9 2 LEU A 309 GLU A 311 -1 O GLN A 310 N ASP A 302 SHEET 1 AB1 4 ILE A 344 GLY A 348 0 SHEET 2 AB1 4 ASP A 357 ALA A 362 -1 O ALA A 359 N ALA A 345 SHEET 3 AB1 4 ILE A 372 PHE A 376 -1 O ILE A 372 N ALA A 362 SHEET 4 AB1 4 GLN A 389 GLU A 392 -1 O GLN A 389 N ILE A 375 SHEET 1 AB2 2 GLY A 378 ARG A 379 0 SHEET 2 AB2 2 GLY A 382 LEU A 383 -1 O GLY A 382 N ARG A 379 SHEET 1 AB3 4 VAL H 5 GLN H 6 0 SHEET 2 AB3 4 SER H 17 LYS H 23 -1 O LYS H 23 N VAL H 5 SHEET 3 AB3 4 THR H 78 SER H 84 -1 O VAL H 79 N CYS H 22 SHEET 4 AB3 4 VAL H 68 ASP H 73 -1 N THR H 69 O GLU H 82 SHEET 1 AB4 6 GLU H 10 VAL H 11 0 SHEET 2 AB4 6 THR H 113 THR H 116 1 O THR H 114 N GLU H 10 SHEET 3 AB4 6 ALA H 92 TYR H 100 -1 N TYR H 94 O THR H 113 SHEET 4 AB4 6 GLY H 33 GLN H 39 -1 N ASN H 35 O ALA H 97 SHEET 5 AB4 6 LEU H 45 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AB4 6 THR H 58 TYR H 60 -1 O GLU H 59 N TYR H 50 SHEET 1 AB5 4 GLU H 10 VAL H 11 0 SHEET 2 AB5 4 THR H 113 THR H 116 1 O THR H 114 N GLU H 10 SHEET 3 AB5 4 ALA H 92 TYR H 100 -1 N TYR H 94 O THR H 113 SHEET 4 AB5 4 SER H 103 TYR H 108 -1 O TYR H 108 N LEU H 98 SHEET 1 AB6 4 GLN L 6 SER L 7 0 SHEET 2 AB6 4 ALA L 19 CYS L 23 -1 O SER L 22 N SER L 7 SHEET 3 AB6 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AB6 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB7 5 GLN L 53 SER L 54 0 SHEET 2 AB7 5 ARG L 45 LYS L 49 -1 N LYS L 49 O GLN L 53 SHEET 3 AB7 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AB7 5 VAL L 85 GLN L 90 -1 O PHE L 87 N TYR L 36 SHEET 5 AB7 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB8 5 VAL B 76 THR B 77 0 SHEET 2 AB8 5 ALA B 91 VAL B 97 -1 O LYS B 96 N THR B 77 SHEET 3 AB8 5 VAL B 386 MET B 394 -1 O VAL B 392 N ALA B 91 SHEET 4 AB8 5 ILE B 357 ILE B 364 -1 N ILE B 364 O LEU B 387 SHEET 5 AB8 5 ARG B 370 PRO B 372 -1 O LYS B 371 N ALA B 363 SHEET 1 AB9 4 GLU B 80 SER B 82 0 SHEET 2 AB9 4 LYS B 418 HIS B 420 1 O HIS B 420 N VAL B 81 SHEET 3 AB9 4 TYR B 405 PRO B 410 -1 N ALA B 406 O ILE B 419 SHEET 4 AB9 4 VAL B 348 GLU B 351 -1 N GLU B 351 O ILE B 407 SHEET 1 AC1 6 TYR B 182 THR B 189 0 SHEET 2 AC1 6 SER B 139 TYR B 149 -1 N LEU B 144 O THR B 189 SHEET 3 AC1 6 TYR B 103 ASP B 112 1 N LEU B 107 O ARG B 143 SHEET 4 AC1 6 LYS B 235 THR B 242 1 O LYS B 235 N PRO B 104 SHEET 5 AC1 6 ILE B 295 VAL B 301 1 O ILE B 298 N VAL B 240 SHEET 6 AC1 6 THR B 319 GLU B 323 1 O GLY B 322 N PHE B 299 SSBOND 1 CYS A 59 CYS A 67 1555 1555 2.03 SSBOND 2 CYS A 108 CYS A 128 1555 1555 2.02 SSBOND 3 CYS A 142 CYS A 155 1555 1555 2.04 SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.02 SSBOND 6 CYS B 169 CYS B 176 1555 1555 2.03 SSBOND 7 CYS B 224 CYS B 265 1555 1555 2.03 SSBOND 8 CYS B 365 CYS B 377 1555 1555 2.03 LINK ND2 ASN A 44 C1 NAG A 501 1555 1555 1.43 LINK ND2 ASN A 260 C1 NAG A 502 1555 1555 1.43 LINK ND2 ASN A 266 C1 NAG C 1 1555 1555 1.43 LINK ND2 ASN B 389 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 414 C1 NAG B 502 1555 1555 1.43 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.44 LINK O6 BMA C 3 C1 MAN C 5 1555 1555 1.46 CISPEP 1 SER L 7 PRO L 8 0 -0.28 CISPEP 2 TRP L 94 PRO L 95 0 0.25 CISPEP 3 THR B 77 PRO B 78 0 -1.07 CISPEP 4 SER B 155 PRO B 156 0 2.16 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