HEADER IMMUNE SYSTEM 20-MAR-24 9EQ3 TITLE STRUCTURE OF IGE HMM5 BOUND TO FCERIA CRYO-EM CLASS 8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGE HMM5 HEAVY CHAIN; COMPND 3 CHAIN: H, X; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGE HMM5 LIGHT CHAIN; COMPND 7 CHAIN: L, Y; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR SUBUNIT COMPND 11 ALPHA; COMPND 12 CHAIN: R; COMPND 13 SYNONYM: FC-EPSILON RI-ALPHA,FCERI,IGE FC RECEPTOR SUBUNIT ALPHA; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: FCER1A, FCE1A; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IGE, FC RECEPTOR, ALLERGY, ANTIBODY, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR G.R.ANDERSEN,R.K.JENSEN JRNL AUTH G.R.ANDERSEN,R.K.JENSEN JRNL TITL STRUCTURE OF IGE HMM5 BOUND TO FCERIA CRYO-EM CLASS 8 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 6.90 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) : 6.900 REMARK 3 NUMBER OF PARTICLES : 19161 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 9EQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292137316. 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 : COMPLEX OF IGE HMM5 AND THE REMARK 245 ECTODOMAIN OF FCERIA 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 : 7.50 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) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 59.16 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, R, X, Y, A, B, C, D, E, REMARK 350 AND CHAINS: F, G, I, J 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 HIS H 549 REMARK 465 HIS H 550 REMARK 465 HIS H 551 REMARK 465 LYS X 545 REMARK 465 HIS X 546 REMARK 465 HIS X 547 REMARK 465 HIS X 548 REMARK 465 HIS X 549 REMARK 465 HIS X 550 REMARK 465 HIS X 551 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 CYS X 325 CB CYS X 325 SG -0.097 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 H 237 CA - CB - SG ANGL. DEV. = 7.7 DEGREES REMARK 500 ASP H 238 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES REMARK 500 LEU H 276 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 MET H 427 CA - CB - CG ANGL. DEV. = 12.8 DEGREES REMARK 500 ASN R 50 CB - CA - C ANGL. DEV. = 20.9 DEGREES REMARK 500 ASP R 62 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES REMARK 500 ASP R 62 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 ARG R 106 CB - CG - CD ANGL. DEV. = 18.4 DEGREES REMARK 500 CYS R 107 CA - CB - SG ANGL. DEV. = 9.5 DEGREES REMARK 500 GLN R 157 CA - CB - CG ANGL. DEV. = 14.2 DEGREES REMARK 500 LEU R 165 CB - CG - CD2 ANGL. DEV. = -13.0 DEGREES REMARK 500 ASN X 165 C - N - CA ANGL. DEV. = 17.1 DEGREES REMARK 500 ASN X 165 N - CA - CB ANGL. DEV. = -13.4 DEGREES REMARK 500 ASN X 165 CB - CG - ND2 ANGL. DEV. = -15.4 DEGREES REMARK 500 LEU X 233 CA - CB - CG ANGL. DEV. = 20.6 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 ILE H 47 -62.70 -99.59 REMARK 500 ALA H 101 49.57 -93.60 REMARK 500 ALA H 193 58.07 -94.95 REMARK 500 ASP H 224 -94.76 52.11 REMARK 500 ILE H 347 -61.13 -98.01 REMARK 500 PRO H 362 79.21 -66.61 REMARK 500 SER H 453 51.12 -144.76 REMARK 500 PRO H 468 -169.18 -77.03 REMARK 500 ASN H 542 64.81 27.25 REMARK 500 ASN L 33 -10.26 -144.51 REMARK 500 ALA L 53 -10.42 64.58 REMARK 500 SER L 54 -17.28 -143.66 REMARK 500 ARG L 111 -96.58 -164.30 REMARK 500 GLU L 146 92.92 -65.59 REMARK 500 ASN R 30 52.47 -92.35 REMARK 500 ASN R 42 -12.64 64.29 REMARK 500 GLU R 47 35.28 -80.62 REMARK 500 ASN R 57 83.77 36.82 REMARK 500 HIS R 70 -165.47 -118.29 REMARK 500 GLU R 75 -168.58 -106.15 REMARK 500 ASP R 86 -172.30 -174.04 REMARK 500 GLU R 99 140.10 -28.12 REMARK 500 GLN R 157 -4.68 79.24 REMARK 500 ILE X 47 -62.19 -98.88 REMARK 500 ALA X 101 49.63 -93.68 REMARK 500 ALA X 138 64.60 38.56 REMARK 500 ASN X 165 -84.70 -66.45 REMARK 500 ALA X 193 57.50 -96.17 REMARK 500 ASP X 224 -64.30 58.07 REMARK 500 PHE X 225 61.15 63.78 REMARK 500 SER X 235 154.38 -49.39 REMARK 500 ASP X 327 46.03 -97.58 REMARK 500 SER X 328 -8.27 59.31 REMARK 500 PRO X 362 28.62 -78.10 REMARK 500 SER X 540 58.85 -103.27 REMARK 500 ALA Y 53 -10.03 68.63 REMARK 500 SER Y 54 -18.30 -142.38 REMARK 500 VAL Y 97 77.00 55.79 REMARK 500 ASN Y 141 63.39 61.48 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 SER X 236 CYS X 237 149.99 REMARK 500 ILE X 261 ASN X 262 142.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ASN R 50 0.07 SIDE CHAIN REMARK 500 ASN X 165 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-16377 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-19895 RELATED DB: EMDB REMARK 900 STRUCTURE OF IGE HMM5 BOUND TO FCERIA CRYO-EM CLASS 8 DBREF 9EQ3 H 1 551 PDB 9EQ3 9EQ3 1 551 DBREF 9EQ3 L 1 217 PDB 9EQ3 9EQ3 1 217 DBREF 9EQ3 R 4 174 UNP P12319 FCERA_HUMAN 29 199 DBREF 9EQ3 X 1 551 PDB 9EQ3 9EQ3 1 551 DBREF 9EQ3 Y 1 217 PDB 9EQ3 9EQ3 1 217 SEQRES 1 H 551 GLN SER LEU GLU GLU SER GLY GLY ARG LEU VAL THR PRO SEQRES 2 H 551 GLY THR PRO LEU THR LEU THR CYS THR VAL SER GLY PHE SEQRES 3 H 551 SER LEU SER THR TYR ASN ILE HIS TRP VAL ARG GLN ALA SEQRES 4 H 551 PRO GLY LYS GLY LEU GLU TRP ILE GLY VAL ILE ASP THR SEQRES 5 H 551 GLY GLY GLY THR TYR PHE ALA SER TRP ALA LYS GLY ARG SEQRES 6 H 551 PHE ALA ILE SER LYS THR SER SER THR THR VAL ASP LEU SEQRES 7 H 551 LYS MET THR SER LEU THR ALA ALA ASP THR ALA THR TYR SEQRES 8 H 551 PHE CYS ALA LYS GLY PHE ASP TYR SER ALA SER THR ASN SEQRES 9 H 551 LEU TRP GLY PRO GLY THR LEU VAL THR ILE SER SER ALA SEQRES 10 H 551 SER THR GLN SER PRO SER VAL PHE PRO LEU THR ARG CYS SEQRES 11 H 551 CYS LYS ASN ILE PRO SER ASN ALA THR SER VAL THR LEU SEQRES 12 H 551 GLY CYS LEU ALA THR GLY TYR PHE PRO GLU PRO VAL MET SEQRES 13 H 551 VAL THR TRP ASP THR GLY SER LEU ASN GLY THR THR MET SEQRES 14 H 551 THR LEU PRO ALA THR THR LEU THR LEU SER GLY HIS TYR SEQRES 15 H 551 ALA THR ILE SER LEU LEU THR VAL SER GLY ALA TRP ALA SEQRES 16 H 551 LYS GLN MET PHE THR CYS ARG VAL ALA HIS THR PRO SER SEQRES 17 H 551 SER THR ASP TRP VAL ASP ASN LYS THR PHE SER VAL CYS SEQRES 18 H 551 SER ARG ASP PHE THR PRO PRO THR VAL LYS ILE LEU GLN SEQRES 19 H 551 SER SER CYS ASP GLY GLY GLY HIS PHE PRO PRO THR ILE SEQRES 20 H 551 GLN LEU LEU CYS LEU VAL SER GLY TYR THR PRO GLY THR SEQRES 21 H 551 ILE ASN ILE THR TRP LEU GLU ASP GLY GLN VAL MET ASP SEQRES 22 H 551 VAL ASP LEU SER THR ALA SER THR THR GLN GLU GLY GLU SEQRES 23 H 551 LEU ALA SER THR GLN SER GLU LEU THR LEU SER GLN LYS SEQRES 24 H 551 HIS TRP LEU SER ASP ARG THR TYR THR CYS GLN VAL THR SEQRES 25 H 551 TYR GLN GLY HIS THR PHE GLU ASP SER THR LYS LYS CYS SEQRES 26 H 551 ALA ASP SER ASN PRO ARG GLY VAL SER ALA TYR LEU SER SEQRES 27 H 551 ARG PRO SER PRO PHE ASP LEU PHE ILE ARG LYS SER PRO SEQRES 28 H 551 THR ILE THR CYS LEU VAL VAL ASP LEU ALA PRO SER LYS SEQRES 29 H 551 GLY THR VAL ASN LEU THR TRP SER ARG ALA SER GLY LYS SEQRES 30 H 551 PRO VAL ASN HIS SER THR ARG LYS GLU GLU LYS GLN ARG SEQRES 31 H 551 ASN GLY THR LEU THR VAL THR SER THR LEU PRO VAL GLY SEQRES 32 H 551 THR ARG ASP TRP ILE GLU GLY GLU THR TYR GLN CYS ARG SEQRES 33 H 551 VAL THR HIS PRO HIS LEU PRO ARG ALA LEU MET ARG SER SEQRES 34 H 551 THR THR LYS THR SER GLY PRO ARG ALA ALA PRO GLU VAL SEQRES 35 H 551 TYR ALA PHE ALA THR PRO GLU TRP PRO GLY SER ARG ASP SEQRES 36 H 551 LYS ARG THR LEU ALA CYS LEU ILE GLN ASN PHE MET PRO SEQRES 37 H 551 GLU ASP ILE SER VAL GLN TRP LEU HIS ASN GLU VAL GLN SEQRES 38 H 551 LEU PRO ASP ALA ARG HIS SER THR THR GLN PRO ARG LYS SEQRES 39 H 551 THR LYS GLY SER GLY PHE PHE VAL PHE SER ARG LEU GLU SEQRES 40 H 551 VAL THR ARG ALA GLU TRP GLU GLN LYS ASP GLU PHE ILE SEQRES 41 H 551 CYS ARG ALA VAL HIS GLU ALA ALA SER PRO SER GLN THR SEQRES 42 H 551 VAL GLN ARG ALA VAL SER SER VAL ASN PRO GLY LYS HIS SEQRES 43 H 551 HIS HIS HIS HIS HIS SEQRES 1 L 217 GLU LEU ASP MET THR GLN THR PRO SER SER VAL SER ALA SEQRES 2 L 217 PRO VAL GLY GLY SER VAL THR ILE ASN CYS GLN SER SER SEQRES 3 L 217 GLN SER VAL TYR GLY ASN ASN TYR LEU ALA TRP TYR GLN SEQRES 4 L 217 GLN LYS ALA GLY GLN PRO PRO LYS LEU LEU ILE TYR ARG SEQRES 5 L 217 ALA SER THR LEU ALA SER GLY ALA PRO SER ARG PHE LYS SEQRES 6 L 217 GLY SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER SEQRES 7 L 217 ASP LEU GLU SER ASP ASP ALA ALA THR TYR TYR CYS LEU SEQRES 8 L 217 GLY TYR TYR ASN GLY VAL ILE ASN VAL PHE GLY GLY GLY SEQRES 9 L 217 THR ASN VAL GLU ILE LYS ARG THR VAL GLY ALA PRO SER SEQRES 10 L 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 L 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 L 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 L 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 L 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 L 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 L 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 L 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 R 171 LYS PRO LYS VAL SER LEU ASN PRO PRO TRP ASN ARG ILE SEQRES 2 R 171 PHE LYS GLY GLU ASN VAL THR LEU THR CYS ASN GLY ASN SEQRES 3 R 171 ASN PHE PHE GLU VAL SER SER THR LYS TRP PHE HIS ASN SEQRES 4 R 171 GLY SER LEU SER GLU GLU THR ASN SER SER LEU ASN ILE SEQRES 5 R 171 VAL ASN ALA LYS PHE GLU ASP SER GLY GLU TYR LYS CYS SEQRES 6 R 171 GLN HIS GLN GLN VAL ASN GLU SER GLU PRO VAL TYR LEU SEQRES 7 R 171 GLU VAL PHE SER ASP TRP LEU LEU LEU GLN ALA SER ALA SEQRES 8 R 171 GLU VAL VAL MET GLU GLY GLN PRO LEU PHE LEU ARG CYS SEQRES 9 R 171 HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS VAL ILE TYR SEQRES 10 R 171 TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP TYR GLU ASN SEQRES 11 R 171 HIS ASN ILE SER ILE THR ASN ALA THR VAL GLU ASP SER SEQRES 12 R 171 GLY THR TYR TYR CYS THR GLY LYS VAL TRP GLN LEU ASP SEQRES 13 R 171 TYR GLU SER GLU PRO LEU ASN ILE THR VAL ILE LYS ALA SEQRES 14 R 171 PRO ARG SEQRES 1 X 551 GLN SER LEU GLU GLU SER GLY GLY ARG LEU VAL THR PRO SEQRES 2 X 551 GLY THR PRO LEU THR LEU THR CYS THR VAL SER GLY PHE SEQRES 3 X 551 SER LEU SER THR TYR ASN ILE HIS TRP VAL ARG GLN ALA SEQRES 4 X 551 PRO GLY LYS GLY LEU GLU TRP ILE GLY VAL ILE ASP THR SEQRES 5 X 551 GLY GLY GLY THR TYR PHE ALA SER TRP ALA LYS GLY ARG SEQRES 6 X 551 PHE ALA ILE SER LYS THR SER SER THR THR VAL ASP LEU SEQRES 7 X 551 LYS MET THR SER LEU THR ALA ALA ASP THR ALA THR TYR SEQRES 8 X 551 PHE CYS ALA LYS GLY PHE ASP TYR SER ALA SER THR ASN SEQRES 9 X 551 LEU TRP GLY PRO GLY THR LEU VAL THR ILE SER SER ALA SEQRES 10 X 551 SER THR GLN SER PRO SER VAL PHE PRO LEU THR ARG CYS SEQRES 11 X 551 CYS LYS ASN ILE PRO SER ASN ALA THR SER VAL THR LEU SEQRES 12 X 551 GLY CYS LEU ALA THR GLY TYR PHE PRO GLU PRO VAL MET SEQRES 13 X 551 VAL THR TRP ASP THR GLY SER LEU ASN GLY THR THR MET SEQRES 14 X 551 THR LEU PRO ALA THR THR LEU THR LEU SER GLY HIS TYR SEQRES 15 X 551 ALA THR ILE SER LEU LEU THR VAL SER GLY ALA TRP ALA SEQRES 16 X 551 LYS GLN MET PHE THR CYS ARG VAL ALA HIS THR PRO SER SEQRES 17 X 551 SER THR ASP TRP VAL ASP ASN LYS THR PHE SER VAL CYS SEQRES 18 X 551 SER ARG ASP PHE THR PRO PRO THR VAL LYS ILE LEU GLN SEQRES 19 X 551 SER SER CYS ASP GLY GLY GLY HIS PHE PRO PRO THR ILE SEQRES 20 X 551 GLN LEU LEU CYS LEU VAL SER GLY TYR THR PRO GLY THR SEQRES 21 X 551 ILE ASN ILE THR TRP LEU GLU ASP GLY GLN VAL MET ASP SEQRES 22 X 551 VAL ASP LEU SER THR ALA SER THR THR GLN GLU GLY GLU SEQRES 23 X 551 LEU ALA SER THR GLN SER GLU LEU THR LEU SER GLN LYS SEQRES 24 X 551 HIS TRP LEU SER ASP ARG THR TYR THR CYS GLN VAL THR SEQRES 25 X 551 TYR GLN GLY HIS THR PHE GLU ASP SER THR LYS LYS CYS SEQRES 26 X 551 ALA ASP SER ASN PRO ARG GLY VAL SER ALA TYR LEU SER SEQRES 27 X 551 ARG PRO SER PRO PHE ASP LEU PHE ILE ARG LYS SER PRO SEQRES 28 X 551 THR ILE THR CYS LEU VAL VAL ASP LEU ALA PRO SER LYS SEQRES 29 X 551 GLY THR VAL ASN LEU THR TRP SER ARG ALA SER GLY LYS SEQRES 30 X 551 PRO VAL ASN HIS SER THR ARG LYS GLU GLU LYS GLN ARG SEQRES 31 X 551 ASN GLY THR LEU THR VAL THR SER THR LEU PRO VAL GLY SEQRES 32 X 551 THR ARG ASP TRP ILE GLU GLY GLU THR TYR GLN CYS ARG SEQRES 33 X 551 VAL THR HIS PRO HIS LEU PRO ARG ALA LEU MET ARG SER SEQRES 34 X 551 THR THR LYS THR SER GLY PRO ARG ALA ALA PRO GLU VAL SEQRES 35 X 551 TYR ALA PHE ALA THR PRO GLU TRP PRO GLY SER ARG ASP SEQRES 36 X 551 LYS ARG THR LEU ALA CYS LEU ILE GLN ASN PHE MET PRO SEQRES 37 X 551 GLU ASP ILE SER VAL GLN TRP LEU HIS ASN GLU VAL GLN SEQRES 38 X 551 LEU PRO ASP ALA ARG HIS SER THR THR GLN PRO ARG LYS SEQRES 39 X 551 THR LYS GLY SER GLY PHE PHE VAL PHE SER ARG LEU GLU SEQRES 40 X 551 VAL THR ARG ALA GLU TRP GLU GLN LYS ASP GLU PHE ILE SEQRES 41 X 551 CYS ARG ALA VAL HIS GLU ALA ALA SER PRO SER GLN THR SEQRES 42 X 551 VAL GLN ARG ALA VAL SER SER VAL ASN PRO GLY LYS HIS SEQRES 43 X 551 HIS HIS HIS HIS HIS SEQRES 1 Y 217 GLU LEU ASP MET THR GLN THR PRO SER SER VAL SER ALA SEQRES 2 Y 217 PRO VAL GLY GLY SER VAL THR ILE ASN CYS GLN SER SER SEQRES 3 Y 217 GLN SER VAL TYR GLY ASN ASN TYR LEU ALA TRP TYR GLN SEQRES 4 Y 217 GLN LYS ALA GLY GLN PRO PRO LYS LEU LEU ILE TYR ARG SEQRES 5 Y 217 ALA SER THR LEU ALA SER GLY ALA PRO SER ARG PHE LYS SEQRES 6 Y 217 GLY SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER SEQRES 7 Y 217 ASP LEU GLU SER ASP ASP ALA ALA THR TYR TYR CYS LEU SEQRES 8 Y 217 GLY TYR TYR ASN GLY VAL ILE ASN VAL PHE GLY GLY GLY SEQRES 9 Y 217 THR ASN VAL GLU ILE LYS ARG THR VAL GLY ALA PRO SER SEQRES 10 Y 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 Y 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 Y 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 Y 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 Y 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 Y 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 Y 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 Y 217 THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG H 601 14 HET NAG H 602 14 HET NAG H 603 14 HET NAG H 604 14 HET NAG X 601 14 HET NAG X 602 14 HET NAG X 603 14 HET NAG X 604 14 HET NAG A 1 14 HET NAG A 2 14 HET BMA A 3 11 HET MAN A 4 11 HET MAN A 5 11 HET NAG B 1 14 HET NAG B 2 14 HET MAN B 3 11 HET MAN B 4 11 HET MAN B 5 11 HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET MAN E 4 11 HET MAN E 5 11 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET MAN J 4 11 HET MAN J 5 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 6 NAG 26(C8 H15 N O6) FORMUL 14 BMA 7(C6 H12 O6) FORMUL 14 MAN 9(C6 H12 O6) HELIX 1 AA1 THR H 84 THR H 88 5 5 HELIX 2 AA2 CYS H 130 ILE H 134 5 5 HELIX 3 AA3 ASP H 273 ASP H 275 5 3 HELIX 4 AA4 GLN H 298 SER H 303 1 6 HELIX 5 AA5 SER H 341 ILE H 347 1 7 HELIX 6 AA6 GLY H 403 GLU H 409 1 7 HELIX 7 AA7 PRO H 483 ALA H 485 5 3 HELIX 8 AA8 ARG H 510 LYS H 516 1 7 HELIX 9 AA9 VAL L 29 ASN L 33 5 5 HELIX 10 AB1 GLU L 81 ALA L 85 5 5 HELIX 11 AB2 SER L 124 LYS L 129 1 6 HELIX 12 AB3 LYS L 186 LYS L 191 1 6 HELIX 13 AB4 LYS R 59 SER R 63 5 5 HELIX 14 AB5 ARG R 111 TRP R 113 5 3 HELIX 15 AB6 THR R 142 SER R 146 5 5 HELIX 16 AB7 THR X 84 THR X 88 5 5 HELIX 17 AB8 ASP X 273 ASP X 275 5 3 HELIX 18 AB9 GLN X 298 SER X 303 1 6 HELIX 19 AC1 SER X 341 ILE X 347 1 7 HELIX 20 AC2 GLY X 403 GLU X 409 1 7 HELIX 21 AC3 PRO X 483 ALA X 485 5 3 HELIX 22 AC4 ARG X 510 LYS X 516 1 7 HELIX 23 AC5 VAL Y 29 ASN Y 33 5 5 HELIX 24 AC6 GLU Y 81 ALA Y 85 5 5 HELIX 25 AC7 SER Y 124 LYS Y 129 1 6 HELIX 26 AC8 LYS Y 186 LYS Y 191 1 6 SHEET 1 AA1 4 SER H 2 SER H 6 0 SHEET 2 AA1 4 LEU H 17 SER H 24 -1 O THR H 20 N SER H 6 SHEET 3 AA1 4 THR H 75 MET H 80 -1 O VAL H 76 N CYS H 21 SHEET 4 AA1 4 PHE H 66 LYS H 70 -1 N ALA H 67 O LYS H 79 SHEET 1 AA2 5 THR H 56 PHE H 58 0 SHEET 2 AA2 5 GLU H 45 ILE H 50 -1 N VAL H 49 O TYR H 57 SHEET 3 AA2 5 ASN H 32 GLN H 38 -1 N ARG H 37 O GLU H 45 SHEET 4 AA2 5 ALA H 89 GLY H 96 -1 O THR H 90 N GLN H 38 SHEET 5 AA2 5 THR H 110 VAL H 112 -1 O VAL H 112 N ALA H 89 SHEET 1 AA3 4 SER H 123 LEU H 127 0 SHEET 2 AA3 4 SER H 140 TYR H 150 -1 O GLY H 144 N LEU H 127 SHEET 3 AA3 4 TYR H 182 SER H 191 -1 O TYR H 182 N TYR H 150 SHEET 4 AA3 4 GLY H 166 THR H 170 -1 N MET H 169 O LEU H 187 SHEET 1 AA4 4 SER H 123 LEU H 127 0 SHEET 2 AA4 4 SER H 140 TYR H 150 -1 O GLY H 144 N LEU H 127 SHEET 3 AA4 4 TYR H 182 SER H 191 -1 O TYR H 182 N TYR H 150 SHEET 4 AA4 4 THR H 174 THR H 175 -1 N THR H 174 O ALA H 183 SHEET 1 AA5 3 MET H 156 ASP H 160 0 SHEET 2 AA5 3 PHE H 199 ALA H 204 -1 O THR H 200 N ASP H 160 SHEET 3 AA5 3 VAL H 213 PHE H 218 -1 O PHE H 218 N PHE H 199 SHEET 1 AA6 8 SER H 277 GLU H 284 0 SHEET 2 AA6 8 LEU H 287 SER H 297 -1 O LEU H 287 N GLU H 284 SHEET 3 AA6 8 THR H 246 TYR H 256 -1 N VAL H 253 O THR H 290 SHEET 4 AA6 8 VAL H 230 SER H 235 -1 N LYS H 231 O LEU H 252 SHEET 5 AA6 8 THR X 229 SER X 235 -1 O GLN X 234 N GLN H 234 SHEET 6 AA6 8 THR X 246 TYR X 256 -1 O LEU X 252 N LYS X 231 SHEET 7 AA6 8 LEU X 287 SER X 297 -1 O ALA X 288 N TYR X 256 SHEET 8 AA6 8 SER X 277 GLU X 284 -1 N THR X 282 O SER X 289 SHEET 1 AA7 4 GLN H 270 VAL H 271 0 SHEET 2 AA7 4 ILE H 261 GLU H 267 -1 N GLU H 267 O GLN H 270 SHEET 3 AA7 4 TYR H 307 TYR H 313 -1 O GLN H 310 N THR H 264 SHEET 4 AA7 4 HIS H 316 THR H 322 -1 O HIS H 316 N TYR H 313 SHEET 1 AA8 4 SER H 334 LEU H 337 0 SHEET 2 AA8 4 THR H 352 LEU H 360 -1 O VAL H 358 N SER H 334 SHEET 3 AA8 4 LEU H 394 PRO H 401 -1 O VAL H 396 N VAL H 357 SHEET 4 AA8 4 THR H 383 LYS H 388 -1 N GLU H 387 O THR H 395 SHEET 1 AA9 3 ASN H 368 ARG H 373 0 SHEET 2 AA9 3 TYR H 413 THR H 418 -1 O GLN H 414 N SER H 372 SHEET 3 AA9 3 LEU H 426 THR H 430 -1 O LEU H 426 N VAL H 417 SHEET 1 AB1 4 GLU H 441 ALA H 446 0 SHEET 2 AB1 4 LYS H 456 PHE H 466 -1 O GLN H 464 N GLU H 441 SHEET 3 AB1 4 PHE H 500 THR H 509 -1 O VAL H 508 N ARG H 457 SHEET 4 AB1 4 HIS H 487 THR H 489 -1 N SER H 488 O ARG H 505 SHEET 1 AB2 4 GLU H 441 ALA H 446 0 SHEET 2 AB2 4 LYS H 456 PHE H 466 -1 O GLN H 464 N GLU H 441 SHEET 3 AB2 4 PHE H 500 THR H 509 -1 O VAL H 508 N ARG H 457 SHEET 4 AB2 4 ARG H 493 LYS H 494 -1 N ARG H 493 O PHE H 501 SHEET 1 AB3 3 ILE H 471 HIS H 477 0 SHEET 2 AB3 3 GLU H 518 HIS H 525 -1 O ARG H 522 N GLN H 474 SHEET 3 AB3 3 THR H 533 SER H 539 -1 O VAL H 534 N ALA H 523 SHEET 1 AB4 4 MET L 4 THR L 7 0 SHEET 2 AB4 4 SER L 18 SER L 25 -1 O ASN L 22 N THR L 7 SHEET 3 AB4 4 GLN L 72 SER L 78 -1 O LEU L 75 N ILE L 21 SHEET 4 AB4 4 PHE L 64 SER L 69 -1 N LYS L 65 O THR L 76 SHEET 1 AB5 5 THR L 55 LEU L 56 0 SHEET 2 AB5 5 LYS L 47 TYR L 51 -1 N TYR L 51 O THR L 55 SHEET 3 AB5 5 LEU L 35 GLN L 40 -1 N GLN L 39 O LYS L 47 SHEET 4 AB5 5 THR L 87 TYR L 94 -1 O THR L 87 N GLN L 40 SHEET 5 AB5 5 ILE L 98 PHE L 101 -1 O VAL L 100 N GLY L 92 SHEET 1 AB6 4 SER L 117 PHE L 121 0 SHEET 2 AB6 4 THR L 132 PHE L 142 -1 O LEU L 138 N PHE L 119 SHEET 3 AB6 4 TYR L 176 SER L 185 -1 O TYR L 176 N PHE L 142 SHEET 4 AB6 4 SER L 162 VAL L 166 -1 N GLN L 163 O THR L 181 SHEET 1 AB7 4 ALA L 156 LEU L 157 0 SHEET 2 AB7 4 LYS L 148 VAL L 153 -1 N VAL L 153 O ALA L 156 SHEET 3 AB7 4 VAL L 194 THR L 200 -1 O GLU L 198 N GLN L 150 SHEET 4 AB7 4 VAL L 208 ASN L 213 -1 O VAL L 208 N VAL L 199 SHEET 1 AB8 3 LYS R 6 ASN R 10 0 SHEET 2 AB8 3 VAL R 22 ASN R 27 -1 O THR R 25 N SER R 8 SHEET 3 AB8 3 SER R 52 ILE R 55 -1 O LEU R 53 N LEU R 24 SHEET 1 AB9 5 ARG R 15 PHE R 17 0 SHEET 2 AB9 5 VAL R 79 PHE R 84 1 O PHE R 84 N ILE R 16 SHEET 3 AB9 5 GLY R 64 GLN R 69 -1 N TYR R 66 O VAL R 79 SHEET 4 AB9 5 LYS R 38 HIS R 41 -1 N PHE R 40 O LYS R 67 SHEET 5 AB9 5 SER R 44 SER R 46 -1 O SER R 46 N TRP R 39 SHEET 1 AC1 3 LEU R 88 ALA R 92 0 SHEET 2 AC1 3 LEU R 103 GLY R 109 -1 O ARG R 106 N GLN R 91 SHEET 3 AC1 3 ASN R 135 ILE R 138 -1 O ILE R 136 N LEU R 105 SHEET 1 AC2 5 VAL R 96 MET R 98 0 SHEET 2 AC2 5 LEU R 165 ILE R 170 1 O ILE R 170 N VAL R 97 SHEET 3 AC2 5 GLY R 147 VAL R 155 -1 N TYR R 149 O LEU R 165 SHEET 4 AC2 5 VAL R 115 LYS R 122 -1 N TYR R 116 O LYS R 154 SHEET 5 AC2 5 GLU R 125 TRP R 130 -1 O LYS R 128 N TYR R 120 SHEET 1 AC3 4 VAL R 96 MET R 98 0 SHEET 2 AC3 4 LEU R 165 ILE R 170 1 O ILE R 170 N VAL R 97 SHEET 3 AC3 4 GLY R 147 VAL R 155 -1 N TYR R 149 O LEU R 165 SHEET 4 AC3 4 LEU R 158 GLU R 161 -1 O TYR R 160 N GLY R 153 SHEET 1 AC4 4 SER X 2 SER X 6 0 SHEET 2 AC4 4 LEU X 17 SER X 24 -1 O THR X 20 N SER X 6 SHEET 3 AC4 4 THR X 75 MET X 80 -1 O VAL X 76 N CYS X 21 SHEET 4 AC4 4 PHE X 66 LYS X 70 -1 N ALA X 67 O LYS X 79 SHEET 1 AC5 6 LEU X 10 VAL X 11 0 SHEET 2 AC5 6 THR X 110 ILE X 114 1 O THR X 113 N VAL X 11 SHEET 3 AC5 6 ALA X 89 GLY X 96 -1 N TYR X 91 O THR X 110 SHEET 4 AC5 6 ASN X 32 GLN X 38 -1 N VAL X 36 O PHE X 92 SHEET 5 AC5 6 GLU X 45 ILE X 50 -1 O GLU X 45 N ARG X 37 SHEET 6 AC5 6 THR X 56 PHE X 58 -1 O TYR X 57 N VAL X 49 SHEET 1 AC6 4 SER X 123 LEU X 127 0 SHEET 2 AC6 4 SER X 140 TYR X 150 -1 O THR X 148 N SER X 123 SHEET 3 AC6 4 TYR X 182 SER X 191 -1 O TYR X 182 N TYR X 150 SHEET 4 AC6 4 THR X 167 THR X 170 -1 N MET X 169 O LEU X 187 SHEET 1 AC7 4 SER X 123 LEU X 127 0 SHEET 2 AC7 4 SER X 140 TYR X 150 -1 O THR X 148 N SER X 123 SHEET 3 AC7 4 TYR X 182 SER X 191 -1 O TYR X 182 N TYR X 150 SHEET 4 AC7 4 THR X 174 THR X 175 -1 N THR X 174 O ALA X 183 SHEET 1 AC8 3 MET X 156 ASP X 160 0 SHEET 2 AC8 3 PHE X 199 ALA X 204 -1 O THR X 200 N ASP X 160 SHEET 3 AC8 3 VAL X 213 PHE X 218 -1 O PHE X 218 N PHE X 199 SHEET 1 AC9 4 GLN X 270 VAL X 271 0 SHEET 2 AC9 4 ILE X 261 GLU X 267 -1 N GLU X 267 O GLN X 270 SHEET 3 AC9 4 TYR X 307 TYR X 313 -1 O GLN X 310 N THR X 264 SHEET 4 AC9 4 HIS X 316 THR X 322 -1 O PHE X 318 N VAL X 311 SHEET 1 AD1 4 SER X 334 LEU X 337 0 SHEET 2 AD1 4 THR X 352 LEU X 360 -1 O LEU X 356 N TYR X 336 SHEET 3 AD1 4 LEU X 394 PRO X 401 -1 O VAL X 396 N VAL X 357 SHEET 4 AD1 4 THR X 383 LYS X 388 -1 N LYS X 385 O THR X 397 SHEET 1 AD2 3 ASN X 368 ARG X 373 0 SHEET 2 AD2 3 TYR X 413 THR X 418 -1 O THR X 418 N ASN X 368 SHEET 3 AD2 3 LEU X 426 THR X 430 -1 O LEU X 426 N VAL X 417 SHEET 1 AD3 4 GLU X 441 ALA X 446 0 SHEET 2 AD3 4 LYS X 456 PHE X 466 -1 O GLN X 464 N GLU X 441 SHEET 3 AD3 4 PHE X 500 THR X 509 -1 O VAL X 508 N ARG X 457 SHEET 4 AD3 4 HIS X 487 THR X 489 -1 N SER X 488 O ARG X 505 SHEET 1 AD4 4 GLU X 441 ALA X 446 0 SHEET 2 AD4 4 LYS X 456 PHE X 466 -1 O GLN X 464 N GLU X 441 SHEET 3 AD4 4 PHE X 500 THR X 509 -1 O VAL X 508 N ARG X 457 SHEET 4 AD4 4 ARG X 493 LYS X 494 -1 N ARG X 493 O PHE X 501 SHEET 1 AD5 4 VAL X 480 GLN X 481 0 SHEET 2 AD5 4 ILE X 471 HIS X 477 -1 N HIS X 477 O VAL X 480 SHEET 3 AD5 4 PHE X 519 HIS X 525 -1 O VAL X 524 N SER X 472 SHEET 4 AD5 4 THR X 533 VAL X 538 -1 O VAL X 534 N ALA X 523 SHEET 1 AD6 4 MET Y 4 THR Y 7 0 SHEET 2 AD6 4 VAL Y 19 SER Y 25 -1 O ASN Y 22 N THR Y 7 SHEET 3 AD6 4 GLN Y 72 ILE Y 77 -1 O LEU Y 75 N ILE Y 21 SHEET 4 AD6 4 PHE Y 64 SER Y 69 -1 N SER Y 67 O THR Y 74 SHEET 1 AD7 6 SER Y 10 ALA Y 13 0 SHEET 2 AD7 6 THR Y 105 ILE Y 109 1 O GLU Y 108 N VAL Y 11 SHEET 3 AD7 6 THR Y 87 TYR Y 94 -1 N TYR Y 88 O THR Y 105 SHEET 4 AD7 6 LEU Y 35 GLN Y 40 -1 N GLN Y 40 O THR Y 87 SHEET 5 AD7 6 LYS Y 47 TYR Y 51 -1 O LYS Y 47 N GLN Y 39 SHEET 6 AD7 6 THR Y 55 LEU Y 56 -1 O THR Y 55 N TYR Y 51 SHEET 1 AD8 4 SER Y 10 ALA Y 13 0 SHEET 2 AD8 4 THR Y 105 ILE Y 109 1 O GLU Y 108 N VAL Y 11 SHEET 3 AD8 4 THR Y 87 TYR Y 94 -1 N TYR Y 88 O THR Y 105 SHEET 4 AD8 4 ILE Y 98 PHE Y 101 -1 O VAL Y 100 N GLY Y 92 SHEET 1 AD9 4 SER Y 117 PHE Y 121 0 SHEET 2 AD9 4 THR Y 132 PHE Y 142 -1 O LEU Y 138 N PHE Y 119 SHEET 3 AD9 4 TYR Y 176 SER Y 185 -1 O LEU Y 178 N LEU Y 139 SHEET 4 AD9 4 SER Y 162 VAL Y 166 -1 N GLN Y 163 O THR Y 181 SHEET 1 AE1 4 ALA Y 156 LEU Y 157 0 SHEET 2 AE1 4 ALA Y 147 VAL Y 153 -1 N VAL Y 153 O ALA Y 156 SHEET 3 AE1 4 VAL Y 194 HIS Y 201 -1 O GLU Y 198 N GLN Y 150 SHEET 4 AE1 4 VAL Y 208 ASN Y 213 -1 O VAL Y 208 N VAL Y 199 SSBOND 1 CYS H 21 CYS H 93 1555 1555 2.03 SSBOND 2 CYS H 130 CYS L 217 1555 1555 2.03 SSBOND 3 CYS H 131 CYS H 221 1555 1555 2.05 SSBOND 4 CYS H 145 CYS H 201 1555 1555 2.03 SSBOND 5 CYS H 237 CYS X 325 1555 1555 2.08 SSBOND 6 CYS H 251 CYS H 309 1555 1555 2.04 SSBOND 7 CYS H 325 CYS X 237 1555 1555 2.06 SSBOND 8 CYS H 355 CYS H 415 1555 1555 2.04 SSBOND 9 CYS H 461 CYS H 521 1555 1555 2.04 SSBOND 10 CYS L 23 CYS L 90 1555 1555 2.03 SSBOND 11 CYS L 137 CYS L 197 1555 1555 2.03 SSBOND 12 CYS R 26 CYS R 68 1555 1555 2.03 SSBOND 13 CYS R 107 CYS R 151 1555 1555 2.04 SSBOND 14 CYS X 21 CYS X 93 1555 1555 2.03 SSBOND 15 CYS X 130 CYS Y 217 1555 1555 2.04 SSBOND 16 CYS X 131 CYS X 221 1555 1555 2.03 SSBOND 17 CYS X 145 CYS X 201 1555 1555 2.03 SSBOND 18 CYS X 251 CYS X 309 1555 1555 2.04 SSBOND 19 CYS X 355 CYS X 415 1555 1555 2.03 SSBOND 20 CYS X 461 CYS X 521 1555 1555 2.04 SSBOND 21 CYS Y 23 CYS Y 90 1555 1555 2.03 SSBOND 22 CYS Y 137 CYS Y 197 1555 1555 2.03 LINK ND2 ASN H 137 C1 NAG H 603 1555 1555 1.43 LINK ND2 ASN H 165 C1 NAG H 601 1555 1555 1.44 LINK ND2 ASN H 215 C1 NAG H 602 1555 1555 1.44 LINK ND2 ASN H 262 C1 NAG H 604 1555 1555 1.48 LINK ND2 ASN H 391 C1 NAG A 1 1555 1555 1.44 LINK ND2 ASN R 21 C1 NAG E 1 1555 1555 1.47 LINK ND2 ASN R 42 C1 NAG B 1 1555 1555 1.48 LINK ND2 ASN R 50 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN R 74 C1 NAG C 1 1555 1555 1.45 LINK ND2 ASN R 135 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN R 140 C1 NAG I 1 1555 1555 1.42 LINK ND2 ASN R 166 C1 NAG F 1 1555 1555 1.42 LINK ND2 ASN X 137 C1 NAG X 601 1555 1555 1.45 LINK ND2 ASN X 165 C1 NAG X 604 1555 1555 1.41 LINK ND2 ASN X 215 C1 NAG X 602 1555 1555 1.45 LINK ND2 ASN X 262 C1 NAG X 603 1555 1555 1.44 LINK ND2 ASN X 391 C1 NAG J 1 1555 1555 1.47 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.44 LINK O4 NAG A 2 C1 BMA A 3 1555 1555 1.45 LINK O3 BMA A 3 C1 MAN A 4 1555 1555 1.44 LINK O6 BMA A 3 C1 MAN A 5 1555 1555 1.44 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.47 LINK O3 MAN B 3 C1 MAN B 4 1555 1555 1.44 LINK O6 MAN B 3 C1 MAN B 5 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.48 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.47 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.48 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.46 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.46 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.47 LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.47 LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.47 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.48 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.46 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45 LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.44 LINK O6 BMA J 3 C1 MAN J 5 1555 1555 1.44 CISPEP 1 PHE H 151 PRO H 152 0 -12.39 CISPEP 2 GLU H 153 PRO H 154 0 -3.98 CISPEP 3 MET H 467 PRO H 468 0 -2.44 CISPEP 4 SER H 529 PRO H 530 0 -3.86 CISPEP 5 THR L 7 PRO L 8 0 -5.46 CISPEP 6 TYR L 143 PRO L 144 0 15.29 CISPEP 7 ASN R 10 PRO R 11 0 -3.86 CISPEP 8 PHE X 151 PRO X 152 0 -11.81 CISPEP 9 GLU X 153 PRO X 154 0 -3.41 CISPEP 10 MET X 467 PRO X 468 0 -3.65 CISPEP 11 SER X 529 PRO X 530 0 5.18 CISPEP 12 THR Y 7 PRO Y 8 0 -4.64 CISPEP 13 TYR Y 143 PRO Y 144 0 -5.55 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