HEADER VIRAL PROTEIN/IMMUNE SYSTEM 02-APR-23 8SB4 TITLE CRYOEM STRUCTURE OF DH270.1-CH848.10.17 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CH848.10.17 GP120; COMPND 3 CHAIN: A, F, K; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CH848.10.17 GP41; COMPND 7 CHAIN: B, G, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: DH270.1 VARIABLE HEAVY CHAIN; COMPND 11 CHAIN: C, H, M; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: DH270.1 VARIABLE LIGHT CHAIN; COMPND 15 CHAIN: D, I, N; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HIV-1 06TG.HT008; SOURCE 3 ORGANISM_TAXID: 587638; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HIV-1 06TG.HT008; SOURCE 9 ORGANISM_TAXID: 587638; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, ANTIBODY, DH270.1, CH848.10.17, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.HENDERSON,Y.ZHOU,V.STALLS,B.BARTESAGHI,P.ACHARYA JRNL AUTH R.HENDERSON,Y.ZHOU,V.STALLS,K.WIEHE,K.O.SAUNDERS,K.WAGH, JRNL AUTH 2 K.ANASTI,M.BARR,R.PARKS,S.M.ALAM,B.KORBER,B.F.HAYNES, JRNL AUTH 3 A.BARTESAGHI,P.ACHARYA JRNL TITL STRUCTURAL BASIS FOR BREADTH DEVELOPMENT IN A HIV-1 JRNL TITL 2 NEUTRALIZING ANTIBODY JRNL REF BIORXIV 2022 JRNL REFN ISSN 2692-8205 JRNL DOI 10.1101/2022.09.14.507935 REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LATITUDE 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) : 3.600 REMARK 3 NUMBER OF PARTICLES : 125676 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 8SB4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000273320. 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 : DH270.UCA.G57R-CH848.10.17DT REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.50 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.20 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) : 700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 4100.00 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) : 60.00 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, G, H, I, K, L, REMARK 350 AND CHAINS: M, N, E, J, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X 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 ALA A 31 REMARK 465 ALA F 31 REMARK 465 ALA K 31 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 OG1 THR D 5 OG1 THR D 23 2.07 REMARK 500 OG1 THR N 5 OG1 THR N 23 2.07 REMARK 500 OG1 THR I 5 OG1 THR I 23 2.09 REMARK 500 O THR M 30 OG SER M 54 2.10 REMARK 500 O THR C 30 OG SER C 54 2.12 REMARK 500 O ILE A 491 NH2 ARG B 585 2.13 REMARK 500 OD1 ASN H 52 OG SER H 54 2.18 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 F 247 CA - CB - SG ANGL. DEV. = 9.0 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 LYS A 121 45.76 -92.99 REMARK 500 LEU A 122 -132.37 34.71 REMARK 500 THR A 123 -42.81 103.33 REMARK 500 ALA A 134 -179.40 64.69 REMARK 500 GLU A 153 173.14 65.97 REMARK 500 ARG A 166 -97.74 55.13 REMARK 500 ASP A 167 49.67 -85.11 REMARK 500 CYS A 196 -5.09 73.66 REMARK 500 THR A 257 -61.01 -94.11 REMARK 500 ASN A 262 119.42 -29.12 REMARK 500 LEU B 602 -59.79 -124.07 REMARK 500 ALA D 3 -39.51 -132.59 REMARK 500 SER D 9 147.94 -170.36 REMARK 500 VAL D 53 -26.21 62.81 REMARK 500 ASN D 54 13.65 -141.98 REMARK 500 ASN F 88 22.97 -140.79 REMARK 500 LYS F 121 45.95 -93.20 REMARK 500 LEU F 122 -133.10 34.89 REMARK 500 THR F 123 -43.79 102.41 REMARK 500 ALA F 134 -173.40 65.40 REMARK 500 LYS F 137 -3.15 69.17 REMARK 500 GLU F 153 176.61 60.74 REMARK 500 ARG F 166 -96.30 53.04 REMARK 500 ASP F 167 49.95 -84.63 REMARK 500 CYS F 196 -8.46 78.03 REMARK 500 THR F 257 -61.30 -94.31 REMARK 500 ASN F 262 119.95 -33.45 REMARK 500 LEU G 602 -61.07 -123.95 REMARK 500 ALA I 3 -39.43 -134.67 REMARK 500 ASP I 28 -60.26 -101.05 REMARK 500 VAL I 53 -22.54 62.38 REMARK 500 ASN I 54 19.15 -143.38 REMARK 500 LYS K 121 45.70 -93.09 REMARK 500 LEU K 122 -133.31 34.51 REMARK 500 THR K 123 -40.75 102.50 REMARK 500 ALA K 134 -174.35 66.33 REMARK 500 LYS K 137 -2.47 68.84 REMARK 500 GLU K 153 176.12 61.01 REMARK 500 ARG K 166 -96.51 54.61 REMARK 500 ASN K 195 -167.77 -100.92 REMARK 500 CYS K 196 -8.68 79.47 REMARK 500 THR K 257 -60.92 -94.62 REMARK 500 ASN K 262 118.71 -28.17 REMARK 500 PHE L 519 19.67 -140.59 REMARK 500 LEU L 602 -59.64 -125.12 REMARK 500 ALA N 3 -39.46 -132.62 REMARK 500 VAL N 53 -26.27 62.55 REMARK 500 ASN N 54 20.26 -142.68 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 GLY A 431 ARG A 432 -148.67 REMARK 500 GLY F 431 ARG F 432 -148.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-40282 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40283 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40285 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40286 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40287 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40288 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40291 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40290 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40289 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40284 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40280 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40278 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40277 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40275 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40281 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40279 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40274 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-40273 RELATED DB: EMDB DBREF1 8SB4 A 34 505 UNP A0A1W6IPB2_9HIV1 DBREF2 8SB4 A A0A1W6IPB2 30 489 DBREF 8SB4 B 512 664 PDB 8SB4 8SB4 512 664 DBREF 8SB4 C 1 126 PDB 8SB4 8SB4 1 126 DBREF 8SB4 D 1 110 PDB 8SB4 8SB4 1 110 DBREF1 8SB4 F 34 505 UNP A0A1W6IPB2_9HIV1 DBREF2 8SB4 F A0A1W6IPB2 30 489 DBREF 8SB4 G 512 664 PDB 8SB4 8SB4 512 664 DBREF 8SB4 H 1 126 PDB 8SB4 8SB4 1 126 DBREF 8SB4 I 1 110 PDB 8SB4 8SB4 1 110 DBREF1 8SB4 K 34 505 UNP A0A1W6IPB2_9HIV1 DBREF2 8SB4 K A0A1W6IPB2 30 489 DBREF 8SB4 L 512 664 PDB 8SB4 8SB4 512 664 DBREF 8SB4 M 1 126 PDB 8SB4 8SB4 1 126 DBREF 8SB4 N 1 110 PDB 8SB4 8SB4 1 110 SEQADV 8SB4 ALA A 31 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 GLU A 32 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 ASN A 33 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 CYS A 201 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8SB4 CYS A 433 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8SB4 LYS A 490 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8SB4 GLU A 492 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8SB4 VAL A 496 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8SB4 ARG A 500 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8SB4 CYS A 501 UNP A0A1W6IPB ALA 485 CONFLICT SEQADV 8SB4 ALA F 31 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 GLU F 32 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 ASN F 33 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 CYS F 201 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8SB4 CYS F 433 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8SB4 LYS F 490 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8SB4 GLU F 492 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8SB4 VAL F 496 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8SB4 ARG F 500 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8SB4 CYS F 501 UNP A0A1W6IPB ALA 485 CONFLICT SEQADV 8SB4 ALA K 31 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 GLU K 32 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 ASN K 33 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8SB4 CYS K 201 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8SB4 CYS K 433 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8SB4 LYS K 490 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8SB4 GLU K 492 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8SB4 VAL K 496 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8SB4 ARG K 500 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8SB4 CYS K 501 UNP A0A1W6IPB ALA 485 CONFLICT SEQRES 1 A 463 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 463 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 A 463 ASP ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP SEQRES 4 A 463 ALA THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN SEQRES 5 A 463 GLU LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 A 463 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE SEQRES 7 A 463 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 463 LEU THR PRO LEU CYS VAL THR LEU ILE CYS SER ASN ALA SEQRES 9 A 463 THR VAL LYS ASN GLY THR VAL GLU GLU MET LYS ASN CYS SEQRES 10 A 463 SER PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS SEQRES 11 A 463 LYS GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO SEQRES 12 A 463 LEU SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE SEQRES 13 A 463 ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS SEQRES 14 A 463 VAL THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 A 463 ALA GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE SEQRES 16 A 463 ASN GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN SEQRES 17 A 463 CYS THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU SEQRES 18 A 463 LEU LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE SEQRES 19 A 463 ARG SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE SEQRES 20 A 463 VAL HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG SEQRES 21 A 463 PRO ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO SEQRES 22 A 463 GLY GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP SEQRES 23 A 463 ILE LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP SEQRES 24 A 463 ASN ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS SEQRES 25 A 463 HIS PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA SEQRES 26 A 463 GLY GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS SEQRES 27 A 463 GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE SEQRES 28 A 463 ASN GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SEQRES 29 A 463 SER ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG SEQRES 30 A 463 ILE LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG SEQRES 31 A 463 CYS MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 A 463 ARG SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 A 463 GLY THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA SEQRES 34 A 463 GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 A 463 LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA SEQRES 36 A 463 PRO THR ARG CYS LYS ARG ARG VAL SEQRES 1 B 132 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 132 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 132 THR VAL GLN ALA ARG ASN LEU LEU SER GLY THR VAL TRP SEQRES 4 B 132 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 5 B 132 ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 6 B 132 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 7 B 132 ASN SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP SEQRES 8 B 132 ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER SEQRES 9 B 132 ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER SEQRES 10 B 132 GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA SEQRES 11 B 132 LEU ASP SEQRES 1 C 126 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU MET LYS LYS SEQRES 2 C 126 PRO GLY ALA SER VAL ARG VAL SER CYS LYS ALA SER GLY SEQRES 3 C 126 TYR THR PHE THR ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 C 126 ALA PRO GLY GLN GLY PRO GLU TRP MET GLY TRP ILE ASN SEQRES 5 C 126 PRO SER THR GLY ARG THR ASN SER PRO GLN LYS PHE GLN SEQRES 6 C 126 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 C 126 ALA TYR MET ASP LEU ASN ARG LEU THR SER ASP ASP THR SEQRES 8 C 126 ALA MET TYR TYR CYS THR THR GLY GLY TRP ILE GLY LEU SEQRES 9 C 126 TYR SER ASP THR SER GLY TYR PRO ASN PHE ASP TYR TRP SEQRES 10 C 126 GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1 D 110 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 D 110 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR ASN SEQRES 3 D 110 TYR ASP VAL GLY SER TYR ASN LEU VAL SER TRP TYR GLN SEQRES 4 D 110 GLN HIS PRO GLY LYS VAL PRO LYS TYR ILE ILE TYR GLU SEQRES 5 D 110 VAL ASN LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 D 110 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 D 110 GLY LEU GLN ALA GLU ASP GLU ALA THR TYR TYR CYS CYS SEQRES 8 D 110 SER TYR ALA GLY SER SER ILE ILE PHE PHE GLY GLY GLY SEQRES 9 D 110 THR LYS LEU THR VAL ILE SEQRES 1 F 463 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 F 463 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 F 463 ASP ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP SEQRES 4 F 463 ALA THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN SEQRES 5 F 463 GLU LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 F 463 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE SEQRES 7 F 463 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 F 463 LEU THR PRO LEU CYS VAL THR LEU ILE CYS SER ASN ALA SEQRES 9 F 463 THR VAL LYS ASN GLY THR VAL GLU GLU MET LYS ASN CYS SEQRES 10 F 463 SER PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS SEQRES 11 F 463 LYS GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO SEQRES 12 F 463 LEU SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE SEQRES 13 F 463 ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS SEQRES 14 F 463 VAL THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 F 463 ALA GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE SEQRES 16 F 463 ASN GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN SEQRES 17 F 463 CYS THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU SEQRES 18 F 463 LEU LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE SEQRES 19 F 463 ARG SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE SEQRES 20 F 463 VAL HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG SEQRES 21 F 463 PRO ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO SEQRES 22 F 463 GLY GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP SEQRES 23 F 463 ILE LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP SEQRES 24 F 463 ASN ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS SEQRES 25 F 463 HIS PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA SEQRES 26 F 463 GLY GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS SEQRES 27 F 463 GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE SEQRES 28 F 463 ASN GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SEQRES 29 F 463 SER ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG SEQRES 30 F 463 ILE LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG SEQRES 31 F 463 CYS MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 F 463 ARG SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 F 463 GLY THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA SEQRES 34 F 463 GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 F 463 LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA SEQRES 36 F 463 PRO THR ARG CYS LYS ARG ARG VAL SEQRES 1 G 132 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 G 132 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 G 132 THR VAL GLN ALA ARG ASN LEU LEU SER GLY THR VAL TRP SEQRES 4 G 132 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 5 G 132 ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 6 G 132 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 7 G 132 ASN SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP SEQRES 8 G 132 ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER SEQRES 9 G 132 ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER SEQRES 10 G 132 GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA SEQRES 11 G 132 LEU ASP SEQRES 1 H 126 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU MET LYS LYS SEQRES 2 H 126 PRO GLY ALA SER VAL ARG VAL SER CYS LYS ALA SER GLY SEQRES 3 H 126 TYR THR PHE THR ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 H 126 ALA PRO GLY GLN GLY PRO GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 126 PRO SER THR GLY ARG THR ASN SER PRO GLN LYS PHE GLN SEQRES 6 H 126 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 126 ALA TYR MET ASP LEU ASN ARG LEU THR SER ASP ASP THR SEQRES 8 H 126 ALA MET TYR TYR CYS THR THR GLY GLY TRP ILE GLY LEU SEQRES 9 H 126 TYR SER ASP THR SER GLY TYR PRO ASN PHE ASP TYR TRP SEQRES 10 H 126 GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1 I 110 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 I 110 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR ASN SEQRES 3 I 110 TYR ASP VAL GLY SER TYR ASN LEU VAL SER TRP TYR GLN SEQRES 4 I 110 GLN HIS PRO GLY LYS VAL PRO LYS TYR ILE ILE TYR GLU SEQRES 5 I 110 VAL ASN LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 I 110 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 I 110 GLY LEU GLN ALA GLU ASP GLU ALA THR TYR TYR CYS CYS SEQRES 8 I 110 SER TYR ALA GLY SER SER ILE ILE PHE PHE GLY GLY GLY SEQRES 9 I 110 THR LYS LEU THR VAL ILE SEQRES 1 K 463 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 K 463 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 K 463 ASP ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP SEQRES 4 K 463 ALA THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN SEQRES 5 K 463 GLU LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 K 463 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE SEQRES 7 K 463 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 K 463 LEU THR PRO LEU CYS VAL THR LEU ILE CYS SER ASN ALA SEQRES 9 K 463 THR VAL LYS ASN GLY THR VAL GLU GLU MET LYS ASN CYS SEQRES 10 K 463 SER PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS SEQRES 11 K 463 LYS GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO SEQRES 12 K 463 LEU SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE SEQRES 13 K 463 ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS SEQRES 14 K 463 VAL THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 K 463 ALA GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE SEQRES 16 K 463 ASN GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN SEQRES 17 K 463 CYS THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU SEQRES 18 K 463 LEU LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE SEQRES 19 K 463 ARG SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE SEQRES 20 K 463 VAL HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG SEQRES 21 K 463 PRO ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO SEQRES 22 K 463 GLY GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP SEQRES 23 K 463 ILE LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP SEQRES 24 K 463 ASN ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS SEQRES 25 K 463 HIS PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA SEQRES 26 K 463 GLY GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS SEQRES 27 K 463 GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE SEQRES 28 K 463 ASN GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SEQRES 29 K 463 SER ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG SEQRES 30 K 463 ILE LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG SEQRES 31 K 463 CYS MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 K 463 ARG SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 K 463 GLY THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA SEQRES 34 K 463 GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 K 463 LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA SEQRES 36 K 463 PRO THR ARG CYS LYS ARG ARG VAL SEQRES 1 L 132 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 L 132 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 L 132 THR VAL GLN ALA ARG ASN LEU LEU SER GLY THR VAL TRP SEQRES 4 L 132 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 5 L 132 ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 6 L 132 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 7 L 132 ASN SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP SEQRES 8 L 132 ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER SEQRES 9 L 132 ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER SEQRES 10 L 132 GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA SEQRES 11 L 132 LEU ASP SEQRES 1 M 126 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU MET LYS LYS SEQRES 2 M 126 PRO GLY ALA SER VAL ARG VAL SER CYS LYS ALA SER GLY SEQRES 3 M 126 TYR THR PHE THR ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 M 126 ALA PRO GLY GLN GLY PRO GLU TRP MET GLY TRP ILE ASN SEQRES 5 M 126 PRO SER THR GLY ARG THR ASN SER PRO GLN LYS PHE GLN SEQRES 6 M 126 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 M 126 ALA TYR MET ASP LEU ASN ARG LEU THR SER ASP ASP THR SEQRES 8 M 126 ALA MET TYR TYR CYS THR THR GLY GLY TRP ILE GLY LEU SEQRES 9 M 126 TYR SER ASP THR SER GLY TYR PRO ASN PHE ASP TYR TRP SEQRES 10 M 126 GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1 N 110 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 N 110 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR ASN SEQRES 3 N 110 TYR ASP VAL GLY SER TYR ASN LEU VAL SER TRP TYR GLN SEQRES 4 N 110 GLN HIS PRO GLY LYS VAL PRO LYS TYR ILE ILE TYR GLU SEQRES 5 N 110 VAL ASN LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 N 110 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 N 110 GLY LEU GLN ALA GLU ASP GLU ALA THR TYR TYR CYS CYS SEQRES 8 N 110 SER TYR ALA GLY SER SER ILE ILE PHE PHE GLY GLY GLY SEQRES 9 N 110 THR LYS LEU THR VAL ILE 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 J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET MAN J 4 11 HET MAN J 5 11 HET MAN J 6 11 HET MAN J 7 11 HET MAN J 8 11 HET MAN J 9 11 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET MAN Q 4 11 HET MAN Q 5 11 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET MAN R 4 11 HET MAN R 5 11 HET MAN R 6 11 HET MAN R 7 11 HET MAN R 8 11 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET MAN U 5 11 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET MAN V 5 11 HET MAN V 6 11 HET MAN V 7 11 HET MAN V 8 11 HET MAN V 9 11 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET NAG X 1 14 HET NAG X 2 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 13 NAG 24(C8 H15 N O6) FORMUL 13 BMA 9(C6 H12 O6) FORMUL 13 MAN 23(C6 H12 O6) HELIX 1 AA1 TRP A 69 CYS A 74 1 6 HELIX 2 AA2 ASN A 98 LEU A 116 1 19 HELIX 3 AA3 TYR A 177 PRO A 179 5 3 HELIX 4 AA4 SER A 334 LYS A 351 1 18 HELIX 5 AA5 ASP A 368 THR A 373 1 6 HELIX 6 AA6 MET A 475 SER A 481 1 7 HELIX 7 AA7 THR B 529 MET B 535 1 7 HELIX 8 AA8 LEU B 537 ARG B 542 1 6 HELIX 9 AA9 ILE B 573 TRP B 596 1 24 HELIX 10 AB1 ASN B 611 SER B 615 5 5 HELIX 11 AB2 ASN B 618 ASP B 624 1 7 HELIX 12 AB3 THR B 627 SER B 636 1 10 HELIX 13 AB4 TYR B 638 ASP B 664 1 27 HELIX 14 AB5 THR C 28 THR C 30 5 3 HELIX 15 AB6 THR C 87 THR C 91 5 5 HELIX 16 AB7 GLN D 81 GLU D 85 5 5 HELIX 17 AB8 ALA F 58 TYR F 61 5 4 HELIX 18 AB9 VAL F 68 HIS F 72 5 5 HELIX 19 AC1 ASN F 98 LEU F 116 1 19 HELIX 20 AC2 TYR F 177 PRO F 179 5 3 HELIX 21 AC3 SER F 334 LYS F 351 1 18 HELIX 22 AC4 ASP F 368 THR F 373 1 6 HELIX 23 AC5 MET F 475 SER F 481 1 7 HELIX 24 AC6 THR G 529 MET G 535 1 7 HELIX 25 AC7 LEU G 537 ARG G 542 1 6 HELIX 26 AC8 ILE G 573 TRP G 596 1 24 HELIX 27 AC9 ASN G 611 SER G 615 5 5 HELIX 28 AD1 ASN G 618 ASP G 624 1 7 HELIX 29 AD2 THR G 627 SER G 636 1 10 HELIX 30 AD3 TYR G 638 ASP G 664 1 27 HELIX 31 AD4 THR H 28 THR H 30 5 3 HELIX 32 AD5 THR H 87 THR H 91 5 5 HELIX 33 AD6 GLN I 81 GLU I 85 5 5 HELIX 34 AD7 ALA K 58 TYR K 61 5 4 HELIX 35 AD8 TRP K 69 CYS K 74 1 6 HELIX 36 AD9 ASN K 98 LEU K 116 1 19 HELIX 37 AE1 TYR K 177 PRO K 179 5 3 HELIX 38 AE2 GLU K 335 LYS K 351 1 17 HELIX 39 AE3 ASP K 368 THR K 373 1 6 HELIX 40 AE4 MET K 475 SER K 481 1 7 HELIX 41 AE5 GLU K 482 TYR K 484 5 3 HELIX 42 AE6 THR L 529 MET L 535 1 7 HELIX 43 AE7 LEU L 537 ARG L 542 1 6 HELIX 44 AE8 ILE L 573 TRP L 596 1 24 HELIX 45 AE9 ASN L 611 SER L 615 5 5 HELIX 46 AF1 ASN L 618 ASP L 624 1 7 HELIX 47 AF2 THR L 627 SER L 636 1 10 HELIX 48 AF3 TYR L 638 ASP L 664 1 27 HELIX 49 AF4 THR M 28 THR M 30 5 3 HELIX 50 AF5 THR M 87 THR M 91 5 5 HELIX 51 AF6 GLN N 81 GLU N 85 5 5 SHEET 1 AA1 3 LEU A 494 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 40 -1 N THR A 37 O ALA A 497 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AA2 5 TRP A 45 GLU A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 TYR A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 LEU A 84 VAL A 85 -1 N LEU A 84 O THR A 244 SHEET 1 AA3 3 VAL A 75 PRO A 76 0 SHEET 2 AA3 3 PHE A 53 SER A 56 1 N SER A 56 O VAL A 75 SHEET 3 AA3 3 ILE A 215 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA5 5 ARG A 166 PHE A 176 0 SHEET 2 AA5 5 LYS A 155 THR A 163 -1 N PHE A 159 O GLU A 172 SHEET 3 AA5 5 LEU A 129 SER A 132 -1 N ILE A 130 O SER A 158 SHEET 4 AA5 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA5 5 ILE A 181 PRO A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA6 3 THR A 202 GLN A 203 0 SHEET 2 AA6 3 CYS A 433 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA6 3 ILE A 423 ASN A 425 -1 N ILE A 424 O MET A 434 SHEET 1 AA712 VAL A 271 ARG A 273 0 SHEET 2 AA712 ILE A 284 ARG A 308 -1 O ILE A 285 N ARG A 273 SHEET 3 AA712 THR A 316 ILE A 323 -1 O ALA A 319 N LYS A 305 SHEET 4 AA712 HIS A 330 ILE A 333 -1 O ASN A 332 N VAL A 295 SHEET 5 AA712 ILE A 359 TYR A 361 0 SHEET 6 AA712 HIS A 374 CYS A 378 0 SHEET 7 AA712 GLU A 381 ASN A 386 -1 O CYS A 385 N HIS A 374 SHEET 8 AA712 GLY A 393 TYR A 395 -1 O TYR A 395 N ILE A 359 SHEET 9 AA712 ILE A 414 LYS A 421 -1 O GLN A 417 N ASN A 386 SHEET 10 AA712 GLY A 441 THR A 444 -1 O GLY A 441 N ASN A 302 SHEET 11 AA712 SER A 447 ARG A 456 -1 O LEU A 452 N VAL A 286 SHEET 12 AA712 THR A 467 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AA8 4 GLN C 3 GLN C 6 0 SHEET 2 AA8 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AA8 4 THR C 78 LEU C 83 -1 O ALA C 79 N CYS C 22 SHEET 4 AA8 4 VAL C 68 ASP C 73 -1 N THR C 69 O ASP C 82 SHEET 1 AA9 6 TYR C 32 GLN C 39 0 SHEET 2 AA9 6 GLU C 46 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 3 AA9 6 THR C 58 ASN C 59 -1 O ASN C 59 N TRP C 50 SHEET 4 AA9 6 ALA C 92 TRP C 101 -1 O GLY C 99 N TYR C 33 SHEET 5 AA9 6 TYR C 116 TRP C 117 -1 O TYR C 116 N THR C 98 SHEET 6 AA9 6 THR C 121 VAL C 123 -1 O THR C 121 N TYR C 94 SHEET 1 AB1 3 ILE D 20 THR D 23 0 SHEET 2 AB1 3 THR D 72 THR D 76 -1 O ALA D 73 N CYS D 22 SHEET 3 AB1 3 SER D 65 SER D 69 -1 N SER D 65 O THR D 76 SHEET 1 AB2 4 LYS D 47 ILE D 50 0 SHEET 2 AB2 4 VAL D 35 GLN D 40 -1 N GLN D 39 O LYS D 47 SHEET 3 AB2 4 THR D 87 TYR D 93 -1 O THR D 87 N GLN D 40 SHEET 4 AB2 4 ILE D 99 PHE D 101 -1 O PHE D 100 N SER D 92 SHEET 1 AB3 3 LEU F 494 THR F 499 0 SHEET 2 AB3 3 TRP F 35 TYR F 40 -1 N TRP F 35 O THR F 499 SHEET 3 AB3 3 ILE G 603 PRO G 609 -1 O CYS G 604 N VAL F 38 SHEET 1 AB4 5 TRP F 45 GLU F 47 0 SHEET 2 AB4 5 TYR F 486 ILE F 491 -1 O LYS F 490 N LYS F 46 SHEET 3 AB4 5 TYR F 223 CYS F 228 -1 N LEU F 226 O LYS F 487 SHEET 4 AB4 5 VAL F 242 VAL F 245 -1 O SER F 243 N LYS F 227 SHEET 5 AB4 5 LEU F 84 VAL F 85 -1 N LEU F 84 O THR F 244 SHEET 1 AB5 3 VAL F 75 PRO F 76 0 SHEET 2 AB5 3 PHE F 53 SER F 56 1 N SER F 56 O VAL F 75 SHEET 3 AB5 3 ILE F 215 CYS F 218 -1 O HIS F 216 N ALA F 55 SHEET 1 AB6 2 GLU F 91 ASN F 94 0 SHEET 2 AB6 2 THR F 236 CYS F 239 -1 O CYS F 239 N GLU F 91 SHEET 1 AB7 5 ARG F 166 PHE F 176 0 SHEET 2 AB7 5 LYS F 155 THR F 163 -1 N PHE F 159 O GLU F 172 SHEET 3 AB7 5 LEU F 129 SER F 132 -1 N SER F 132 O ASN F 156 SHEET 4 AB7 5 GLU F 190 LEU F 193 -1 O TYR F 191 N LEU F 129 SHEET 5 AB7 5 ILE F 181 PRO F 183 -1 N VAL F 182 O ARG F 192 SHEET 1 AB8 3 THR F 202 GLN F 203 0 SHEET 2 AB8 3 CYS F 433 TYR F 435 1 O TYR F 435 N THR F 202 SHEET 3 AB8 3 ILE F 423 ASN F 425 -1 N ILE F 424 O MET F 434 SHEET 1 AB913 LEU F 259 LEU F 260 0 SHEET 2 AB913 VAL F 271 ARG F 273 0 SHEET 3 AB913 ILE F 284 ARG F 308 -1 O ILE F 285 N ARG F 273 SHEET 4 AB913 THR F 316 ILE F 323 -1 O GLY F 321 N THR F 303 SHEET 5 AB913 HIS F 330 ILE F 333 -1 O ASN F 332 N VAL F 295 SHEET 6 AB913 ILE F 359 TYR F 361 0 SHEET 7 AB913 HIS F 374 CYS F 378 0 SHEET 8 AB913 GLU F 381 ASN F 386 -1 O CYS F 385 N HIS F 374 SHEET 9 AB913 THR F 394 TYR F 395 -1 O TYR F 395 N ILE F 359 SHEET 10 AB913 ILE F 414 LYS F 421 -1 O GLN F 417 N ASN F 386 SHEET 11 AB913 GLY F 441 THR F 444 -1 O GLY F 441 N ASN F 302 SHEET 12 AB913 SER F 447 ARG F 456 -1 O LEU F 452 N VAL F 286 SHEET 13 AB913 THR F 467 PRO F 470 -1 O ARG F 469 N THR F 455 SHEET 1 AC1 4 GLN H 3 GLN H 6 0 SHEET 2 AC1 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AC1 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AC1 4 VAL H 68 ASP H 73 -1 N THR H 69 O ASP H 82 SHEET 1 AC2 5 THR H 58 ASN H 59 0 SHEET 2 AC2 5 GLU H 46 ILE H 51 -1 N TRP H 50 O ASN H 59 SHEET 3 AC2 5 TYR H 32 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AC2 5 ALA H 92 TRP H 101 -1 O GLY H 99 N TYR H 33 SHEET 5 AC2 5 THR H 121 VAL H 123 -1 O THR H 121 N TYR H 94 SHEET 1 AC3 2 SER I 9 GLY I 12 0 SHEET 2 AC3 2 LYS I 106 VAL I 109 1 O LYS I 106 N VAL I 10 SHEET 1 AC4 3 ILE I 20 CYS I 22 0 SHEET 2 AC4 3 THR I 72 THR I 76 -1 O ALA I 73 N CYS I 22 SHEET 3 AC4 3 SER I 65 SER I 69 -1 N SER I 65 O THR I 76 SHEET 1 AC5 4 LYS I 47 ILE I 50 0 SHEET 2 AC5 4 VAL I 35 GLN I 40 -1 N GLN I 39 O LYS I 47 SHEET 3 AC5 4 THR I 87 TYR I 93 -1 O TYR I 89 N TYR I 38 SHEET 4 AC5 4 ILE I 99 PHE I 101 -1 O PHE I 100 N SER I 92 SHEET 1 AC6 3 LEU K 494 THR K 499 0 SHEET 2 AC6 3 TRP K 35 TYR K 40 -1 N THR K 37 O ALA K 497 SHEET 3 AC6 3 ILE L 603 PRO L 609 -1 O CYS L 604 N VAL K 38 SHEET 1 AC7 5 TRP K 45 GLU K 47 0 SHEET 2 AC7 5 TYR K 486 ILE K 491 -1 O LYS K 490 N LYS K 46 SHEET 3 AC7 5 TYR K 223 CYS K 228 -1 N LEU K 226 O LYS K 487 SHEET 4 AC7 5 VAL K 242 VAL K 245 -1 O SER K 243 N LYS K 227 SHEET 5 AC7 5 LEU K 84 LEU K 86 -1 N LEU K 84 O THR K 244 SHEET 1 AC8 3 VAL K 75 PRO K 76 0 SHEET 2 AC8 3 PHE K 53 SER K 56 1 N SER K 56 O VAL K 75 SHEET 3 AC8 3 ILE K 215 CYS K 218 -1 O HIS K 216 N ALA K 55 SHEET 1 AC9 2 GLU K 91 ASN K 94 0 SHEET 2 AC9 2 THR K 236 CYS K 239 -1 O CYS K 239 N GLU K 91 SHEET 1 AD1 5 ARG K 166 PHE K 176 0 SHEET 2 AD1 5 LYS K 155 THR K 163 -1 N PHE K 159 O GLU K 172 SHEET 3 AD1 5 LEU K 129 SER K 132 -1 N SER K 132 O ASN K 156 SHEET 4 AD1 5 GLU K 190 LEU K 193 -1 O TYR K 191 N LEU K 129 SHEET 5 AD1 5 ILE K 181 PRO K 183 -1 N VAL K 182 O ARG K 192 SHEET 1 AD2 3 THR K 202 GLN K 203 0 SHEET 2 AD2 3 CYS K 433 TYR K 435 1 O TYR K 435 N THR K 202 SHEET 3 AD2 3 ILE K 423 ASN K 425 -1 N ILE K 424 O MET K 434 SHEET 1 AD312 VAL K 271 ARG K 273 0 SHEET 2 AD312 ILE K 284 ARG K 308 -1 O ILE K 285 N ARG K 273 SHEET 3 AD312 THR K 316 ILE K 323 -1 O ALA K 319 N LYS K 305 SHEET 4 AD312 HIS K 330 SER K 334 -1 O ASN K 332 N VAL K 295 SHEET 5 AD312 ILE K 359 TYR K 361 0 SHEET 6 AD312 HIS K 374 CYS K 378 0 SHEET 7 AD312 GLU K 381 ASN K 386 -1 O CYS K 385 N HIS K 374 SHEET 8 AD312 THR K 394 TYR K 395 -1 O TYR K 395 N ILE K 359 SHEET 9 AD312 THR K 413 LYS K 421 -1 O GLN K 417 N ASN K 386 SHEET 10 AD312 GLY K 441 THR K 444 -1 O GLY K 441 N ASN K 302 SHEET 11 AD312 SER K 447 ARG K 456 -1 O LEU K 452 N VAL K 286 SHEET 12 AD312 THR K 467 PRO K 470 -1 O ARG K 469 N THR K 455 SHEET 1 AD4 4 GLN M 3 GLN M 6 0 SHEET 2 AD4 4 SER M 17 SER M 25 -1 O LYS M 23 N VAL M 5 SHEET 3 AD4 4 THR M 78 ASN M 84 -1 O ALA M 79 N CYS M 22 SHEET 4 AD4 4 VAL M 68 ASP M 73 -1 N THR M 69 O ASP M 82 SHEET 1 AD5 5 THR M 58 ASN M 59 0 SHEET 2 AD5 5 GLU M 46 ILE M 51 -1 N TRP M 50 O ASN M 59 SHEET 3 AD5 5 TYR M 32 GLN M 39 -1 N ARG M 38 O GLU M 46 SHEET 4 AD5 5 ALA M 92 TRP M 101 -1 O GLY M 99 N TYR M 33 SHEET 5 AD5 5 THR M 121 VAL M 123 -1 O THR M 121 N TYR M 94 SHEET 1 AD6 2 SER N 9 GLY N 12 0 SHEET 2 AD6 2 LYS N 106 VAL N 109 1 O LYS N 106 N VAL N 10 SHEET 1 AD7 3 ILE N 20 THR N 23 0 SHEET 2 AD7 3 THR N 72 THR N 76 -1 O ALA N 73 N CYS N 22 SHEET 3 AD7 3 SER N 65 SER N 69 -1 N SER N 65 O THR N 76 SHEET 1 AD8 4 LYS N 47 ILE N 50 0 SHEET 2 AD8 4 VAL N 35 GLN N 40 -1 N GLN N 39 O LYS N 47 SHEET 3 AD8 4 THR N 87 TYR N 93 -1 O TYR N 89 N TYR N 38 SHEET 4 AD8 4 ILE N 99 PHE N 101 -1 O PHE N 100 N SER N 92 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.04 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 201 CYS A 433 1555 1555 2.03 SSBOND 6 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 7 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 8 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 9 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 10 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 11 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 12 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 13 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 14 CYS D 22 CYS D 90 1555 1555 2.03 SSBOND 15 CYS F 54 CYS F 74 1555 1555 2.03 SSBOND 16 CYS F 119 CYS F 205 1555 1555 2.03 SSBOND 17 CYS F 126 CYS F 196 1555 1555 2.03 SSBOND 18 CYS F 131 CYS F 157 1555 1555 2.03 SSBOND 19 CYS F 201 CYS F 433 1555 1555 2.03 SSBOND 20 CYS F 218 CYS F 247 1555 1555 2.05 SSBOND 21 CYS F 228 CYS F 239 1555 1555 2.03 SSBOND 22 CYS F 296 CYS F 331 1555 1555 2.03 SSBOND 23 CYS F 378 CYS F 445 1555 1555 2.02 SSBOND 24 CYS F 385 CYS F 418 1555 1555 2.03 SSBOND 25 CYS F 501 CYS G 605 1555 1555 2.03 SSBOND 26 CYS G 598 CYS G 604 1555 1555 2.03 SSBOND 27 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 28 CYS I 22 CYS I 90 1555 1555 2.03 SSBOND 29 CYS K 54 CYS K 74 1555 1555 2.04 SSBOND 30 CYS K 119 CYS K 205 1555 1555 2.03 SSBOND 31 CYS K 126 CYS K 196 1555 1555 2.03 SSBOND 32 CYS K 131 CYS K 157 1555 1555 2.03 SSBOND 33 CYS K 201 CYS K 433 1555 1555 2.03 SSBOND 34 CYS K 218 CYS K 247 1555 1555 2.03 SSBOND 35 CYS K 228 CYS K 239 1555 1555 2.03 SSBOND 36 CYS K 296 CYS K 331 1555 1555 2.03 SSBOND 37 CYS K 378 CYS K 445 1555 1555 2.02 SSBOND 38 CYS K 385 CYS K 418 1555 1555 2.03 SSBOND 39 CYS K 501 CYS L 605 1555 1555 2.03 SSBOND 40 CYS L 598 CYS L 604 1555 1555 2.02 SSBOND 41 CYS M 22 CYS M 96 1555 1555 2.03 SSBOND 42 CYS N 22 CYS N 90 1555 1555 2.03 LINK ND2 ASN A 156 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 442 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN F 156 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN F 301 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN F 332 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN F 442 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN K 156 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN K 301 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN K 332 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN K 442 C1 NAG X 1 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45 LINK O2 MAN E 4 C1 MAN E 5 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44 LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.44 LINK O6 BMA J 3 C1 MAN J 7 1555 1555 1.45 LINK O2 MAN J 4 C1 MAN J 5 1555 1555 1.46 LINK O2 MAN J 5 C1 MAN J 6 1555 1555 1.46 LINK O6 MAN J 7 C1 MAN J 8 1555 1555 1.45 LINK O2 MAN J 8 C1 MAN J 9 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.45 LINK O2 MAN Q 4 C1 MAN Q 5 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.44 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.44 LINK O6 BMA R 3 C1 MAN R 7 1555 1555 1.45 LINK O2 MAN R 4 C1 MAN R 5 1555 1555 1.46 LINK O2 MAN R 5 C1 MAN R 6 1555 1555 1.46 LINK O6 MAN R 7 C1 MAN R 8 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.45 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.45 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.45 LINK O2 MAN U 4 C1 MAN U 5 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.44 LINK O6 BMA V 3 C1 MAN V 7 1555 1555 1.45 LINK O2 MAN V 4 C1 MAN V 5 1555 1555 1.46 LINK O2 MAN V 5 C1 MAN V 6 1555 1555 1.46 LINK O6 MAN V 7 C1 MAN V 8 1555 1555 1.45 LINK O2 MAN V 8 C1 MAN V 9 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 CISPEP 1 ASN A 67 VAL A 68 0 -10.46 CISPEP 2 SER A 80 PRO A 81 0 -3.19 CISPEP 3 ASN A 403 SER A 404 0 -4.79 CISPEP 4 THR D 23 GLY D 24 0 -6.55 CISPEP 5 ASN F 67 VAL F 68 0 -9.25 CISPEP 6 SER F 80 PRO F 81 0 -3.36 CISPEP 7 ASN F 403 SER F 404 0 -4.14 CISPEP 8 THR I 23 GLY I 24 0 -12.26 CISPEP 9 ASN K 67 VAL K 68 0 -9.11 CISPEP 10 SER K 80 PRO K 81 0 -3.11 CISPEP 11 ASN K 403 SER K 404 0 -4.41 CISPEP 12 THR N 23 GLY N 24 0 -11.31 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