HEADER VIRAL PROTEIN/IMMUNE SYSTEM 12-MAY-22 8CSJ TITLE CRYO-EM STRUCTURE OF NTD-DIRECTED NON-NEUTRALIZING ANTIBODY 4-33 IN TITLE 2 COMPLEX WITH PREFUSION SARS-COV-2 SPIKE GLYCOPROTEIN CAVEAT 8CSJ RESIDUES THR 307 AND VAL 308 THAT ARE NEXT TO EACH OTHER IN CAVEAT 2 8CSJ THE SAMPLE SEQUENCE OF CHAINS A, B, AND C ARE NOT PROPERLY CAVEAT 3 8CSJ LINKED. COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 4-33 HEAVY CHAIN; COMPND 8 CHAIN: H, D, F; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 4-33 LIGHT CHAIN; COMPND 12 CHAIN: L, E, G; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NON-NEUTRALIZING ANTIBODY, FUSION PROTEIN, SPIKE GLYCOPROTEIN, COVID- KEYWDS 2 19, NTD, NTD-DIRECTED ANTIBODY, 4-33, VIRAL PROTEIN, IMMUNE SYSTEM, KEYWDS 3 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR E.R.REDDEM,L.SHAPIRO JRNL AUTH E.R.REDDEM,L.SHAPIRO JRNL TITL CRYO-EM STRUCTURE OF NTD-DIRECTED NON-NEUTRALIZING ANTIBODY JRNL TITL 2 4-33 IN COMPLEX WITH PREFUSION SARS-COV-2 SPIKE GLYCOPROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.53 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC 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 : FLEXIBLE FIT 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) : 3.530 REMARK 3 NUMBER OF PARTICLES : 420343 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 8CSJ 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_1000265121. 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 : PREFUSION SARS-COV-2 SPIKE REMARK 245 GLYCOPROTEIN IN COMPLEX WITH 4- REMARK 245 18 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 : 4.50 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 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 42.00 REMARK 245 ILLUMINATION MODE : OTHER 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: NONAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, B, C, D, E, F, G, I, REMARK 350 AND CHAINS: J, K, M, N, O REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 VAL A 445 REMARK 465 GLY A 446 REMARK 465 GLN A 677 REMARK 465 THR A 678 REMARK 465 ASN A 679 REMARK 465 SER A 680 REMARK 465 PRO A 681 REMARK 465 ARG A 682 REMARK 465 ARG A 683 REMARK 465 ALA A 684 REMARK 465 ARG A 685 REMARK 465 SER A 686 REMARK 465 VAL A 687 REMARK 465 ALA A 688 REMARK 465 VAL B 445 REMARK 465 GLY B 446 REMARK 465 GLN B 677 REMARK 465 THR B 678 REMARK 465 ASN B 679 REMARK 465 SER B 680 REMARK 465 PRO B 681 REMARK 465 ARG B 682 REMARK 465 ARG B 683 REMARK 465 ALA B 684 REMARK 465 ARG B 685 REMARK 465 SER B 686 REMARK 465 VAL B 687 REMARK 465 ALA B 688 REMARK 465 VAL C 445 REMARK 465 GLY C 446 REMARK 465 GLN C 677 REMARK 465 THR C 678 REMARK 465 ASN C 679 REMARK 465 SER C 680 REMARK 465 PRO C 681 REMARK 465 ARG C 682 REMARK 465 ARG C 683 REMARK 465 ALA C 684 REMARK 465 ARG C 685 REMARK 465 SER C 686 REMARK 465 VAL C 687 REMARK 465 ALA C 688 REMARK 465 ALA C 829 REMARK 465 ASP C 830 REMARK 465 ALA C 831 REMARK 465 GLY C 832 REMARK 465 PHE C 833 REMARK 465 ILE C 834 REMARK 465 LYS C 835 REMARK 465 GLN C 836 REMARK 465 TYR C 837 REMARK 465 GLY C 838 REMARK 465 ASP C 839 REMARK 465 CYS C 840 REMARK 465 LEU C 841 REMARK 465 GLY C 842 REMARK 465 ASP C 843 REMARK 465 ILE C 844 REMARK 465 ALA C 845 REMARK 465 ALA C 846 REMARK 465 ARG C 847 REMARK 465 ASP C 848 REMARK 465 LEU C 849 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 ILE C 850 CG1 CG2 CD1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ILE C 850 NZ LYS C 854 1.27 REMARK 500 O3 NAG M 1 N2 NAG M 2 1.42 REMARK 500 NZ LYS A 462 C8 NAG A 1313 1.43 REMARK 500 CE LYS A 462 C8 NAG A 1313 1.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 560 CA - CB - CG ANGL. DEV. = 19.1 DEGREES REMARK 500 PRO A 589 CA - N - CD ANGL. DEV. = -12.4 DEGREES REMARK 500 ASP B 428 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES REMARK 500 ASP B 830 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES REMARK 500 LEU C 518 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 ASP D 72 CB - CG - OD2 ANGL. DEV. = 7.5 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 41 33.91 -97.59 REMARK 500 ALA A 123 -66.19 61.33 REMARK 500 LYS A 150 34.99 -98.45 REMARK 500 ARG A 214 31.91 -143.74 REMARK 500 LEU A 226 -60.37 -93.44 REMARK 500 THR A 333 -37.26 -130.74 REMARK 500 THR A 393 -75.86 55.95 REMARK 500 ASP A 428 36.97 -99.09 REMARK 500 ASN A 450 49.28 -91.03 REMARK 500 LYS A 535 142.63 64.71 REMARK 500 ASP A 571 17.34 54.30 REMARK 500 PHE A 592 121.44 58.46 REMARK 500 VAL A 729 -54.99 -123.08 REMARK 500 SER A 758 36.82 -98.99 REMARK 500 ALA A 846 53.71 -92.71 REMARK 500 CYS A1043 54.94 -94.25 REMARK 500 GLU A1111 86.62 -154.58 REMARK 500 ASN L 51 -9.67 70.69 REMARK 500 SER L 52 -14.02 -141.13 REMARK 500 LYS B 150 34.09 -94.30 REMARK 500 ARG B 214 30.79 -143.86 REMARK 500 PRO B 272 107.94 -51.62 REMARK 500 ALA B 411 149.31 -172.52 REMARK 500 ALA B 475 53.17 -91.16 REMARK 500 SER B 477 52.21 -92.59 REMARK 500 ASN B 710 15.55 -140.02 REMARK 500 PHE B 855 54.53 -91.79 REMARK 500 LYS C 150 33.23 -95.69 REMARK 500 ARG C 214 31.41 -143.57 REMARK 500 LYS C 386 41.30 -109.77 REMARK 500 ASP C 428 35.45 -99.71 REMARK 500 LEU C 518 17.07 56.12 REMARK 500 PHE C 562 54.07 -91.34 REMARK 500 ASP C 568 -169.92 -118.17 REMARK 500 ASP C 614 -5.13 71.15 REMARK 500 ILE C 666 -53.07 -121.34 REMARK 500 LEU C 699 32.94 -96.97 REMARK 500 VAL C 729 -55.14 -121.30 REMARK 500 SER C 758 37.02 -99.86 REMARK 500 ALA C 852 -134.74 37.31 REMARK 500 GLN C 853 -17.87 62.40 REMARK 500 LYS C 854 46.49 -65.70 REMARK 500 LEU C 945 32.64 -93.88 REMARK 500 ASP C1041 -3.57 72.01 REMARK 500 CYS C1043 58.38 -97.15 REMARK 500 HIS C1083 -64.21 -92.28 REMARK 500 CYS C1126 56.39 -90.44 REMARK 500 LEU C1141 -60.68 -97.68 REMARK 500 ASN E 51 -9.36 70.19 REMARK 500 SER E 52 -14.64 -140.93 REMARK 500 REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS. 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 LEU A 560 PRO A 561 -127.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLN B 271 10.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG I 1 REMARK 610 NAG M 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-26964 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF NTD-DIRECTED NON-NEUTRALIZING ANTIBODY 4-33 IN REMARK 900 COMPLEX WITH PREFUSION SARS-COV-2 SPIKE GLYCOPROTEIN DBREF 8CSJ A 14 1147 UNP P0DTC2 SPIKE_SARS2 14 1147 DBREF 8CSJ H 2 113 PDB 8CSJ 8CSJ 2 113 DBREF 8CSJ L 2 107 PDB 8CSJ 8CSJ 2 107 DBREF 8CSJ B 14 1147 UNP P0DTC2 SPIKE_SARS2 14 1147 DBREF 8CSJ C 14 1147 UNP P0DTC2 SPIKE_SARS2 14 1147 DBREF 8CSJ D 2 113 PDB 8CSJ 8CSJ 2 113 DBREF 8CSJ E 2 107 PDB 8CSJ 8CSJ 2 107 DBREF 8CSJ F 2 113 PDB 8CSJ 8CSJ 2 113 DBREF 8CSJ G 2 107 PDB 8CSJ 8CSJ 2 107 SEQADV 8CSJ PRO A 986 UNP P0DTC2 LYS 986 CONFLICT SEQADV 8CSJ PRO A 987 UNP P0DTC2 VAL 987 CONFLICT SEQADV 8CSJ PRO B 986 UNP P0DTC2 LYS 986 CONFLICT SEQADV 8CSJ PRO B 987 UNP P0DTC2 VAL 987 CONFLICT SEQADV 8CSJ PRO C 986 UNP P0DTC2 LYS 986 CONFLICT SEQADV 8CSJ PRO C 987 UNP P0DTC2 VAL 987 CONFLICT SEQRES 1 A 1134 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 2 A 1134 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 3 A 1134 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 4 A 1134 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 5 A 1134 HIS ALA ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 6 A 1134 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 7 A 1134 PHE ALA SER THR GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 8 A 1134 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 9 A 1134 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 10 A 1134 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU GLY VAL SEQRES 11 A 1134 TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU SEQRES 12 A 1134 PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU SEQRES 13 A 1134 TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS SEQRES 14 A 1134 GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS SEQRES 15 A 1134 ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR SEQRES 16 A 1134 PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER SEQRES 17 A 1134 ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN SEQRES 18 A 1134 ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER SEQRES 19 A 1134 TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA SEQRES 20 A 1134 GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG SEQRES 21 A 1134 THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR SEQRES 22 A 1134 ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR SEQRES 23 A 1134 LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE SEQRES 24 A 1134 TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER SEQRES 25 A 1134 ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 26 A 1134 GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR SEQRES 27 A 1134 ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP SEQRES 28 A 1134 TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE SEQRES 29 A 1134 LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU SEQRES 30 A 1134 CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG SEQRES 31 A 1134 GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 32 A 1134 LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 33 A 1134 THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SEQRES 34 A 1134 SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU SEQRES 35 A 1134 PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SEQRES 36 A 1134 SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN SEQRES 37 A 1134 GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER SEQRES 38 A 1134 TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO SEQRES 39 A 1134 TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA SEQRES 40 A 1134 PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU SEQRES 41 A 1134 VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU SEQRES 42 A 1134 THR GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE SEQRES 43 A 1134 LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR SEQRES 44 A 1134 THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU SEQRES 45 A 1134 ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE SEQRES 46 A 1134 THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU SEQRES 47 A 1134 TYR GLN ASP VAL ASN CYS THR GLU VAL PRO VAL ALA ILE SEQRES 48 A 1134 HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER SEQRES 49 A 1134 THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU SEQRES 50 A 1134 ILE GLY ALA GLU HIS VAL ASN ASN SER TYR GLU CYS ASP SEQRES 51 A 1134 ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR SEQRES 52 A 1134 GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER SEQRES 53 A 1134 GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU SEQRES 54 A 1134 ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO SEQRES 55 A 1134 THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO SEQRES 56 A 1134 VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR SEQRES 57 A 1134 ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU SEQRES 58 A 1134 GLN TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU SEQRES 59 A 1134 THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU SEQRES 60 A 1134 VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO SEQRES 61 A 1134 ILE LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU SEQRES 62 A 1134 PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU SEQRES 63 A 1134 ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY SEQRES 64 A 1134 PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA SEQRES 65 A 1134 ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU SEQRES 66 A 1134 THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA SEQRES 67 A 1134 GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER SEQRES 68 A 1134 GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO SEQRES 69 A 1134 PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY SEQRES 70 A 1134 VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE SEQRES 71 A 1134 ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SEQRES 72 A 1134 SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN SEQRES 73 A 1134 ASP VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU SEQRES 74 A 1134 VAL LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER SEQRES 75 A 1134 VAL LEU ASN ASP ILE LEU SER ARG LEU ASP PRO PRO GLU SEQRES 76 A 1134 ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU SEQRES 77 A 1134 GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG SEQRES 78 A 1134 ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR SEQRES 79 A 1134 LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL SEQRES 80 A 1134 ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO SEQRES 81 A 1134 GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR SEQRES 82 A 1134 TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO SEQRES 83 A 1134 ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU SEQRES 84 A 1134 GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR SEQRES 85 A 1134 GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP SEQRES 86 A 1134 ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY SEQRES 87 A 1134 ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU SEQRES 88 A 1134 LEU ASP SER SEQRES 1 H 122 VAL GLN LEU VAL GLN SER GLY SER GLU LEU LYS LYS PRO SEQRES 2 H 122 GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY TYR SEQRES 3 H 122 THR PHE THR SER TYR ALA MET ASN TRP VAL ARG GLN ALA SEQRES 4 H 122 PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN THR SEQRES 5 H 122 ASN THR GLY ASN PRO THR TYR ALA GLN GLY PHE THR GLY SEQRES 6 H 122 ARG PHE VAL PHE SER LEU ASP THR SER VAL SER THR ALA SEQRES 7 H 122 TYR LEU GLN ILE SER SER LEU LYS THR GLU ASP THR ALA SEQRES 8 H 122 VAL TYR TYR CYS ALA ARG GLU LEU TRP PHE GLY GLU LEU SEQRES 9 H 122 LEU SER GLY ASP PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 H 122 VAL THR VAL SER SER SEQRES 1 L 110 SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA PRO SEQRES 2 L 110 GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SER SEQRES 3 L 110 ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN GLN SEQRES 4 L 110 LEU PRO GLY THR ALA PRO LYS ILE ILE ILE TYR ASP ASN SEQRES 5 L 110 SER ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 L 110 SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR GLY SEQRES 7 L 110 LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER SEQRES 8 L 110 TYR ASP SER SER LEU SER GLY ARG VAL PHE GLY GLY GLY SEQRES 9 L 110 THR LYS LEU THR VAL LEU SEQRES 1 B 1134 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 2 B 1134 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 3 B 1134 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 4 B 1134 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 5 B 1134 HIS ALA ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 6 B 1134 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 7 B 1134 PHE ALA SER THR GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 8 B 1134 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 9 B 1134 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 10 B 1134 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU GLY VAL SEQRES 11 B 1134 TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU SEQRES 12 B 1134 PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU SEQRES 13 B 1134 TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS SEQRES 14 B 1134 GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS SEQRES 15 B 1134 ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR SEQRES 16 B 1134 PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER SEQRES 17 B 1134 ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN SEQRES 18 B 1134 ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER SEQRES 19 B 1134 TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA SEQRES 20 B 1134 GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG SEQRES 21 B 1134 THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR SEQRES 22 B 1134 ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR SEQRES 23 B 1134 LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE SEQRES 24 B 1134 TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER SEQRES 25 B 1134 ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 26 B 1134 GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR SEQRES 27 B 1134 ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP SEQRES 28 B 1134 TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE SEQRES 29 B 1134 LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU SEQRES 30 B 1134 CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG SEQRES 31 B 1134 GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 32 B 1134 LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 33 B 1134 THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SEQRES 34 B 1134 SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU SEQRES 35 B 1134 PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SEQRES 36 B 1134 SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN SEQRES 37 B 1134 GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER SEQRES 38 B 1134 TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO SEQRES 39 B 1134 TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA SEQRES 40 B 1134 PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU SEQRES 41 B 1134 VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU SEQRES 42 B 1134 THR GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE SEQRES 43 B 1134 LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR SEQRES 44 B 1134 THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU SEQRES 45 B 1134 ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE SEQRES 46 B 1134 THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU SEQRES 47 B 1134 TYR GLN ASP VAL ASN CYS THR GLU VAL PRO VAL ALA ILE SEQRES 48 B 1134 HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER SEQRES 49 B 1134 THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU SEQRES 50 B 1134 ILE GLY ALA GLU HIS VAL ASN ASN SER TYR GLU CYS ASP SEQRES 51 B 1134 ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR SEQRES 52 B 1134 GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER SEQRES 53 B 1134 GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU SEQRES 54 B 1134 ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO SEQRES 55 B 1134 THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO SEQRES 56 B 1134 VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR SEQRES 57 B 1134 ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU SEQRES 58 B 1134 GLN TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU SEQRES 59 B 1134 THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU SEQRES 60 B 1134 VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO SEQRES 61 B 1134 ILE LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU SEQRES 62 B 1134 PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU SEQRES 63 B 1134 ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY SEQRES 64 B 1134 PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA SEQRES 65 B 1134 ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU SEQRES 66 B 1134 THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA SEQRES 67 B 1134 GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER SEQRES 68 B 1134 GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO SEQRES 69 B 1134 PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY SEQRES 70 B 1134 VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE SEQRES 71 B 1134 ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SEQRES 72 B 1134 SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN SEQRES 73 B 1134 ASP VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU SEQRES 74 B 1134 VAL LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER SEQRES 75 B 1134 VAL LEU ASN ASP ILE LEU SER ARG LEU ASP PRO PRO GLU SEQRES 76 B 1134 ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU SEQRES 77 B 1134 GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG SEQRES 78 B 1134 ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR SEQRES 79 B 1134 LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL SEQRES 80 B 1134 ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO SEQRES 81 B 1134 GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR SEQRES 82 B 1134 TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO SEQRES 83 B 1134 ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU SEQRES 84 B 1134 GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR SEQRES 85 B 1134 GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP SEQRES 86 B 1134 ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY SEQRES 87 B 1134 ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU SEQRES 88 B 1134 LEU ASP SER SEQRES 1 C 1134 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 2 C 1134 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 3 C 1134 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 4 C 1134 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 5 C 1134 HIS ALA ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 6 C 1134 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 7 C 1134 PHE ALA SER THR GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 8 C 1134 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 9 C 1134 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 10 C 1134 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU GLY VAL SEQRES 11 C 1134 TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU SEQRES 12 C 1134 PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU SEQRES 13 C 1134 TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS SEQRES 14 C 1134 GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS SEQRES 15 C 1134 ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR SEQRES 16 C 1134 PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER SEQRES 17 C 1134 ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN SEQRES 18 C 1134 ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER SEQRES 19 C 1134 TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA SEQRES 20 C 1134 GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG SEQRES 21 C 1134 THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR SEQRES 22 C 1134 ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR SEQRES 23 C 1134 LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE SEQRES 24 C 1134 TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER SEQRES 25 C 1134 ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 26 C 1134 GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR SEQRES 27 C 1134 ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP SEQRES 28 C 1134 TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE SEQRES 29 C 1134 LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU SEQRES 30 C 1134 CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG SEQRES 31 C 1134 GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 32 C 1134 LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 33 C 1134 THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SEQRES 34 C 1134 SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU SEQRES 35 C 1134 PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SEQRES 36 C 1134 SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN SEQRES 37 C 1134 GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER SEQRES 38 C 1134 TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO SEQRES 39 C 1134 TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA SEQRES 40 C 1134 PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU SEQRES 41 C 1134 VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU SEQRES 42 C 1134 THR GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE SEQRES 43 C 1134 LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR SEQRES 44 C 1134 THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU SEQRES 45 C 1134 ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE SEQRES 46 C 1134 THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU SEQRES 47 C 1134 TYR GLN ASP VAL ASN CYS THR GLU VAL PRO VAL ALA ILE SEQRES 48 C 1134 HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER SEQRES 49 C 1134 THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU SEQRES 50 C 1134 ILE GLY ALA GLU HIS VAL ASN ASN SER TYR GLU CYS ASP SEQRES 51 C 1134 ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR SEQRES 52 C 1134 GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER SEQRES 53 C 1134 GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU SEQRES 54 C 1134 ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO SEQRES 55 C 1134 THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO SEQRES 56 C 1134 VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR SEQRES 57 C 1134 ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU SEQRES 58 C 1134 GLN TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU SEQRES 59 C 1134 THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU SEQRES 60 C 1134 VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO SEQRES 61 C 1134 ILE LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU SEQRES 62 C 1134 PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU SEQRES 63 C 1134 ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY SEQRES 64 C 1134 PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA SEQRES 65 C 1134 ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU SEQRES 66 C 1134 THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA SEQRES 67 C 1134 GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER SEQRES 68 C 1134 GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO SEQRES 69 C 1134 PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY SEQRES 70 C 1134 VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE SEQRES 71 C 1134 ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SEQRES 72 C 1134 SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN SEQRES 73 C 1134 ASP VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU SEQRES 74 C 1134 VAL LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER SEQRES 75 C 1134 VAL LEU ASN ASP ILE LEU SER ARG LEU ASP PRO PRO GLU SEQRES 76 C 1134 ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU SEQRES 77 C 1134 GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG SEQRES 78 C 1134 ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR SEQRES 79 C 1134 LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL SEQRES 80 C 1134 ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO SEQRES 81 C 1134 GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR SEQRES 82 C 1134 TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO SEQRES 83 C 1134 ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU SEQRES 84 C 1134 GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR SEQRES 85 C 1134 GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP SEQRES 86 C 1134 ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY SEQRES 87 C 1134 ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU SEQRES 88 C 1134 LEU ASP SER SEQRES 1 D 122 VAL GLN LEU VAL GLN SER GLY SER GLU LEU LYS LYS PRO SEQRES 2 D 122 GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY TYR SEQRES 3 D 122 THR PHE THR SER TYR ALA MET ASN TRP VAL ARG GLN ALA SEQRES 4 D 122 PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN THR SEQRES 5 D 122 ASN THR GLY ASN PRO THR TYR ALA GLN GLY PHE THR GLY SEQRES 6 D 122 ARG PHE VAL PHE SER LEU ASP THR SER VAL SER THR ALA SEQRES 7 D 122 TYR LEU GLN ILE SER SER LEU LYS THR GLU ASP THR ALA SEQRES 8 D 122 VAL TYR TYR CYS ALA ARG GLU LEU TRP PHE GLY GLU LEU SEQRES 9 D 122 LEU SER GLY ASP PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 D 122 VAL THR VAL SER SER SEQRES 1 E 110 SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA PRO SEQRES 2 E 110 GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SER SEQRES 3 E 110 ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN GLN SEQRES 4 E 110 LEU PRO GLY THR ALA PRO LYS ILE ILE ILE TYR ASP ASN SEQRES 5 E 110 SER ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 E 110 SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR GLY SEQRES 7 E 110 LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER SEQRES 8 E 110 TYR ASP SER SER LEU SER GLY ARG VAL PHE GLY GLY GLY SEQRES 9 E 110 THR LYS LEU THR VAL LEU SEQRES 1 F 122 VAL GLN LEU VAL GLN SER GLY SER GLU LEU LYS LYS PRO SEQRES 2 F 122 GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY TYR SEQRES 3 F 122 THR PHE THR SER TYR ALA MET ASN TRP VAL ARG GLN ALA SEQRES 4 F 122 PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN THR SEQRES 5 F 122 ASN THR GLY ASN PRO THR TYR ALA GLN GLY PHE THR GLY SEQRES 6 F 122 ARG PHE VAL PHE SER LEU ASP THR SER VAL SER THR ALA SEQRES 7 F 122 TYR LEU GLN ILE SER SER LEU LYS THR GLU ASP THR ALA SEQRES 8 F 122 VAL TYR TYR CYS ALA ARG GLU LEU TRP PHE GLY GLU LEU SEQRES 9 F 122 LEU SER GLY ASP PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 F 122 VAL THR VAL SER SER SEQRES 1 G 110 SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA PRO SEQRES 2 G 110 GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SER SEQRES 3 G 110 ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN GLN SEQRES 4 G 110 LEU PRO GLY THR ALA PRO LYS ILE ILE ILE TYR ASP ASN SEQRES 5 G 110 SER ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 G 110 SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR GLY SEQRES 7 G 110 LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER SEQRES 8 G 110 TYR ASP SER SER LEU SER GLY ARG VAL PHE GLY GLY GLY SEQRES 9 G 110 THR LYS LEU THR VAL LEU HET NAG A1301 14 HET NAG A1302 14 HET NAG A1303 14 HET NAG A1304 14 HET NAG A1305 14 HET NAG A1306 14 HET NAG A1307 14 HET NAG A1308 14 HET NAG A1309 14 HET NAG A1310 14 HET NAG A1311 14 HET NAG A1312 14 HET NAG A1313 14 HET NAG B1201 14 HET NAG B1202 14 HET NAG B1203 14 HET NAG B1204 14 HET NAG B1205 14 HET NAG B1206 14 HET NAG B1207 14 HET NAG B1208 14 HET NAG B1209 14 HET NAG B1210 14 HET NAG C1201 14 HET NAG C1202 14 HET NAG C1203 14 HET NAG C1204 14 HET NAG C1205 14 HET NAG C1206 14 HET NAG C1207 14 HET NAG C1208 14 HET NAG C1209 14 HET NAG C1210 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 10 NAG 45(C8 H15 N O6) HELIX 1 AA1 ASP A 294 LYS A 304 1 11 HELIX 2 AA2 TYR A 365 TYR A 369 5 5 HELIX 3 AA3 SER A 383 LEU A 387 5 5 HELIX 4 AA4 ASP A 405 ALA A 411 5 7 HELIX 5 AA5 GLU A 619 ILE A 624 1 6 HELIX 6 AA6 HIS A 625 LEU A 629 5 5 HELIX 7 AA7 THR A 630 TYR A 636 1 7 HELIX 8 AA8 ASP A 737 CYS A 743 1 7 HELIX 9 AA9 SER A 746 LEU A 754 1 9 HELIX 10 AB1 GLN A 755 GLY A 757 5 3 HELIX 11 AB2 SER A 758 ALA A 783 1 26 HELIX 12 AB3 SER A 816 LYS A 825 1 10 HELIX 13 AB4 ASP A 848 ASN A 856 1 9 HELIX 14 AB5 THR A 866 SER A 884 1 19 HELIX 15 AB6 TRP A 886 GLY A 891 1 6 HELIX 16 AB7 PRO A 897 GLY A 908 1 12 HELIX 17 AB8 THR A 912 ASN A 919 1 8 HELIX 18 AB9 ASN A 919 SER A 940 1 22 HELIX 19 AC1 LEU A 945 GLN A 965 1 21 HELIX 20 AC2 LEU A 966 SER A 968 5 3 HELIX 21 AC3 VAL A 976 LEU A 984 1 9 HELIX 22 AC4 ASP A 985 VAL A 1033 1 49 HELIX 23 AC5 LEU A 1141 ASP A 1146 5 6 HELIX 24 AC6 LYS H 83 THR H 87 5 5 HELIX 25 AC7 GLN L 79 GLU L 83 5 5 HELIX 26 AC8 ASP B 294 LYS B 304 1 11 HELIX 27 AC9 PRO B 337 ASN B 343 1 7 HELIX 28 AD1 TYR B 365 ASN B 370 1 6 HELIX 29 AD2 SER B 383 ASP B 389 5 7 HELIX 30 AD3 ARG B 403 GLN B 409 5 7 HELIX 31 AD4 LYS B 417 ASN B 422 1 6 HELIX 32 AD5 GLU B 619 ILE B 624 1 6 HELIX 33 AD6 HIS B 625 GLN B 628 5 4 HELIX 34 AD7 THR B 630 TYR B 636 1 7 HELIX 35 AD8 ASP B 737 CYS B 743 1 7 HELIX 36 AD9 SER B 746 GLN B 755 1 10 HELIX 37 AE1 SER B 758 ALA B 783 1 26 HELIX 38 AE2 SER B 816 VAL B 826 1 11 HELIX 39 AE3 GLY B 832 CYS B 840 1 9 HELIX 40 AE4 THR B 866 GLY B 885 1 20 HELIX 41 AE5 TRP B 886 GLY B 891 1 6 HELIX 42 AE6 PRO B 897 GLY B 908 1 12 HELIX 43 AE7 THR B 912 SER B 940 1 29 HELIX 44 AE8 LEU B 945 GLN B 965 1 21 HELIX 45 AE9 LEU B 966 SER B 968 5 3 HELIX 46 AF1 VAL B 976 LEU B 984 1 9 HELIX 47 AF2 ASP B 985 VAL B 1033 1 49 HELIX 48 AF3 ASP C 294 LYS C 304 1 11 HELIX 49 AF4 PHE C 338 ASN C 343 1 6 HELIX 50 AF5 ASP C 364 LEU C 368 5 5 HELIX 51 AF6 SER C 383 LEU C 387 5 5 HELIX 52 AF7 GLU C 406 ALA C 411 5 6 HELIX 53 AF8 GLY C 416 ASN C 422 1 7 HELIX 54 AF9 SER C 438 SER C 443 1 6 HELIX 55 AG1 GLU C 619 ILE C 624 1 6 HELIX 56 AG2 THR C 630 VAL C 635 1 6 HELIX 57 AG3 ASP C 737 CYS C 743 1 7 HELIX 58 AG4 SER C 746 LEU C 754 1 9 HELIX 59 AG5 GLN C 755 GLY C 757 5 3 HELIX 60 AG6 CYS C 760 ALA C 783 1 24 HELIX 61 AG7 SER C 816 VAL C 826 1 11 HELIX 62 AG8 THR C 866 SER C 884 1 19 HELIX 63 AG9 TRP C 886 GLY C 891 1 6 HELIX 64 AH1 PRO C 897 GLY C 908 1 12 HELIX 65 AH2 THR C 912 SER C 940 1 29 HELIX 66 AH3 LEU C 945 GLN C 965 1 21 HELIX 67 AH4 LEU C 966 SER C 968 5 3 HELIX 68 AH5 VAL C 976 LEU C 984 1 9 HELIX 69 AH6 ASP C 985 VAL C 1033 1 49 HELIX 70 AH7 THR D 28 THR D 30 5 3 HELIX 71 AH8 LYS D 83 THR D 87 5 5 HELIX 72 AH9 GLN E 79 GLU E 83 5 5 HELIX 73 AI1 THR F 28 THR F 30 5 3 HELIX 74 AI2 LYS F 83 THR F 87 5 5 HELIX 75 AI3 GLN G 79 GLU G 83 5 5 SHEET 1 AA1 9 ALA A 27 ASN A 30 0 SHEET 2 AA1 9 VAL A 36 TYR A 37 0 SHEET 3 AA1 9 ASN A 61 HIS A 69 -1 O TRP A 64 N ALA A 27 SHEET 4 AA1 9 LYS A 77 PHE A 79 -1 O ARG A 78 N ILE A 68 SHEET 5 AA1 9 GLY A 89 GLU A 96 0 SHEET 6 AA1 9 ASN A 188 ILE A 197 -1 O PHE A 192 N PHE A 92 SHEET 7 AA1 9 TYR A 200 PRO A 209 -1 O THR A 208 N LEU A 189 SHEET 8 AA1 9 ALA A 222 PRO A 230 -1 O LEU A 229 N PHE A 201 SHEET 9 AA1 9 ALA A 263 TYR A 269 -1 O TYR A 266 N ALA A 93 SHEET 1 AA2 3 VAL A 47 PHE A 55 0 SHEET 2 AA2 3 GLN A 271 TYR A 279 -1 O GLN A 271 N PHE A 55 SHEET 3 AA2 3 ILE A 285 ASP A 290 -1 O VAL A 289 N LEU A 276 SHEET 1 AA3 7 LEU A 84 PRO A 85 0 SHEET 2 AA3 7 GLY A 103 GLY A 107 0 SHEET 3 AA3 7 SER A 116 ASN A 122 -1 O ILE A 119 N TRP A 104 SHEET 4 AA3 7 ASN A 125 TYR A 144 -1 O VAL A 127 N VAL A 120 SHEET 5 AA3 7 GLU A 154 VAL A 171 -1 O SER A 161 N GLN A 134 SHEET 6 AA3 7 ARG A 237 THR A 240 -1 O ARG A 237 N GLY A 107 SHEET 7 AA3 7 ALA A 243 ARG A 246 1 O LEU A 244 N VAL A 143 SHEET 1 AA4 5 GLY A 311 THR A 315 0 SHEET 2 AA4 5 VAL A 595 THR A 599 -1 O THR A 599 N GLY A 311 SHEET 3 AA4 5 ALA A 609 GLN A 613 -1 O LEU A 611 N SER A 596 SHEET 4 AA4 5 GLY A 648 ILE A 651 -1 O CYS A 649 N TYR A 612 SHEET 5 AA4 5 VAL A 642 GLN A 644 -1 N PHE A 643 O LEU A 650 SHEET 1 AA5 5 SER A 325 ARG A 328 0 SHEET 2 AA5 5 CYS A 538 PHE A 543 1 O ASN A 542 N ARG A 328 SHEET 3 AA5 5 LEU A 546 THR A 553 -1 O GLY A 550 N VAL A 539 SHEET 4 AA5 5 ILE A 584 THR A 588 -1 O THR A 588 N VAL A 551 SHEET 5 AA5 5 ALA A 575 ARG A 577 -1 N VAL A 576 O LEU A 585 SHEET 1 AA6 5 ASN A 354 ILE A 358 0 SHEET 2 AA6 5 VAL A 395 ARG A 403 -1 O ALA A 397 N LYS A 356 SHEET 3 AA6 5 PRO A 507 PHE A 515 -1 O SER A 514 N TYR A 396 SHEET 4 AA6 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA6 5 THR A 376 CYS A 379 -1 N THR A 376 O ALA A 435 SHEET 1 AA7 2 LEU A 452 ARG A 454 0 SHEET 2 AA7 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA8 2 TYR A 473 GLN A 474 0 SHEET 2 AA8 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA9 2 PHE A 565 GLY A 566 0 SHEET 2 AA9 2 VAL B 42 PHE B 43 1 O PHE B 43 N PHE A 565 SHEET 1 AB1 4 GLU A 654 HIS A 655 0 SHEET 2 AB1 4 SER A 691 THR A 696 1 O ALA A 694 N GLU A 654 SHEET 3 AB1 4 ILE A 670 GLN A 675 -1 N GLN A 675 O SER A 691 SHEET 4 AB1 4 ILE A 664 GLY A 667 -1 N ILE A 666 O ILE A 670 SHEET 1 AB2 2 ALA A 701 SER A 704 0 SHEET 2 AB2 2 GLN B 787 LYS B 790 1 O ILE B 788 N ASN A 703 SHEET 1 AB3 5 SER A 711 PRO A 728 0 SHEET 2 AB3 5 TYR A1047 ALA A1056 0 SHEET 3 AB3 5 GLY A1059 THR A1077 -1 O VAL A1065 N MET A1050 SHEET 4 AB3 5 VAL A1094 SER A1097 -1 O SER A1097 N THR A1076 SHEET 5 AB3 5 TRP A1102 THR A1105 -1 O PHE A1103 N VAL A1096 SHEET 1 AB4 2 THR A 734 VAL A 736 0 SHEET 2 AB4 2 LEU A 858 VAL A 860 -1 O THR A 859 N SER A 735 SHEET 1 AB5 2 ILE A 788 LYS A 790 0 SHEET 2 AB5 2 GLU C 702 SER C 704 1 O ASN C 703 N ILE A 788 SHEET 1 AB6 4 THR A1120 ASN A1125 0 SHEET 2 AB6 4 LYS A1086 PRO A1090 -1 N PHE A1089 O PHE A1121 SHEET 3 AB6 4 ILE A1081 CYS A1082 -1 N ILE A1081 O HIS A1088 SHEET 4 AB6 4 VAL A1133 ASN A1134 1 O VAL A1133 N CYS A1082 SHEET 1 AB7 4 GLN H 3 GLN H 6 0 SHEET 2 AB7 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AB7 4 THR H 77 ILE H 82 -1 O LEU H 80 N VAL H 20 SHEET 4 AB7 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AB8 6 GLU H 10 LYS H 12 0 SHEET 2 AB8 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AB8 6 ALA H 88 LEU H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AB8 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AB8 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AB8 6 PRO H 57 TYR H 59 -1 O THR H 58 N TRP H 50 SHEET 1 AB9 6 SER L 9 GLY L 13 0 SHEET 2 AB9 6 VAL L 33 GLN L 38 0 SHEET 3 AB9 6 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 4 AB9 6 ASP L 85 TYR L 91 -1 O TYR L 87 N TYR L 36 SHEET 5 AB9 6 ARG L 96 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 6 AB9 6 THR L 102 VAL L 106 -1 O THR L 102 N TYR L 86 SHEET 1 AC1 3 ARG L 18 THR L 24 0 SHEET 2 AC1 3 SER L 70 THR L 76 -1 O LEU L 73 N ILE L 21 SHEET 3 AC1 3 PHE L 62 SER L 67 -1 N SER L 63 O ALA L 74 SHEET 1 AC2 8 ALA B 27 ASN B 30 0 SHEET 2 AC2 8 ASN B 61 HIS B 69 -1 O TRP B 64 N ALA B 27 SHEET 3 AC2 8 LYS B 77 PHE B 79 -1 O ARG B 78 N ILE B 68 SHEET 4 AC2 8 GLY B 89 GLU B 96 0 SHEET 5 AC2 8 ASN B 188 ILE B 197 -1 O PHE B 192 N PHE B 92 SHEET 6 AC2 8 TYR B 200 PRO B 209 -1 O THR B 208 N LEU B 189 SHEET 7 AC2 8 GLU B 224 PRO B 230 -1 O LEU B 226 N ILE B 203 SHEET 8 AC2 8 ALA B 263 TYR B 269 -1 O TYR B 266 N ALA B 93 SHEET 1 AC3 3 LEU B 48 PHE B 55 0 SHEET 2 AC3 3 GLN B 271 TYR B 279 -1 O GLN B 271 N PHE B 55 SHEET 3 AC3 3 ILE B 285 ASP B 290 -1 O ASP B 287 N LYS B 278 SHEET 1 AC4 6 LEU B 84 PRO B 85 0 SHEET 2 AC4 6 ARG B 237 LEU B 241 -1 O PHE B 238 N LEU B 84 SHEET 3 AC4 6 GLY B 103 GLY B 107 -1 N GLY B 103 O LEU B 241 SHEET 4 AC4 6 LEU B 117 ASN B 121 -1 O LEU B 117 N PHE B 106 SHEET 5 AC4 6 VAL B 126 CYS B 131 -1 O LYS B 129 N LEU B 118 SHEET 6 AC4 6 CYS B 166 VAL B 171 -1 O TYR B 170 N ILE B 128 SHEET 1 AC5 3 GLU B 154 TYR B 160 0 SHEET 2 AC5 3 PHE B 135 TYR B 144 -1 N GLY B 142 O GLU B 156 SHEET 3 AC5 3 ALA B 243 ARG B 246 1 O LEU B 244 N VAL B 143 SHEET 1 AC6 5 GLY B 311 ARG B 319 0 SHEET 2 AC6 5 PHE B 592 THR B 599 -1 O VAL B 595 N SER B 316 SHEET 3 AC6 5 ALA B 609 TYR B 612 -1 O ALA B 609 N ILE B 598 SHEET 4 AC6 5 LEU B 650 ILE B 651 -1 O ILE B 651 N VAL B 610 SHEET 5 AC6 5 VAL B 642 PHE B 643 -1 N PHE B 643 O LEU B 650 SHEET 1 AC7 5 SER B 325 ARG B 328 0 SHEET 2 AC7 5 VAL B 539 PHE B 543 1 O ASN B 540 N ILE B 326 SHEET 3 AC7 5 THR B 547 GLU B 554 -1 O GLY B 550 N VAL B 539 SHEET 4 AC7 5 ILE B 584 THR B 588 -1 O ASP B 586 N THR B 553 SHEET 5 AC7 5 ALA B 575 ARG B 577 -1 N VAL B 576 O LEU B 585 SHEET 1 AC8 6 ASN B 354 ILE B 358 0 SHEET 2 AC8 6 THR B 376 CYS B 379 0 SHEET 3 AC8 6 CYS B 391 ILE B 402 -1 O VAL B 395 N ILE B 358 SHEET 4 AC8 6 GLY B 431 ASN B 437 -1 O VAL B 433 N LYS B 378 SHEET 5 AC8 6 TYR B 508 GLU B 516 -1 O ARG B 509 N TRP B 436 SHEET 6 AC8 6 VAL B 524 CYS B 525 -1 O VAL B 524 N PHE B 392 SHEET 1 AC9 2 LEU B 452 ARG B 454 0 SHEET 2 AC9 2 LEU B 492 SER B 494 -1 O GLN B 493 N TYR B 453 SHEET 1 AD1 2 TYR B 473 GLN B 474 0 SHEET 2 AD1 2 CYS B 488 TYR B 489 -1 O TYR B 489 N TYR B 473 SHEET 1 AD2 4 GLU B 654 TYR B 660 0 SHEET 2 AD2 4 ILE B 692 MET B 697 1 O ALA B 694 N GLU B 654 SHEET 3 AD2 4 ILE B 670 TYR B 674 -1 N SER B 673 O ILE B 693 SHEET 4 AD2 4 ILE B 664 GLY B 667 -1 N ILE B 664 O ALA B 672 SHEET 1 AD3 2 GLU B 702 ASN B 703 0 SHEET 2 AD3 2 ILE C 788 TYR C 789 1 O ILE C 788 N ASN B 703 SHEET 1 AD4 4 SER B 711 PRO B 715 0 SHEET 2 AD4 4 GLU B1072 ALA B1078 -1 O PHE B1075 N ILE B 712 SHEET 3 AD4 4 VAL B1094 SER B1097 -1 O SER B1097 N THR B1076 SHEET 4 AD4 4 TRP B1102 THR B1105 -1 O PHE B1103 N VAL B1096 SHEET 1 AD5 3 PHE B 718 PRO B 728 0 SHEET 2 AD5 3 GLY B1059 PRO B1069 -1 O VAL B1068 N THR B 719 SHEET 3 AD5 3 TYR B1047 ALA B1056 -1 N TYR B1047 O TYR B1067 SHEET 1 AD6 2 THR B 734 VAL B 736 0 SHEET 2 AD6 2 LEU B 858 VAL B 860 -1 O THR B 859 N SER B 735 SHEET 1 AD7 4 THR B1120 VAL B1122 0 SHEET 2 AD7 4 ALA B1087 PRO B1090 -1 N PHE B1089 O PHE B1121 SHEET 3 AD7 4 ILE B1081 CYS B1082 -1 N ILE B1081 O HIS B1088 SHEET 4 AD7 4 VAL B1133 ASN B1134 1 O VAL B1133 N CYS B1082 SHEET 1 AD811 ALA C 27 ASN C 30 0 SHEET 2 AD811 VAL C 36 TYR C 37 0 SHEET 3 AD811 LEU C 48 PHE C 55 0 SHEET 4 AD811 ASN C 61 HIS C 69 -1 O TRP C 64 N ALA C 27 SHEET 5 AD811 LYS C 77 PHE C 79 -1 O ARG C 78 N ILE C 68 SHEET 6 AD811 GLY C 89 GLU C 96 0 SHEET 7 AD811 ASN C 188 ILE C 197 -1 O PHE C 192 N PHE C 92 SHEET 8 AD811 TYR C 200 PRO C 209 -1 O THR C 208 N LEU C 189 SHEET 9 AD811 ALA C 222 VAL C 227 -1 O LEU C 226 N ILE C 203 SHEET 10 AD811 ALA C 263 TYR C 279 -1 O TYR C 266 N ALA C 93 SHEET 11 AD811 ILE C 285 ASP C 290 -1 O ASP C 287 N LYS C 278 SHEET 1 AD9 8 LEU C 84 PRO C 85 0 SHEET 2 AD9 8 ILE C 101 GLY C 107 0 SHEET 3 AD9 8 LEU C 117 ASN C 121 -1 O LEU C 117 N PHE C 106 SHEET 4 AD9 8 VAL C 126 CYS C 131 -1 O VAL C 127 N VAL C 120 SHEET 5 AD9 8 PHE C 135 TYR C 144 0 SHEET 6 AD9 8 GLU C 154 TYR C 160 -1 O SER C 155 N GLY C 142 SHEET 7 AD9 8 CYS C 166 VAL C 171 -1 O TYR C 170 N ILE C 128 SHEET 8 AD9 8 ARG C 237 ARG C 246 1 O LEU C 244 N VAL C 143 SHEET 1 AE1 5 GLY C 311 GLN C 314 0 SHEET 2 AE1 5 VAL C 595 THR C 599 -1 O VAL C 597 N TYR C 313 SHEET 3 AE1 5 ALA C 609 GLN C 613 -1 O LEU C 611 N SER C 596 SHEET 4 AE1 5 GLY C 648 ILE C 651 -1 O CYS C 649 N TYR C 612 SHEET 5 AE1 5 VAL C 642 GLN C 644 -1 N PHE C 643 O LEU C 650 SHEET 1 AE2 5 ASN C 354 ILE C 358 0 SHEET 2 AE2 5 THR C 393 ILE C 402 -1 O VAL C 395 N ILE C 358 SHEET 3 AE2 5 TYR C 508 GLU C 516 -1 O TYR C 508 N ILE C 402 SHEET 4 AE2 5 GLY C 431 ASN C 437 -1 N ILE C 434 O VAL C 511 SHEET 5 AE2 5 THR C 376 CYS C 379 -1 N THR C 376 O ALA C 435 SHEET 1 AE3 2 CYS C 361 VAL C 362 0 SHEET 2 AE3 2 VAL C 524 CYS C 525 1 O CYS C 525 N CYS C 361 SHEET 1 AE4 2 LEU C 452 ARG C 454 0 SHEET 2 AE4 2 LEU C 492 SER C 494 -1 O GLN C 493 N TYR C 453 SHEET 1 AE5 2 TYR C 473 GLN C 474 0 SHEET 2 AE5 2 CYS C 488 TYR C 489 -1 O TYR C 489 N TYR C 473 SHEET 1 AE6 5 VAL C 539 PHE C 543 0 SHEET 2 AE6 5 LEU C 546 SER C 555 -1 O LEU C 546 N PHE C 543 SHEET 3 AE6 5 ILE C 584 THR C 588 -1 O ASP C 586 N THR C 553 SHEET 4 AE6 5 THR C 573 ARG C 577 -1 N ASP C 574 O ILE C 587 SHEET 5 AE6 5 PHE C 565 ARG C 567 -1 N GLY C 566 O ALA C 575 SHEET 1 AE7 4 GLU C 654 HIS C 655 0 SHEET 2 AE7 4 SER C 691 THR C 696 1 O ILE C 692 N GLU C 654 SHEET 3 AE7 4 ILE C 670 GLN C 675 -1 N GLN C 675 O SER C 691 SHEET 4 AE7 4 ILE C 664 GLY C 667 -1 N ILE C 666 O ILE C 670 SHEET 1 AE8 3 SER C 711 PRO C 728 0 SHEET 2 AE8 3 GLY C1059 THR C1076 -1 O PHE C1062 N GLU C 725 SHEET 3 AE8 3 TYR C1047 ALA C1056 -1 N TYR C1047 O TYR C1067 SHEET 1 AE9 2 LYS C 733 VAL C 736 0 SHEET 2 AE9 2 LEU C 858 LEU C 861 -1 O THR C 859 N SER C 735 SHEET 1 AF1 4 THR C1120 ASN C1125 0 SHEET 2 AF1 4 LYS C1086 PRO C1090 -1 N PHE C1089 O PHE C1121 SHEET 3 AF1 4 ILE C1081 CYS C1082 -1 N ILE C1081 O HIS C1088 SHEET 4 AF1 4 VAL C1133 ASN C1134 1 O VAL C1133 N CYS C1082 SHEET 1 AF2 2 VAL C1094 SER C1097 0 SHEET 2 AF2 2 TRP C1102 THR C1105 -1 O PHE C1103 N VAL C1096 SHEET 1 AF3 4 GLN D 3 GLN D 6 0 SHEET 2 AF3 4 VAL D 18 SER D 25 -1 O LYS D 23 N VAL D 5 SHEET 3 AF3 4 THR D 77 ILE D 82 -1 O LEU D 80 N VAL D 20 SHEET 4 AF3 4 PHE D 67 SER D 70 -1 N VAL D 68 O GLN D 81 SHEET 1 AF4 5 GLU D 10 LYS D 12 0 SHEET 2 AF4 5 THR D 107 VAL D 111 1 O THR D 110 N LYS D 12 SHEET 3 AF4 5 ALA D 88 LEU D 96 -1 N ALA D 88 O VAL D 109 SHEET 4 AF4 5 TYR D 32 GLN D 39 -1 N ALA D 33 O GLU D 95 SHEET 5 AF4 5 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 1 AF5 6 SER E 9 GLY E 13 0 SHEET 2 AF5 6 VAL E 33 GLN E 38 0 SHEET 3 AF5 6 LYS E 45 ILE E 48 -1 O LYS E 45 N GLN E 37 SHEET 4 AF5 6 ASP E 85 TYR E 91 -1 O TYR E 87 N TYR E 36 SHEET 5 AF5 6 ARG E 96 PHE E 98 -1 O VAL E 97 N SER E 90 SHEET 6 AF5 6 THR E 102 VAL E 106 -1 O THR E 102 N TYR E 86 SHEET 1 AF6 3 ARG E 18 THR E 24 0 SHEET 2 AF6 3 SER E 70 THR E 76 -1 O LEU E 73 N ILE E 21 SHEET 3 AF6 3 PHE E 62 SER E 67 -1 N SER E 63 O ALA E 74 SHEET 1 AF7 4 GLN F 3 GLN F 6 0 SHEET 2 AF7 4 VAL F 18 SER F 25 -1 O LYS F 23 N VAL F 5 SHEET 3 AF7 4 THR F 77 ILE F 82 -1 O LEU F 80 N VAL F 20 SHEET 4 AF7 4 PHE F 67 SER F 70 -1 N VAL F 68 O GLN F 81 SHEET 1 AF8 6 GLU F 10 LYS F 12 0 SHEET 2 AF8 6 THR F 107 VAL F 111 1 O THR F 110 N LYS F 12 SHEET 3 AF8 6 VAL F 89 LEU F 96 -1 N TYR F 90 O THR F 107 SHEET 4 AF8 6 TYR F 32 GLN F 39 -1 N ASN F 35 O ALA F 93 SHEET 5 AF8 6 GLU F 46 ILE F 51 -1 O GLU F 46 N ARG F 38 SHEET 6 AF8 6 PRO F 57 TYR F 59 -1 O THR F 58 N TRP F 50 SHEET 1 AF9 6 SER G 9 GLY G 13 0 SHEET 2 AF9 6 VAL G 33 GLN G 38 0 SHEET 3 AF9 6 LYS G 45 ILE G 48 -1 O LYS G 45 N GLN G 37 SHEET 4 AF9 6 ASP G 85 TYR G 91 -1 O TYR G 87 N TYR G 36 SHEET 5 AF9 6 ARG G 96 PHE G 98 -1 O VAL G 97 N SER G 90 SHEET 6 AF9 6 THR G 102 VAL G 106 -1 O THR G 102 N TYR G 86 SHEET 1 AG1 3 ARG G 18 CYS G 23 0 SHEET 2 AG1 3 SER G 70 THR G 76 -1 O LEU G 73 N ILE G 21 SHEET 3 AG1 3 PHE G 62 SER G 67 -1 N SER G 63 O ALA G 74 SSBOND 1 CYS A 15 CYS A 136 1555 1555 2.03 SSBOND 2 CYS A 131 CYS A 166 1555 1555 2.03 SSBOND 3 CYS A 291 CYS A 301 1555 1555 2.03 SSBOND 4 CYS A 336 CYS A 361 1555 1555 2.03 SSBOND 5 CYS A 379 CYS A 432 1555 1555 2.04 SSBOND 6 CYS A 391 CYS A 525 1555 1555 2.03 SSBOND 7 CYS A 480 CYS A 488 1555 1555 2.03 SSBOND 8 CYS A 538 CYS A 590 1555 1555 2.03 SSBOND 9 CYS A 617 CYS A 649 1555 1555 2.03 SSBOND 10 CYS A 662 CYS A 671 1555 1555 2.03 SSBOND 11 CYS A 738 CYS A 760 1555 1555 2.03 SSBOND 12 CYS A 743 CYS A 749 1555 1555 2.03 SSBOND 13 CYS A 840 CYS A 851 1555 1555 2.03 SSBOND 14 CYS A 1032 CYS A 1043 1555 1555 2.03 SSBOND 15 CYS A 1082 CYS A 1126 1555 1555 2.03 SSBOND 16 CYS B 15 CYS B 136 1555 1555 2.03 SSBOND 17 CYS B 131 CYS B 166 1555 1555 2.03 SSBOND 18 CYS B 291 CYS B 301 1555 1555 2.03 SSBOND 19 CYS B 336 CYS B 361 1555 1555 2.03 SSBOND 20 CYS B 379 CYS B 432 1555 1555 2.03 SSBOND 21 CYS B 391 CYS B 525 1555 1555 2.03 SSBOND 22 CYS B 480 CYS B 488 1555 1555 2.03 SSBOND 23 CYS B 538 CYS B 590 1555 1555 2.03 SSBOND 24 CYS B 617 CYS B 649 1555 1555 2.03 SSBOND 25 CYS B 662 CYS B 671 1555 1555 2.03 SSBOND 26 CYS B 738 CYS B 760 1555 1555 2.03 SSBOND 27 CYS B 743 CYS B 749 1555 1555 2.03 SSBOND 28 CYS B 840 CYS B 851 1555 1555 2.03 SSBOND 29 CYS B 1032 CYS B 1043 1555 1555 2.03 SSBOND 30 CYS B 1082 CYS B 1126 1555 1555 2.03 SSBOND 31 CYS C 15 CYS C 136 1555 1555 2.03 SSBOND 32 CYS C 131 CYS C 166 1555 1555 2.03 SSBOND 33 CYS C 291 CYS C 301 1555 1555 2.03 SSBOND 34 CYS C 336 CYS C 361 1555 1555 2.03 SSBOND 35 CYS C 379 CYS C 432 1555 1555 2.03 SSBOND 36 CYS C 391 CYS C 525 1555 1555 2.03 SSBOND 37 CYS C 480 CYS C 488 1555 1555 2.03 SSBOND 38 CYS C 538 CYS C 590 1555 1555 2.03 SSBOND 39 CYS C 617 CYS C 649 1555 1555 2.03 SSBOND 40 CYS C 662 CYS C 671 1555 1555 2.03 SSBOND 41 CYS C 738 CYS C 760 1555 1555 2.03 SSBOND 42 CYS C 743 CYS C 749 1555 1555 2.03 SSBOND 43 CYS C 1032 CYS C 1043 1555 1555 2.03 SSBOND 44 CYS C 1082 CYS C 1126 1555 1555 2.03 LINK ND2 ASN A 17 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 61 C1 NAG A1311 1555 1555 1.44 LINK ND2 ASN A 74 C1 NAG A1310 1555 1555 1.44 LINK ND2 ASN A 149 C1 NAG A1308 1555 1555 1.45 LINK ND2 ASN A 165 C1 NAG A1307 1555 1555 1.45 LINK ND2 ASN A 234 C1 NAG A1312 1555 1555 1.44 LINK ND2 ASN A 282 C1 NAG A1309 1555 1555 1.44 LINK ND2 ASN A 331 C1 NAG A1301 1555 1555 1.44 LINK ND2 ASN A 343 C1 NAG A1302 1555 1555 1.44 LINK ND2 ASN A 603 C1 NAG A1303 1555 1555 1.44 LINK ND2 ASN A 616 C1 NAG A1304 1555 1555 1.44 LINK ND2 ASN A 657 C1 NAG A1305 1555 1555 1.44 LINK ND2 ASN A 709 C1 NAG A1306 1555 1555 1.44 LINK C1 NAG A1313 ND2 ASN B 234 1555 1555 1.44 LINK ND2 ASN B 17 C1 NAG B1210 1555 1555 1.44 LINK ND2 ASN B 61 C1 NAG B1209 1555 1555 1.44 LINK ND2 ASN B 74 C1 NAG B1208 1555 1555 1.44 LINK ND2 ASN B 122 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN B 149 C1 NAG B1206 1555 1555 1.46 LINK ND2 ASN B 282 C1 NAG B1207 1555 1555 1.44 LINK ND2 ASN B 603 C1 NAG B1201 1555 1555 1.45 LINK ND2 ASN B 616 C1 NAG B1202 1555 1555 1.44 LINK ND2 ASN B 657 C1 NAG B1203 1555 1555 1.44 LINK ND2 ASN B 709 C1 NAG B1204 1555 1555 1.44 LINK ND2 ASN B1074 C1 NAG B1205 1555 1555 1.44 LINK ND2 ASN C 17 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN C 61 C1 NAG C1209 1555 1555 1.44 LINK ND2 ASN C 74 C1 NAG C1208 1555 1555 1.44 LINK ND2 ASN C 122 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN C 149 C1 NAG C1207 1555 1555 1.45 LINK ND2 ASN C 234 C1 NAG C1210 1555 1555 1.44 LINK ND2 ASN C 282 C1 NAG M 1 1555 1555 1.46 LINK ND2 ASN C 331 C1 NAG C1201 1555 1555 1.44 LINK ND2 ASN C 343 C1 NAG C1202 1555 1555 1.44 LINK ND2 ASN C 616 C1 NAG C1203 1555 1555 1.44 LINK ND2 ASN C 657 C1 NAG C1204 1555 1555 1.44 LINK ND2 ASN C 709 C1 NAG C1205 1555 1555 1.44 LINK ND2 ASN C1074 C1 NAG C1206 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.46 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O3 NAG M 1 C2 NAG M 2 1555 1555 1.46 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.46 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