HEADER VIRAL PROTEIN 10-JUL-23 8K18 TITLE NEUTRALIZATION ANTIBODY ZCP4C9 BOUND WITH SARS-COV-2 OMICRON BA.5 RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ZCP4C9 HEAVY CHAIN; COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ZCP4C9 LIGHT CHAIN; COMPND 11 CHAIN: D; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR T.BINGJIE,D.SHANGYU REVDAT 1 09-OCT-24 8K18 0 JRNL AUTH T.BINGJIE,D.SHANGYU JRNL TITL NEUTRALIZATION ANTIBODY ZCP4C9 BOUND WITH SARS-COV-2 OMICRON JRNL TITL 2 BA.5 RBD JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.680 REMARK 3 NUMBER OF PARTICLES : 200759 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 8K18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ. REMARK 100 THE DEPOSITION ID IS D_1300039205. 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 : NEUTRALIZATION ANTIBODY ZCP4C9 REMARK 245 BOUND WITH SARS-COV-2 OMICRON REMARK 245 BA.5 RBD REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 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) : 5000.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LEU E 518 REMARK 465 HIS E 519 REMARK 465 ALA E 520 REMARK 465 PRO E 521 REMARK 465 ALA E 522 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 CG ARG E 355 OD1 ASP E 398 2.00 REMARK 500 OD1 ASN E 417 CE2 TYR C 52 2.00 REMARK 500 OD2 ASP E 420 OG SER C 56 2.09 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 TYR E 365 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES REMARK 500 ARG C 66 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES REMARK 500 ARG C 71 NE - CZ - NH2 ANGL. DEV. = 6.2 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 SER E 359 -67.88 -93.99 REMARK 500 ASN E 370 36.05 -84.34 REMARK 500 ASP E 389 49.89 -92.76 REMARK 500 TYR E 423 112.33 -161.92 REMARK 500 SER E 459 -153.69 59.49 REMARK 500 PHE E 464 16.52 58.79 REMARK 500 ASN E 481 50.79 36.33 REMARK 500 SER E 496 53.02 -145.88 REMARK 500 HIS E 505 21.92 -147.36 REMARK 500 ARG C 31 31.31 -144.48 REMARK 500 ASP C 65 -7.05 63.04 REMARK 500 GLU C 101 -158.58 53.68 REMARK 500 TRP C 102 3.69 -67.57 REMARK 500 ASN D 30 -127.36 51.54 REMARK 500 ALA D 51 -19.45 77.56 REMARK 500 ILE D 83 97.62 -64.68 REMARK 500 TYR D 91 23.87 -144.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ASP E 389 0.08 SIDE CHAIN REMARK 500 TYR E 449 0.08 SIDE CHAIN REMARK 500 ARG E 457 0.27 SIDE CHAIN REMARK 500 GLU C 6 0.07 SIDE CHAIN REMARK 500 ASP C 89 0.07 SIDE CHAIN REMARK 500 ARG C 103 0.18 SIDE CHAIN REMARK 500 ASP D 1 0.09 SIDE CHAIN REMARK 500 GLU D 55 0.10 SIDE CHAIN REMARK 500 GLU D 105 0.08 SIDE CHAIN 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 SER E 496 11.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36788 RELATED DB: EMDB REMARK 900 NEUTRALIZATION ANTIBODY ZCP4C9 BOUND WITH SARS-COV-2 OMICRON BA.5 REMARK 900 RBD DBREF 8K18 E 334 526 UNP P0DTC2 SPIKE_SARS2 334 526 DBREF 8K18 C 1 119 PDB 8K18 8K18 1 119 DBREF 8K18 D 1 107 PDB 8K18 8K18 1 107 SEQADV 8K18 ASP E 339 UNP P0DTC2 GLY 339 VARIANT SEQADV 8K18 LYS E 346 UNP P0DTC2 ARG 346 CONFLICT SEQADV 8K18 PRO E 348 UNP P0DTC2 ALA 348 CONFLICT SEQADV 8K18 GLU E 354 UNP P0DTC2 ASN 354 CONFLICT SEQADV 8K18 LYS E 357 UNP P0DTC2 ARG 357 CONFLICT SEQADV 8K18 PHE E 371 UNP P0DTC2 SER 371 VARIANT SEQADV 8K18 THR E 372 UNP P0DTC2 ALA 372 CONFLICT SEQADV 8K18 PRO E 373 UNP P0DTC2 SER 373 VARIANT SEQADV 8K18 PHE E 375 UNP P0DTC2 SER 375 VARIANT SEQADV 8K18 ALA E 376 UNP P0DTC2 THR 376 VARIANT SEQADV 8K18 ALA E 384 UNP P0DTC2 PRO 384 CONFLICT SEQADV 8K18 SER E 393 UNP P0DTC2 THR 393 CONFLICT SEQADV 8K18 VAL E 402 UNP P0DTC2 ILE 402 CONFLICT SEQADV 8K18 LYS E 403 UNP P0DTC2 ARG 403 CONFLICT SEQADV 8K18 ASP E 406 UNP P0DTC2 GLU 406 CONFLICT SEQADV 8K18 SER E 408 UNP P0DTC2 ARG 408 VARIANT SEQADV 8K18 ASN E 417 UNP P0DTC2 LYS 417 VARIANT SEQADV 8K18 MET E 430 UNP P0DTC2 THR 430 CONFLICT SEQADV 8K18 LEU E 434 UNP P0DTC2 ILE 434 CONFLICT SEQADV 8K18 THR E 438 UNP P0DTC2 SER 438 CONFLICT SEQADV 8K18 ARG E 439 UNP P0DTC2 ASN 439 CONFLICT SEQADV 8K18 LYS E 440 UNP P0DTC2 ASN 440 VARIANT SEQADV 8K18 ILE E 441 UNP P0DTC2 LEU 441 CONFLICT SEQADV 8K18 ALA E 443 UNP P0DTC2 SER 443 CONFLICT SEQADV 8K18 THR E 444 UNP P0DTC2 LYS 444 CONFLICT SEQADV 8K18 SER E 445 UNP P0DTC2 VAL 445 CONFLICT SEQADV 8K18 THR E 446 UNP P0DTC2 GLY 446 CONFLICT SEQADV 8K18 ARG E 452 UNP P0DTC2 LEU 452 VARIANT SEQADV 8K18 ASN E 477 UNP P0DTC2 SER 477 VARIANT SEQADV 8K18 LYS E 478 UNP P0DTC2 THR 478 VARIANT SEQADV 8K18 ALA E 484 UNP P0DTC2 GLU 484 VARIANT SEQADV 8K18 VAL E 486 UNP P0DTC2 PHE 486 VARIANT SEQADV 8K18 SER E 496 UNP P0DTC2 GLY 496 CONFLICT SEQADV 8K18 ARG E 498 UNP P0DTC2 GLN 498 VARIANT SEQADV 8K18 TYR E 501 UNP P0DTC2 ASN 501 VARIANT SEQADV 8K18 HIS E 505 UNP P0DTC2 TYR 505 VARIANT SEQRES 1 E 193 ASN LEU CYS PRO PHE ASP GLU VAL PHE ASN ALA THR LYS SEQRES 2 E 193 PHE PRO SER VAL TYR ALA TRP GLU ARG LYS LYS ILE SER SEQRES 3 E 193 ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN PHE THR SEQRES 4 E 193 PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER ALA THR SEQRES 5 E 193 LYS LEU ASN ASP LEU CYS PHE SER ASN VAL TYR ALA ASP SEQRES 6 E 193 SER PHE VAL VAL LYS GLY ASP ASP VAL SER GLN ILE ALA SEQRES 7 E 193 PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR LYS SEQRES 8 E 193 LEU PRO ASP ASP PHE MET GLY CYS VAL LEU ALA TRP ASN SEQRES 9 E 193 THR ARG LYS ILE ASP ALA THR SER THR GLY ASN TYR ASN SEQRES 10 E 193 TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU LYS PRO SEQRES 11 E 193 PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA GLY SEQRES 12 E 193 ASN LYS PRO CYS ASN GLY VAL ALA GLY VAL ASN CYS TYR SEQRES 13 E 193 PHE PRO LEU GLN SER TYR SER PHE ARG PRO THR TYR GLY SEQRES 14 E 193 VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 15 E 193 GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 1 C 119 GLU VAL GLN LEU VAL GLU SER GLY GLY ASN LEU VAL GLN SEQRES 2 C 119 PRO GLY GLY SER LEU ARG LEU SER CYS GLU VAL SER GLY SEQRES 3 C 119 PHE ILE VAL SER ARG ASN TYR MET SER TRP VAL ARG GLN SEQRES 4 C 119 ALA PRO GLY GLN GLY LEU GLU TRP LEU SER ILE ILE TYR SEQRES 5 C 119 PRO GLY GLY SER THR PHE TYR ALA GLU SER VAL LYS ASP SEQRES 6 C 119 ARG PHE THR ILE SER ARG PRO ASP SER LYS ASN THR LEU SEQRES 7 C 119 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR GLY SEQRES 8 C 119 THR TYR PHE CYS ALA ARG GLY LEU LEU GLU TRP ARG TYR SEQRES 9 C 119 GLY GLN ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SEQRES 10 C 119 SER SER SEQRES 1 D 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 107 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 D 107 GLN ASP VAL ASN GLU ASP LEU ASN TRP TYR GLN GLN LYS SEQRES 4 D 107 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA PHE SEQRES 5 D 107 ASN LEU GLU THR GLY VAL SER SER LYS PHE SER GLY SER SEQRES 6 D 107 GLY SER GLY THR HIS PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 107 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 D 107 GLY HIS GLN ALA LEU SER PHE GLY GLY GLY THR LYS VAL SEQRES 9 D 107 GLU ILE LYS HELIX 1 AA1 PHE E 338 ASN E 343 1 6 HELIX 2 AA2 SER E 349 TRP E 353 5 5 HELIX 3 AA3 ASP E 364 LEU E 368 5 5 HELIX 4 AA4 ASP E 405 ILE E 410 5 6 HELIX 5 AA5 GLY E 416 ASN E 422 1 7 HELIX 6 AA6 THR E 438 ALA E 443 1 6 HELIX 7 AA7 ILE C 28 ASN C 32 5 5 HELIX 8 AA8 ARG C 86 THR C 90 5 5 HELIX 9 AA9 GLN D 79 ILE D 83 5 5 SHEET 1 AA1 4 GLU E 354 ILE E 358 0 SHEET 2 AA1 4 PHE E 392 LYS E 403 -1 O VAL E 395 N ILE E 358 SHEET 3 AA1 4 VAL E 524 CYS E 525 -1 O VAL E 524 N PHE E 392 SHEET 4 AA1 4 CYS E 361 VAL E 362 1 N CYS E 361 O CYS E 525 SHEET 1 AA2 5 GLU E 354 ILE E 358 0 SHEET 2 AA2 5 PHE E 392 LYS E 403 -1 O VAL E 395 N ILE E 358 SHEET 3 AA2 5 PRO E 507 LEU E 517 -1 O VAL E 510 N PHE E 400 SHEET 4 AA2 5 GLY E 431 ASN E 437 -1 N CYS E 432 O LEU E 513 SHEET 5 AA2 5 ALA E 376 TYR E 380 -1 N TYR E 380 O GLY E 431 SHEET 1 AA3 2 ARG E 452 ARG E 454 0 SHEET 2 AA3 2 LEU E 492 SER E 494 -1 O GLN E 493 N TYR E 453 SHEET 1 AA4 2 TYR E 473 GLN E 474 0 SHEET 2 AA4 2 CYS E 488 TYR E 489 -1 O TYR E 489 N TYR E 473 SHEET 1 AA5 6 LEU C 11 VAL C 12 0 SHEET 2 AA5 6 THR C 113 VAL C 117 1 O THR C 116 N VAL C 12 SHEET 3 AA5 6 GLY C 91 ARG C 97 -1 N GLY C 91 O VAL C 115 SHEET 4 AA5 6 MET C 34 GLN C 39 -1 N VAL C 37 O PHE C 94 SHEET 5 AA5 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AA5 6 THR C 57 TYR C 59 -1 O PHE C 58 N ILE C 50 SHEET 1 AA6 3 SER C 17 LEU C 20 0 SHEET 2 AA6 3 TYR C 79 ASN C 83 -1 O MET C 82 N LEU C 18 SHEET 3 AA6 3 PHE C 67 SER C 70 -1 N SER C 70 O TYR C 79 SHEET 1 AA7 4 MET D 4 SER D 7 0 SHEET 2 AA7 4 VAL D 19 ALA D 25 -1 O GLN D 24 N THR D 5 SHEET 3 AA7 4 HIS D 70 ILE D 75 -1 O PHE D 71 N CYS D 23 SHEET 4 AA7 4 PHE D 62 SER D 65 -1 N SER D 65 O THR D 72 SHEET 1 AA8 2 SER D 10 ALA D 13 0 SHEET 2 AA8 2 LYS D 103 ILE D 106 1 O GLU D 105 N ALA D 13 SHEET 1 AA9 5 ASN D 53 LEU D 54 0 SHEET 2 AA9 5 PRO D 44 TYR D 49 -1 N TYR D 49 O ASN D 53 SHEET 3 AA9 5 LEU D 33 GLN D 38 -1 N TRP D 35 O LEU D 47 SHEET 4 AA9 5 THR D 85 GLN D 90 -1 O TYR D 87 N TYR D 36 SHEET 5 AA9 5 SER D 97 PHE D 98 -1 O SER D 97 N GLN D 90 SSBOND 1 CYS E 336 CYS E 361 1555 1555 2.01 SSBOND 2 CYS E 379 CYS E 432 1555 1555 2.05 SSBOND 3 CYS E 480 CYS E 488 1555 1555 2.02 SSBOND 4 CYS D 23 CYS D 88 1555 1555 2.04 CISPEP 1 GLY C 91 THR C 92 0 -7.53 CISPEP 2 SER D 7 PRO D 8 0 -16.75 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