HEADER TOXIN 03-JUL-24 9FYT TITLE MABS IN COMPLEX WITH COBRATOXIN AT PH 4.5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-COBRATOXIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: ALPHA-CT,ALPHA-CBT,ALPHA-CBTX,ALPHA-CTX,ALPHA-ELAPITOXIN- COMPND 5 NK2A,ALPHA-EPTX-NK2A,LONG NEUROTOXIN 1,SIAMENSIS 3; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: LIGHT CHAIN SCFV A01; COMPND 9 CHAIN: I, C; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: HEAVY CHAIN SCFV AO1; COMPND 13 CHAIN: M, D; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NAJA KAOUTHIA; SOURCE 3 ORGANISM_COMMON: MONOCLED COBRA; SOURCE 4 ORGANISM_TAXID: 8649; SOURCE 5 EXPRESSION_SYSTEM: NAJA KAOUTHIA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 8649; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MABS, COBRATOXIN, ANTIBODY:TOXIN COMPLEX, TOXIN EXPDTA X-RAY DIFFRACTION AUTHOR J.WADE,M.F.BOHN,A.H.LAUSTSEN,J.P.MORTH REVDAT 1 16-JUL-25 9FYT 0 JRNL AUTH J.WADE JRNL TITL STRUCTURAL MECHANISMS OF A-NEUROTOXIN-NEUTRALIZING JRNL TITL 2 ANTIBODIES ENABLE RATIONAL DESIGN OF PH-DEPENDENT ANTIGEN JRNL TITL 3 BINDING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.52 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 88771 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.188 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 8834 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 42.5200 - 4.8100 0.99 5584 303 0.1572 0.1769 REMARK 3 2 4.8100 - 3.8200 0.99 5632 280 0.1228 0.1576 REMARK 3 3 3.8200 - 3.3400 0.99 5513 404 0.1490 0.2108 REMARK 3 4 3.3400 - 3.0300 0.99 5698 234 0.1686 0.2506 REMARK 3 5 3.0300 - 2.8200 0.99 5584 299 0.1771 0.2488 REMARK 3 6 2.8200 - 2.6500 0.99 5602 291 0.1770 0.2124 REMARK 3 7 2.6500 - 2.5200 0.99 5683 303 0.1707 0.2104 REMARK 3 8 2.5200 - 2.4100 1.00 5609 290 0.1619 0.2363 REMARK 3 9 2.4100 - 2.3200 1.00 5637 268 0.1634 0.2250 REMARK 3 10 2.3200 - 2.2400 1.00 5682 267 0.1704 0.2389 REMARK 3 11 2.2400 - 2.1700 0.99 5666 276 0.1686 0.2473 REMARK 3 12 2.1700 - 2.1000 0.99 5682 271 0.1683 0.2096 REMARK 3 13 2.1000 - 2.0500 1.00 5580 301 0.1790 0.2567 REMARK 3 14 2.0500 - 2.0000 1.00 5668 278 0.1877 0.2623 REMARK 3 15 2.0000 - 1.9500 1.00 5619 321 0.1824 0.2488 REMARK 3 16 1.9500 - 1.9100 0.99 5628 287 0.2038 0.2909 REMARK 3 17 1.9100 - 1.8700 0.99 5619 343 0.2236 0.2995 REMARK 3 18 1.8700 - 1.8400 1.00 5574 316 0.2361 0.3024 REMARK 3 19 1.8400 - 1.8000 1.00 5682 299 0.2550 0.2871 REMARK 3 20 1.8000 - 1.7700 0.99 5626 277 0.2573 0.3136 REMARK 3 21 1.7700 - 1.7500 1.00 5646 268 0.2760 0.3200 REMARK 3 22 1.7500 - 1.7200 1.00 5647 321 0.2826 0.3364 REMARK 3 23 1.7200 - 1.6900 0.99 5664 287 0.3044 0.3693 REMARK 3 24 1.6900 - 1.6700 1.00 5618 302 0.3291 0.3738 REMARK 3 25 1.6700 - 1.6500 1.00 5598 330 0.3433 0.4083 REMARK 3 26 1.6500 - 1.6300 1.00 5695 272 0.3636 0.3816 REMARK 3 27 1.6300 - 1.6100 0.99 5647 249 0.3830 0.3886 REMARK 3 28 1.6100 - 1.5900 0.99 5654 286 0.3984 0.4369 REMARK 3 29 1.5900 - 1.5700 0.99 5612 306 0.4291 0.4579 REMARK 3 30 1.5700 - 1.5500 0.95 5359 305 0.4446 0.4480 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.254 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.292 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.44 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 5049 REMARK 3 ANGLE : 1.024 6877 REMARK 3 CHIRALITY : 0.065 743 REMARK 3 PLANARITY : 0.009 899 REMARK 3 DIHEDRAL : 7.319 730 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9FYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292139978. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-OCT-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92830 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550 REMARK 200 RESOLUTION RANGE LOW (A) : 42.520 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.8600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 0.2 M AMMONIUM REMARK 280 SULFATE, 25% PEG 3350, PH 4.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 38.43000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.32500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.93000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.32500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.43000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.93000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28920 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, M, 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 ALA I 0 REMARK 465 GLY I 114 REMARK 465 GLY I 115 REMARK 465 GLY I 116 REMARK 465 GLY I 117 REMARK 465 SER I 118 REMARK 465 GLY I 119 REMARK 465 GLY I 120 REMARK 465 GLY I 121 REMARK 465 GLY I 122 REMARK 465 SER I 123 REMARK 465 GLY I 124 REMARK 465 GLY I 125 REMARK 465 GLY M -2 REMARK 465 ALA M -1 REMARK 465 GLN M 1006 REMARK 465 ALA C 0 REMARK 465 GLY C 114 REMARK 465 GLY C 115 REMARK 465 GLY C 116 REMARK 465 GLY C 117 REMARK 465 SER C 118 REMARK 465 GLY C 119 REMARK 465 GLY C 120 REMARK 465 GLY C 121 REMARK 465 GLY C 122 REMARK 465 SER C 123 REMARK 465 GLY C 124 REMARK 465 GLY C 125 REMARK 465 GLY D -2 REMARK 465 ALA D -1 REMARK 465 GLN D 1006 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 HH21 ARG I 83 O HOH I 301 1.57 REMARK 500 OG SER I 30 OE2 GLU I 73 1.68 REMARK 500 O HOH I 307 O HOH I 392 1.98 REMARK 500 NH2 ARG I 83 O HOH I 301 2.13 REMARK 500 O HOH B 254 O HOH D 1277 2.19 REMARK 500 O HOH D 1249 O HOH D 1293 2.19 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 ASP A 27 -166.51 -101.68 REMARK 500 ASN A 63 56.89 -118.49 REMARK 500 ASP B 27 -167.74 -102.50 REMARK 500 ASN B 63 56.13 -119.85 REMARK 500 THR I 28 92.50 50.52 REMARK 500 GLN I 43 -169.47 -109.69 REMARK 500 TYR I 100J 116.06 -168.81 REMARK 500 ASP M 51 -45.69 74.34 REMARK 500 SER M 52 -1.80 -142.76 REMARK 500 ALA M 84 175.45 179.68 REMARK 500 TYR C 100J 116.61 -171.33 REMARK 500 ASP D 51 -47.94 77.97 REMARK 500 SER D 52 -0.03 -148.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 287 DISTANCE = 6.13 ANGSTROMS REMARK 525 HOH D1310 DISTANCE = 6.35 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA M1102 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ARG M 61 O REMARK 620 2 SER M 63 OG 115.1 REMARK 620 3 SER M 76 OG 93.2 147.4 REMARK 620 4 HOH M1226 O 88.7 94.4 102.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA D1103 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ARG D 61 O REMARK 620 2 SER D 63 OG 120.6 REMARK 620 3 SER D 76 OG 91.5 146.1 REMARK 620 4 HOH D1238 O 82.7 98.6 95.9 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9FYS RELATED DB: PDB DBREF 9FYT A 1 71 UNP P01391 3L21_NAJKA 1 71 DBREF 9FYT B 1 71 UNP P01391 3L21_NAJKA 1 71 DBREF 9FYT I 0 125 PDB 9FYT 9FYT 0 125 DBREF 9FYT M -2 1006 PDB 9FYT 9FYT -2 1006 DBREF 9FYT C 0 125 PDB 9FYT 9FYT 0 125 DBREF 9FYT D -2 1006 PDB 9FYT 9FYT -2 1006 SEQRES 1 A 71 ILE ARG CYS PHE ILE THR PRO ASP ILE THR SER LYS ASP SEQRES 2 A 71 CYS PRO ASN GLY HIS VAL CYS TYR THR LYS THR TRP CYS SEQRES 3 A 71 ASP ALA PHE CYS SER ILE ARG GLY LYS ARG VAL ASP LEU SEQRES 4 A 71 GLY CYS ALA ALA THR CYS PRO THR VAL LYS THR GLY VAL SEQRES 5 A 71 ASP ILE GLN CYS CYS SER THR ASP ASN CYS ASN PRO PHE SEQRES 6 A 71 PRO THR ARG LYS ARG PRO SEQRES 1 B 71 ILE ARG CYS PHE ILE THR PRO ASP ILE THR SER LYS ASP SEQRES 2 B 71 CYS PRO ASN GLY HIS VAL CYS TYR THR LYS THR TRP CYS SEQRES 3 B 71 ASP ALA PHE CYS SER ILE ARG GLY LYS ARG VAL ASP LEU SEQRES 4 B 71 GLY CYS ALA ALA THR CYS PRO THR VAL LYS THR GLY VAL SEQRES 5 B 71 ASP ILE GLN CYS CYS SER THR ASP ASN CYS ASN PRO PHE SEQRES 6 B 71 PRO THR ARG LYS ARG PRO SEQRES 1 I 144 ALA GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS SEQRES 2 I 144 LYS PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER SEQRES 3 I 144 GLY GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG SEQRES 4 I 144 GLN ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE SEQRES 5 I 144 ILE PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE SEQRES 6 I 144 GLN GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER SEQRES 7 I 144 THR ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP SEQRES 8 I 144 THR ALA VAL TYR TYR CYS ALA ARG ASP ASN LEU GLY TYR SEQRES 9 I 144 CYS SER GLY GLY SER CYS TYR SER ASP TYR TYR TYR TYR SEQRES 10 I 144 TYR MET ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 11 I 144 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 12 I 144 GLY SEQRES 1 M 117 GLY ALA SER SER TYR GLU LEU THR GLN PRO PRO SER VAL SEQRES 2 M 117 SER VAL ALA PRO GLY ARG THR ALA THR ILE THR CYS GLU SEQRES 3 M 117 GLY ASP ASN ILE GLY GLN GLN ILE VAL HIS TRP TYR GLN SEQRES 4 M 117 GLN LYS PRO GLY GLN ALA PRO VAL ALA VAL ILE SER SER SEQRES 5 M 117 ASP SER ASP ARG PRO SER GLY ILE PRO GLU ARG PHE SER SEQRES 6 M 117 GLY SER ASN SER GLY ASN THR ALA THR LEU THR ILE SER SEQRES 7 M 117 ARG VAL GLU ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 M 117 VAL TRP ASP SER GLY SER ASP HIS VAL VAL PHE GLY GLY SEQRES 9 M 117 GLY THR LYS VAL THR VAL LEU GLU ASN LEU TYR PHE GLN SEQRES 1 C 144 ALA GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS SEQRES 2 C 144 LYS PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER SEQRES 3 C 144 GLY GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG SEQRES 4 C 144 GLN ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE SEQRES 5 C 144 ILE PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE SEQRES 6 C 144 GLN GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER SEQRES 7 C 144 THR ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP SEQRES 8 C 144 THR ALA VAL TYR TYR CYS ALA ARG ASP ASN LEU GLY TYR SEQRES 9 C 144 CYS SER GLY GLY SER CYS TYR SER ASP TYR TYR TYR TYR SEQRES 10 C 144 TYR MET ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 11 C 144 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 12 C 144 GLY SEQRES 1 D 117 GLY ALA SER SER TYR GLU LEU THR GLN PRO PRO SER VAL SEQRES 2 D 117 SER VAL ALA PRO GLY ARG THR ALA THR ILE THR CYS GLU SEQRES 3 D 117 GLY ASP ASN ILE GLY GLN GLN ILE VAL HIS TRP TYR GLN SEQRES 4 D 117 GLN LYS PRO GLY GLN ALA PRO VAL ALA VAL ILE SER SER SEQRES 5 D 117 ASP SER ASP ARG PRO SER GLY ILE PRO GLU ARG PHE SER SEQRES 6 D 117 GLY SER ASN SER GLY ASN THR ALA THR LEU THR ILE SER SEQRES 7 D 117 ARG VAL GLU ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 D 117 VAL TRP ASP SER GLY SER ASP HIS VAL VAL PHE GLY GLY SEQRES 9 D 117 GLY THR LYS VAL THR VAL LEU GLU ASN LEU TYR PHE GLN HET CL A 101 1 HET CL A 102 1 HET CL A 103 2 HET GOL B 101 13 HET GOL B 102 14 HET SO4 I 201 5 HET GOL M1101 14 HET NA M1102 1 HET GOL D1101 13 HET GOL D1102 13 HET NA D1103 1 HETNAM CL CHLORIDE ION HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETNAM NA SODIUM ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 CL 3(CL 1-) FORMUL 10 GOL 5(C3 H8 O3) FORMUL 12 SO4 O4 S 2- FORMUL 14 NA 2(NA 1+) FORMUL 18 HOH *521(H2 O) HELIX 1 AA1 PHE A 29 GLY A 34 1 6 HELIX 2 AA2 PHE B 29 GLY B 34 1 6 HELIX 3 AA3 ARG I 83 THR I 87 5 5 HELIX 4 AA4 ASN M 27 GLN M 31 5 5 HELIX 5 AA5 GLU M 79 GLU M 83 5 5 HELIX 6 AA6 PRO C 52A GLY C 55 5 4 HELIX 7 AA7 GLU C 73 THR C 75 5 3 HELIX 8 AA8 ARG C 83 THR C 87 5 5 HELIX 9 AA9 ASN D 27 GLN D 31 5 5 HELIX 10 AB1 GLU D 79 GLU D 83 5 5 SHEET 1 AA1 2 ARG A 2 ILE A 5 0 SHEET 2 AA1 2 THR A 10 ASP A 13 -1 O LYS A 12 N CYS A 3 SHEET 1 AA2 5 ASP A 53 CYS A 57 0 SHEET 2 AA2 5 VAL A 19 TRP A 25 -1 N THR A 24 O ASP A 53 SHEET 3 AA2 5 ARG A 36 ALA A 42 -1 O ASP A 38 N LYS A 23 SHEET 4 AA2 5 SER C 100D TYR C 100F-1 O CYS C 100E N VAL A 37 SHEET 5 AA2 5 CYS C 100 SER C 100A-1 N SER C 100A O SER C 100D SHEET 1 AA3 2 ARG B 2 ILE B 5 0 SHEET 2 AA3 2 THR B 10 ASP B 13 -1 O LYS B 12 N CYS B 3 SHEET 1 AA4 5 ASP B 53 CYS B 57 0 SHEET 2 AA4 5 VAL B 19 TRP B 25 -1 N THR B 24 O ASP B 53 SHEET 3 AA4 5 ARG B 36 ALA B 42 -1 O ASP B 38 N LYS B 23 SHEET 4 AA4 5 SER I 100D TYR I 100F-1 O CYS I 100E N VAL B 37 SHEET 5 AA4 5 CYS I 100 SER I 100A-1 N SER I 100A O SER I 100D SHEET 1 AA5 4 LEU I 4 GLN I 6 0 SHEET 2 AA5 4 VAL I 18 ALA I 24 -1 O LYS I 23 N VAL I 5 SHEET 3 AA5 4 THR I 77 LEU I 82 -1 O ALA I 78 N CYS I 22 SHEET 4 AA5 4 VAL I 67 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AA6 6 GLU I 10 LYS I 12 0 SHEET 2 AA6 6 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12 SHEET 3 AA6 6 ALA I 88 ASP I 95 -1 N TYR I 90 O THR I 107 SHEET 4 AA6 6 ILE I 34 GLN I 39 -1 N VAL I 37 O TYR I 91 SHEET 5 AA6 6 LEU I 45 ILE I 52 -1 O MET I 48 N TRP I 36 SHEET 6 AA6 6 THR I 56 TYR I 59 -1 O ASN I 58 N GLY I 50 SHEET 1 AA7 4 GLU I 10 LYS I 12 0 SHEET 2 AA7 4 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12 SHEET 3 AA7 4 ALA I 88 ASP I 95 -1 N TYR I 90 O THR I 107 SHEET 4 AA7 4 MET I 100N TRP I 103 -1 O VAL I 102 N ARG I 94 SHEET 1 AA8 5 SER M 9 VAL M 13 0 SHEET 2 AA8 5 THR M 102 VAL M 106 1 O THR M 105 N VAL M 11 SHEET 3 AA8 5 ALA M 84 ASP M 92 -1 N ALA M 84 O VAL M 104 SHEET 4 AA8 5 HIS M 34 GLN M 38 -1 N GLN M 38 O ASP M 85 SHEET 5 AA8 5 VAL M 45 ILE M 48 -1 O VAL M 45 N GLN M 37 SHEET 1 AA9 4 SER M 9 VAL M 13 0 SHEET 2 AA9 4 THR M 102 VAL M 106 1 O THR M 105 N VAL M 11 SHEET 3 AA9 4 ALA M 84 ASP M 92 -1 N ALA M 84 O VAL M 104 SHEET 4 AA9 4 HIS M 95B PHE M 98 -1 O HIS M 95B N ASP M 92 SHEET 1 AB1 3 ALA M 19 GLU M 24 0 SHEET 2 AB1 3 THR M 70 ILE M 75 -1 O ILE M 75 N ALA M 19 SHEET 3 AB1 3 PHE M 62 SER M 67 -1 N SER M 63 O THR M 74 SHEET 1 AB2 4 GLN C 3 GLN C 6 0 SHEET 2 AB2 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AB2 4 THR C 77 LEU C 82 -1 O ALA C 78 N CYS C 22 SHEET 4 AB2 4 VAL C 67 ASP C 72 -1 N ASP C 72 O THR C 77 SHEET 1 AB3 6 GLU C 10 LYS C 12 0 SHEET 2 AB3 6 THR C 107 VAL C 111 1 O THR C 110 N LYS C 12 SHEET 3 AB3 6 ALA C 88 ASP C 95 -1 N ALA C 88 O VAL C 109 SHEET 4 AB3 6 ILE C 34 GLN C 39 -1 N VAL C 37 O TYR C 91 SHEET 5 AB3 6 LEU C 45 ILE C 52 -1 O MET C 48 N TRP C 36 SHEET 6 AB3 6 THR C 56 TYR C 59 -1 O ASN C 58 N GLY C 50 SHEET 1 AB4 4 GLU C 10 LYS C 12 0 SHEET 2 AB4 4 THR C 107 VAL C 111 1 O THR C 110 N LYS C 12 SHEET 3 AB4 4 ALA C 88 ASP C 95 -1 N ALA C 88 O VAL C 109 SHEET 4 AB4 4 MET C 100N TRP C 103 -1 O VAL C 102 N ARG C 94 SHEET 1 AB5 5 SER D 9 VAL D 13 0 SHEET 2 AB5 5 THR D 102 VAL D 106 1 O THR D 105 N VAL D 11 SHEET 3 AB5 5 ALA D 84 ASP D 92 -1 N ALA D 84 O VAL D 104 SHEET 4 AB5 5 HIS D 34 GLN D 38 -1 N GLN D 38 O ASP D 85 SHEET 5 AB5 5 VAL D 45 ILE D 48 -1 O VAL D 45 N GLN D 37 SHEET 1 AB6 4 SER D 9 VAL D 13 0 SHEET 2 AB6 4 THR D 102 VAL D 106 1 O THR D 105 N VAL D 11 SHEET 3 AB6 4 ALA D 84 ASP D 92 -1 N ALA D 84 O VAL D 104 SHEET 4 AB6 4 HIS D 95B PHE D 98 -1 O HIS D 95B N ASP D 92 SHEET 1 AB7 3 ALA D 19 GLU D 24 0 SHEET 2 AB7 3 THR D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 3 AB7 3 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SSBOND 1 CYS A 3 CYS A 20 1555 1555 2.04 SSBOND 2 CYS A 14 CYS A 41 1555 1555 2.07 SSBOND 3 CYS A 26 CYS A 30 1555 1555 2.08 SSBOND 4 CYS A 45 CYS A 56 1555 1555 2.06 SSBOND 5 CYS A 57 CYS A 62 1555 1555 2.03 SSBOND 6 CYS B 3 CYS B 20 1555 1555 2.03 SSBOND 7 CYS B 14 CYS B 41 1555 1555 2.05 SSBOND 8 CYS B 26 CYS B 30 1555 1555 2.07 SSBOND 9 CYS B 45 CYS B 56 1555 1555 2.06 SSBOND 10 CYS B 57 CYS B 62 1555 1555 2.06 SSBOND 11 CYS I 22 CYS I 92 1555 1555 2.05 SSBOND 12 CYS I 100 CYS I 100E 1555 1555 2.14 SSBOND 13 CYS M 23 CYS M 88 1555 1555 2.09 SSBOND 14 CYS C 22 CYS C 92 1555 1555 2.07 SSBOND 15 CYS C 100 CYS C 100E 1555 1555 2.14 SSBOND 16 CYS D 23 CYS D 88 1555 1555 2.10 LINK O ARG M 61 NA NA M1102 1555 1555 3.04 LINK OG SER M 63 NA NA M1102 1555 1555 2.78 LINK OG SER M 76 NA NA M1102 1555 1555 3.12 LINK NA NA M1102 O HOH M1226 1555 1555 2.63 LINK O ARG D 61 NA NA D1103 1555 1555 2.83 LINK OG SER D 63 NA NA D1103 1555 1555 2.75 LINK OG SER D 76 NA NA D1103 1555 1555 2.68 LINK NA NA D1103 O HOH D1238 1555 1555 2.66 CISPEP 1 THR A 6 PRO A 7 0 7.51 CISPEP 2 THR B 6 PRO B 7 0 6.54 CRYST1 76.860 83.860 98.650 90.00 90.00 90.00 P 21 21 21 8 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 0.013011 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011925 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010137 0.00000