HEADER TOXIN 21-DEC-24 9HUB TITLE D11 MABS BOUND TO ALPHA-BUNGAROTOXIN AT PH 7.5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN; COMPND 3 CHAIN: C, M; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ALPHA-BUNGAROTOXIN; COMPND 7 CHAIN: X, Z; COMPND 8 SYNONYM: ALPHA-BGTX,ALPHA-BTX,ALPHA-BUNGAROTOXIN,ISOFORM A31,ALPHA- COMPND 9 BTX A31,ALPHA-BGTX(A31),ALPHA-BUNGAROTOXIN (A31),BGTX A31,ALPHA- COMPND 10 ELAPITOXIN-BM2A,ALPHA-EPTX-BM2A,LONG NEUROTOXIN 1; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: LIGHT CHAIN; COMPND 13 CHAIN: I, B; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 561; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS; SOURCE 8 ORGANISM_COMMON: MANY-BANDED KRAIT; SOURCE 9 ORGANISM_TAXID: 8616; SOURCE 10 MOL_ID: 3; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 561 KEYWDS PH, TOXIN, ANTIBODY EXPDTA X-RAY DIFFRACTION AUTHOR J.W.WADE,M.F.BOHN,A.H.LAUSTSEN,J.P.MORTH REVDAT 1 19-NOV-25 9HUB 0 JRNL AUTH J.WADE,N.STRANCAR,M.L.FERNANDEZ-QUINTERO,S.SIEBENHAAR, JRNL AUTH 2 T.JANSEN,E.P.W.MEIER,T.P.JENKINS,S.P.BJORN,G.T.T.NGUYEN, JRNL AUTH 3 B.LOMONTE,J.M.GUTIERREZ,C.V.SORENSEN,J.R.LOEFFLER,A.PAUL, JRNL AUTH 4 T.TULIKA,J.ARNSDORF,S.SCHOFFELEN,E.V.S.LUNDQUIST,J.SORENSEN, JRNL AUTH 5 A.B.WARD,B.G.VOLDBORG,M.F.BOHN,E.RIVERA-DE-TORRE,J.P.MORTH, JRNL AUTH 6 A.H.LAUSTSEN JRNL TITL RATIONAL DESIGN OF ANTIBODIES WITH PH-DEPENDENT JRNL TITL 2 ANTIGEN-BINDING PROPERTIES USING STRUCTURAL INSIGHTS FROM JRNL TITL 3 BROADLY NEUTRALIZING ANTIBODIES AGAINST ALPHA-NEUROTOXINS. JRNL REF MABS V. 17 53624 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40936197 JRNL DOI 10.1080/19420862.2025.2553624 REMARK 2 REMARK 2 RESOLUTION. 1.33 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5156 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) : 1.33 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.38 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 158001 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.161 REMARK 3 R VALUE (WORKING SET) : 0.159 REMARK 3 FREE R VALUE : 0.195 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 8021 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 22.3800 - 4.1200 0.99 5276 326 0.1552 0.1745 REMARK 3 2 4.1200 - 3.2800 1.00 5177 245 0.1431 0.1858 REMARK 3 3 3.2800 - 2.8600 1.00 5143 233 0.1480 0.1784 REMARK 3 4 2.8600 - 2.6000 1.00 5076 286 0.1395 0.1584 REMARK 3 5 2.6000 - 2.4200 1.00 5043 272 0.1335 0.1810 REMARK 3 6 2.4200 - 2.2700 1.00 5052 245 0.1328 0.1684 REMARK 3 7 2.2700 - 2.1600 1.00 5055 270 0.1396 0.1695 REMARK 3 8 2.1600 - 2.0700 1.00 4995 283 0.1360 0.1759 REMARK 3 9 2.0700 - 1.9900 1.00 5061 247 0.1334 0.1707 REMARK 3 10 1.9900 - 1.9200 1.00 5039 252 0.1322 0.1817 REMARK 3 11 1.9200 - 1.8600 1.00 5033 263 0.1356 0.1875 REMARK 3 12 1.8600 - 1.8000 1.00 4936 287 0.1339 0.1744 REMARK 3 13 1.8000 - 1.7600 1.00 5017 276 0.1364 0.1796 REMARK 3 14 1.7600 - 1.7100 1.00 5004 270 0.1462 0.2179 REMARK 3 15 1.7100 - 1.6800 1.00 4966 305 0.1582 0.2061 REMARK 3 16 1.6800 - 1.6400 1.00 4955 289 0.1667 0.2269 REMARK 3 17 1.6400 - 1.6100 1.00 4974 260 0.1720 0.2161 REMARK 3 18 1.6100 - 1.5800 1.00 5017 241 0.1879 0.2268 REMARK 3 19 1.5800 - 1.5500 1.00 4998 243 0.2091 0.2434 REMARK 3 20 1.5500 - 1.5200 1.00 5011 245 0.2186 0.2759 REMARK 3 21 1.5200 - 1.5000 1.00 4993 261 0.2233 0.2788 REMARK 3 22 1.5000 - 1.4700 1.00 4957 254 0.2445 0.2836 REMARK 3 23 1.4700 - 1.4500 1.00 5003 257 0.2635 0.3148 REMARK 3 24 1.4500 - 1.4300 1.00 4961 252 0.2862 0.3124 REMARK 3 25 1.4300 - 1.4100 1.00 4936 280 0.3024 0.3265 REMARK 3 26 1.4100 - 1.3900 1.00 4974 280 0.3285 0.3538 REMARK 3 27 1.3900 - 1.3800 1.00 4964 280 0.3497 0.3682 REMARK 3 28 1.3800 - 1.3600 1.00 4931 280 0.3644 0.4073 REMARK 3 29 1.3600 - 1.3400 0.98 4891 269 0.4021 0.4127 REMARK 3 30 1.3400 - 1.3300 0.92 4542 270 0.4235 0.4132 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) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.497 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.91 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.74 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 : 0.008 5253 REMARK 3 ANGLE : 0.996 7139 REMARK 3 CHIRALITY : 0.085 762 REMARK 3 PLANARITY : 0.011 937 REMARK 3 DIHEDRAL : 16.189 1913 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 9HUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292144249. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUL-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 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) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 158613 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330 REMARK 200 RESOLUTION RANGE LOW (A) : 22.380 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 13.30 REMARK 200 R MERGE (I) : 0.12280 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.4400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.34 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.00000 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 (%): 44.92 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 70% (V/V) MPD), REMARK 280 VAPOR DIFFUSION, 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 39.52550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.41450 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.36750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.41450 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.52550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.36750 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4340 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15060 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, X, B 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15250 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z, I, M 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 GLY C 144 REMARK 465 GLN C 264 REMARK 465 MET X -20 REMARK 465 LYS X -19 REMARK 465 THR X -18 REMARK 465 LEU X -17 REMARK 465 LEU X -16 REMARK 465 LEU X -15 REMARK 465 THR X -14 REMARK 465 LEU X -13 REMARK 465 VAL X -12 REMARK 465 VAL X -11 REMARK 465 VAL X -10 REMARK 465 THR X -9 REMARK 465 ILE X -8 REMARK 465 VAL X -7 REMARK 465 CYS X -6 REMARK 465 LEU X -5 REMARK 465 ASP X -4 REMARK 465 LEU X -3 REMARK 465 GLY X -2 REMARK 465 TYR X -1 REMARK 465 THR X 0 REMARK 465 GLY X 74 REMARK 465 MET Z -20 REMARK 465 LYS Z -19 REMARK 465 THR Z -18 REMARK 465 LEU Z -17 REMARK 465 LEU Z -16 REMARK 465 LEU Z -15 REMARK 465 THR Z -14 REMARK 465 LEU Z -13 REMARK 465 VAL Z -12 REMARK 465 VAL Z -11 REMARK 465 VAL Z -10 REMARK 465 THR Z -9 REMARK 465 ILE Z -8 REMARK 465 VAL Z -7 REMARK 465 CYS Z -6 REMARK 465 LEU Z -5 REMARK 465 ASP Z -4 REMARK 465 LEU Z -3 REMARK 465 GLY Z -2 REMARK 465 TYR Z -1 REMARK 465 THR Z 0 REMARK 465 ALA I 0 REMARK 465 GLY I 134 REMARK 465 GLY I 135 REMARK 465 SER I 136 REMARK 465 GLY I 137 REMARK 465 GLY I 138 REMARK 465 GLY I 139 REMARK 465 GLY I 140 REMARK 465 SER I 141 REMARK 465 GLY I 142 REMARK 465 GLY I 143 REMARK 465 GLY M 144 REMARK 465 ALA B 0 REMARK 465 GLY B 134 REMARK 465 GLY B 135 REMARK 465 SER B 136 REMARK 465 GLY B 137 REMARK 465 GLY B 138 REMARK 465 GLY B 139 REMARK 465 GLY B 140 REMARK 465 SER B 141 REMARK 465 GLY B 142 REMARK 465 GLY B 143 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 ALA M 145 CB 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 HOH I 294 O HOH I 342 1.75 REMARK 500 O HOH M 463 O HOH M 467 1.77 REMARK 500 O HOH X 285 O HOH X 301 1.79 REMARK 500 O HOH C 420 O HOH C 421 1.80 REMARK 500 NZ LYS M 254 O HOH M 401 1.81 REMARK 500 O HOH Z 149 O HOH Z 183 1.83 REMARK 500 O HOH X 221 O HOH X 285 1.84 REMARK 500 O HOH M 416 O HOH M 528 1.84 REMARK 500 O HOH B 357 O HOH B 486 1.85 REMARK 500 O HOH C 466 O HOH C 489 1.85 REMARK 500 O HOH C 500 O HOH C 533 1.86 REMARK 500 O HOH X 206 O HOH X 263 1.87 REMARK 500 O HOH M 530 O HOH M 557 1.89 REMARK 500 O HOH B 301 O HOH B 444 1.94 REMARK 500 O HOH Z 106 O HOH Z 175 1.94 REMARK 500 O HOH X 227 O HOH X 292 1.95 REMARK 500 O HOH C 505 O HOH C 514 1.96 REMARK 500 O HOH C 525 O HOH B 426 1.97 REMARK 500 O HOH Z 194 O HOH Z 195 1.99 REMARK 500 O HOH I 336 O HOH M 559 2.00 REMARK 500 O HOH I 202 O HOH I 270 2.01 REMARK 500 O HOH X 229 O HOH Z 172 2.01 REMARK 500 O HOH C 530 O HOH C 536 2.01 REMARK 500 O HOH Z 102 O HOH Z 124 2.03 REMARK 500 O HOH X 228 O HOH B 475 2.03 REMARK 500 O HOH M 476 O HOH M 533 2.04 REMARK 500 O HOH M 458 O HOH M 538 2.04 REMARK 500 O HOH B 416 O HOH B 461 2.06 REMARK 500 O HOH I 311 O HOH I 342 2.07 REMARK 500 O HOH B 302 O HOH B 456 2.07 REMARK 500 O HOH I 267 O HOH I 365 2.08 REMARK 500 O HOH M 507 O HOH M 522 2.09 REMARK 500 O HOH M 428 O HOH M 543 2.09 REMARK 500 O HOH I 339 O HOH I 361 2.09 REMARK 500 O HOH B 427 O HOH B 506 2.10 REMARK 500 O HOH I 235 O HOH M 559 2.11 REMARK 500 O HOH Z 128 O HOH Z 186 2.12 REMARK 500 O HOH I 346 O HOH I 363 2.13 REMARK 500 O HOH X 240 O HOH M 516 2.14 REMARK 500 O HOH M 401 O HOH M 541 2.14 REMARK 500 O HOH I 221 O HOH I 272 2.15 REMARK 500 O HOH B 461 O HOH B 492 2.16 REMARK 500 O HOH M 550 O HOH M 584 2.18 REMARK 500 O HOH X 270 O HOH M 404 2.19 REMARK 500 O HOH X 276 O HOH X 294 2.19 REMARK 500 O HOH I 287 O HOH I 324 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH C 505 O HOH X 203 3545 1.90 REMARK 500 O HOH Z 189 O HOH B 397 3555 1.94 REMARK 500 O HOH Z 192 O HOH B 440 2445 1.95 REMARK 500 O HOH I 259 O HOH B 468 2445 1.97 REMARK 500 O HOH Z 160 O HOH B 479 3555 1.98 REMARK 500 O HOH I 330 O HOH B 337 2445 2.04 REMARK 500 O HOH X 285 O HOH Z 191 2444 2.14 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 C 198 -46.10 76.59 REMARK 500 ASN C 199 12.88 -150.01 REMARK 500 ALA C 233 172.28 178.28 REMARK 500 SER C 239 -159.49 -145.30 REMARK 500 ASN X 66 59.72 -117.66 REMARK 500 ASN Z 66 59.98 -119.18 REMARK 500 THR I 28 -168.69 -75.37 REMARK 500 SER I 30 -128.58 48.12 REMARK 500 SER I 77 53.63 37.46 REMARK 500 ASP M 198 -47.29 78.30 REMARK 500 ASN M 199 12.97 -147.45 REMARK 500 ALA M 233 178.02 177.10 REMARK 500 SER B 30 -137.01 51.10 REMARK 500 SER B 30 -137.70 47.31 REMARK 500 SER B 105 148.83 -170.15 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 ARG X 25 0.08 SIDE CHAIN 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 557 DISTANCE = 5.81 ANGSTROMS REMARK 525 HOH I 378 DISTANCE = 5.97 ANGSTROMS REMARK 525 HOH I 379 DISTANCE = 6.15 ANGSTROMS REMARK 525 HOH B 521 DISTANCE = 6.00 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9FYS RELATED DB: PDB REMARK 900 PH 4.5 DBREF 9HUB C 144 264 PDB 9HUB 9HUB 144 264 DBREF 9HUB X -20 74 UNP P60615 3L21A_BUNMU 1 95 DBREF 9HUB Z -20 74 UNP P60615 3L21A_BUNMU 1 95 DBREF 9HUB I 0 143 PDB 9HUB 9HUB 0 143 DBREF 9HUB M 144 264 PDB 9HUB 9HUB 144 264 DBREF 9HUB B 0 143 PDB 9HUB 9HUB 0 143 SEQRES 1 C 121 GLY ALA SER ASN PHE MET LEU THR GLN PRO ARG SER VAL SEQRES 2 C 121 SER GLU SER PRO GLY LYS THR VAL THR ILE SER CYS THR SEQRES 3 C 121 ARG SER SER GLY SER ILE GLY SER ASP TYR VAL HIS TRP SEQRES 4 C 121 TYR GLN GLN ARG PRO GLY SER SER PRO THR THR VAL ILE SEQRES 5 C 121 TYR GLU ASP ASN GLN ARG PRO SER GLY VAL PRO ASP ARG SEQRES 6 C 121 PHE SER GLY SER ILE ASP SER SER SER ASN SER ALA SER SEQRES 7 C 121 LEU THR ILE SER GLY LEU LYS THR GLU ASP GLU ALA ASP SEQRES 8 C 121 TYR TYR CYS GLN SER TYR ASP ARG SER ASN HIS GLU VAL SEQRES 9 C 121 VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLU ASN SEQRES 10 C 121 LEU TYR PHE GLN SEQRES 1 X 95 MET LYS THR LEU LEU LEU THR LEU VAL VAL VAL THR ILE SEQRES 2 X 95 VAL CYS LEU ASP LEU GLY TYR THR ILE VAL CYS HIS THR SEQRES 3 X 95 THR ALA THR SER PRO ILE SER ALA VAL THR CYS PRO PRO SEQRES 4 X 95 GLY GLU ASN LEU CYS TYR ARG LYS MET TRP CYS ASP ALA SEQRES 5 X 95 PHE CYS SER SER ARG GLY LYS VAL VAL GLU LEU GLY CYS SEQRES 6 X 95 ALA ALA THR CYS PRO SER LYS LYS PRO TYR GLU GLU VAL SEQRES 7 X 95 THR CYS CYS SER THR ASP LYS CYS ASN PRO HIS PRO LYS SEQRES 8 X 95 GLN ARG PRO GLY SEQRES 1 Z 95 MET LYS THR LEU LEU LEU THR LEU VAL VAL VAL THR ILE SEQRES 2 Z 95 VAL CYS LEU ASP LEU GLY TYR THR ILE VAL CYS HIS THR SEQRES 3 Z 95 THR ALA THR SER PRO ILE SER ALA VAL THR CYS PRO PRO SEQRES 4 Z 95 GLY GLU ASN LEU CYS TYR ARG LYS MET TRP CYS ASP ALA SEQRES 5 Z 95 PHE CYS SER SER ARG GLY LYS VAL VAL GLU LEU GLY CYS SEQRES 6 Z 95 ALA ALA THR CYS PRO SER LYS LYS PRO TYR GLU GLU VAL SEQRES 7 Z 95 THR CYS CYS SER THR ASP LYS CYS ASN PRO HIS PRO LYS SEQRES 8 Z 95 GLN ARG PRO GLY 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 121 GLY ALA SER ASN PHE MET LEU THR GLN PRO ARG SER VAL SEQRES 2 M 121 SER GLU SER PRO GLY LYS THR VAL THR ILE SER CYS THR SEQRES 3 M 121 ARG SER SER GLY SER ILE GLY SER ASP TYR VAL HIS TRP SEQRES 4 M 121 TYR GLN GLN ARG PRO GLY SER SER PRO THR THR VAL ILE SEQRES 5 M 121 TYR GLU ASP ASN GLN ARG PRO SER GLY VAL PRO ASP ARG SEQRES 6 M 121 PHE SER GLY SER ILE ASP SER SER SER ASN SER ALA SER SEQRES 7 M 121 LEU THR ILE SER GLY LEU LYS THR GLU ASP GLU ALA ASP SEQRES 8 M 121 TYR TYR CYS GLN SER TYR ASP ARG SER ASN HIS GLU VAL SEQRES 9 M 121 VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLU ASN SEQRES 10 M 121 LEU TYR PHE GLN SEQRES 1 B 144 ALA GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS SEQRES 2 B 144 LYS PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER SEQRES 3 B 144 GLY GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG SEQRES 4 B 144 GLN ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE SEQRES 5 B 144 ILE PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE SEQRES 6 B 144 GLN GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER SEQRES 7 B 144 THR ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP SEQRES 8 B 144 THR ALA VAL TYR TYR CYS ALA ARG ASP ASN LEU GLY TYR SEQRES 9 B 144 CYS SER GLY GLY SER CYS TYR SER ASP TYR TYR TYR TYR SEQRES 10 B 144 TYR MET ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 11 B 144 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 12 B 144 GLY HET EDO C 301 10 HET EDO X 101 10 HET EDO X 102 10 HET EDO M 301 10 HET EDO M 302 10 HET EDO B 201 10 HET EDO B 202 10 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 7 EDO 7(C2 H6 O2) FORMUL 14 HOH *961(H2 O) HELIX 1 AA1 SER C 174 ASP C 178 5 5 HELIX 2 AA2 LYS C 228 GLU C 232 5 5 HELIX 3 AA3 PHE X 32 GLY X 37 1 6 HELIX 4 AA4 HIS X 68 ARG X 72 5 5 HELIX 5 AA5 PHE Z 32 GLY Z 37 1 6 HELIX 6 AA6 HIS Z 68 ARG Z 72 5 5 HELIX 7 AA7 PRO I 53 GLY I 56 5 4 HELIX 8 AA8 GLU I 74 THR I 76 5 3 HELIX 9 AA9 ARG I 87 THR I 91 5 5 HELIX 10 AB1 SER M 174 ASP M 178 5 5 HELIX 11 AB2 SER M 215 SER M 217 5 3 HELIX 12 AB3 LYS M 228 GLU M 232 5 5 HELIX 13 AB4 GLU B 74 THR B 76 5 3 HELIX 14 AB5 ARG B 87 THR B 91 5 5 SHEET 1 AA1 4 LEU C 150 THR C 151 0 SHEET 2 AA1 4 VAL C 164 ARG C 170 -1 O THR C 169 N THR C 151 SHEET 3 AA1 4 SER C 219 ILE C 224 -1 O ILE C 224 N VAL C 164 SHEET 4 AA1 4 PHE C 209 ASP C 214 -1 N ASP C 214 O SER C 219 SHEET 1 AA2 5 SER C 155 GLU C 158 0 SHEET 2 AA2 5 THR C 253 VAL C 257 1 O THR C 256 N VAL C 156 SHEET 3 AA2 5 ALA C 233 ASP C 241 -1 N ALA C 233 O LEU C 255 SHEET 4 AA2 5 HIS C 181 GLN C 185 -1 N GLN C 185 O ASP C 234 SHEET 5 AA2 5 THR C 192 ILE C 195 -1 O ILE C 195 N TRP C 182 SHEET 1 AA3 4 SER C 155 GLU C 158 0 SHEET 2 AA3 4 THR C 253 VAL C 257 1 O THR C 256 N VAL C 156 SHEET 3 AA3 4 ALA C 233 ASP C 241 -1 N ALA C 233 O LEU C 255 SHEET 4 AA3 4 GLU C 246 PHE C 249 -1 O GLU C 246 N ASP C 241 SHEET 1 AA4 2 VAL X 2 THR X 5 0 SHEET 2 AA4 2 SER X 12 THR X 15 -1 O SER X 12 N THR X 5 SHEET 1 AA5 5 GLU X 56 CYS X 60 0 SHEET 2 AA5 5 LEU X 22 TRP X 28 -1 N CYS X 23 O CYS X 60 SHEET 3 AA5 5 VAL X 39 ALA X 45 -1 O VAL X 39 N TRP X 28 SHEET 4 AA5 5 SER B 108 TYR B 110 -1 O CYS B 109 N VAL X 40 SHEET 5 AA5 5 CYS B 104 SER B 105 -1 N SER B 105 O SER B 108 SHEET 1 AA6 2 VAL Z 2 THR Z 5 0 SHEET 2 AA6 2 SER Z 12 THR Z 15 -1 O SER Z 12 N THR Z 5 SHEET 1 AA7 5 GLU Z 55 CYS Z 60 0 SHEET 2 AA7 5 LEU Z 22 TRP Z 28 -1 N CYS Z 23 O CYS Z 60 SHEET 3 AA7 5 VAL Z 39 ALA Z 45 -1 O VAL Z 39 N TRP Z 28 SHEET 4 AA7 5 SER I 108 TYR I 110 -1 O CYS I 109 N VAL Z 40 SHEET 5 AA7 5 CYS I 104 SER I 105 -1 N SER I 105 O SER I 108 SHEET 1 AA8 4 GLN I 3 GLN I 6 0 SHEET 2 AA8 4 VAL I 18 SER I 25 -1 O LYS I 23 N VAL I 5 SHEET 3 AA8 4 THR I 78 LEU I 83 -1 O ALA I 79 N CYS I 22 SHEET 4 AA8 4 VAL I 68 ASP I 73 -1 N ASP I 73 O THR I 78 SHEET 1 AA9 6 GLU I 10 LYS I 12 0 SHEET 2 AA9 6 THR I 125 VAL I 129 1 O THR I 128 N LYS I 12 SHEET 3 AA9 6 ALA I 92 ASP I 99 -1 N TYR I 94 O THR I 125 SHEET 4 AA9 6 ILE I 34 GLN I 39 -1 N VAL I 37 O TYR I 95 SHEET 5 AA9 6 LEU I 45 ILE I 52 -1 O MET I 48 N TRP I 36 SHEET 6 AA9 6 THR I 57 TYR I 60 -1 O ASN I 59 N GLY I 50 SHEET 1 AB1 4 GLU I 10 LYS I 12 0 SHEET 2 AB1 4 THR I 125 VAL I 129 1 O THR I 128 N LYS I 12 SHEET 3 AB1 4 ALA I 92 ASP I 99 -1 N TYR I 94 O THR I 125 SHEET 4 AB1 4 MET I 118 TRP I 121 -1 O VAL I 120 N ARG I 98 SHEET 1 AB2 4 LEU M 150 THR M 151 0 SHEET 2 AB2 4 VAL M 164 ARG M 170 -1 O THR M 169 N THR M 151 SHEET 3 AB2 4 SER M 219 ILE M 224 -1 O ALA M 220 N CYS M 168 SHEET 4 AB2 4 PHE M 209 ASP M 214 -1 N ASP M 214 O SER M 219 SHEET 1 AB3 5 SER M 155 GLU M 158 0 SHEET 2 AB3 5 THR M 253 VAL M 257 1 O THR M 256 N VAL M 156 SHEET 3 AB3 5 ALA M 233 ASP M 241 -1 N ALA M 233 O LEU M 255 SHEET 4 AB3 5 HIS M 181 GLN M 185 -1 N GLN M 185 O ASP M 234 SHEET 5 AB3 5 THR M 192 ILE M 195 -1 O ILE M 195 N TRP M 182 SHEET 1 AB4 4 SER M 155 GLU M 158 0 SHEET 2 AB4 4 THR M 253 VAL M 257 1 O THR M 256 N VAL M 156 SHEET 3 AB4 4 ALA M 233 ASP M 241 -1 N ALA M 233 O LEU M 255 SHEET 4 AB4 4 GLU M 246 PHE M 249 -1 O GLU M 246 N ASP M 241 SHEET 1 AB5 4 LEU B 4 GLN B 6 0 SHEET 2 AB5 4 VAL B 18 ALA B 24 -1 O LYS B 23 N VAL B 5 SHEET 3 AB5 4 THR B 78 LEU B 83 -1 O ALA B 79 N CYS B 22 SHEET 4 AB5 4 VAL B 68 ASP B 73 -1 N THR B 71 O TYR B 80 SHEET 1 AB6 6 GLU B 10 LYS B 12 0 SHEET 2 AB6 6 THR B 125 VAL B 129 1 O THR B 128 N LYS B 12 SHEET 3 AB6 6 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 125 SHEET 4 AB6 6 ILE B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AB6 6 LEU B 45 ILE B 52 -1 O GLU B 46 N ARG B 38 SHEET 6 AB6 6 THR B 57 TYR B 60 -1 O ASN B 59 N GLY B 50 SHEET 1 AB7 4 GLU B 10 LYS B 12 0 SHEET 2 AB7 4 THR B 125 VAL B 129 1 O THR B 128 N LYS B 12 SHEET 3 AB7 4 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 125 SHEET 4 AB7 4 MET B 118 TRP B 121 -1 O VAL B 120 N ARG B 98 SSBOND 1 CYS C 168 CYS C 237 1555 1555 2.12 SSBOND 2 CYS X 3 CYS X 23 1555 1555 2.02 SSBOND 3 CYS X 16 CYS X 44 1555 1555 2.04 SSBOND 4 CYS X 29 CYS X 33 1555 1555 2.08 SSBOND 5 CYS X 48 CYS X 59 1555 1555 2.08 SSBOND 6 CYS X 60 CYS X 65 1555 1555 2.05 SSBOND 7 CYS Z 3 CYS Z 23 1555 1555 2.02 SSBOND 8 CYS Z 16 CYS Z 44 1555 1555 2.06 SSBOND 9 CYS Z 29 CYS Z 33 1555 1555 2.07 SSBOND 10 CYS Z 48 CYS Z 59 1555 1555 2.10 SSBOND 11 CYS Z 60 CYS Z 65 1555 1555 2.01 SSBOND 12 CYS I 22 CYS I 96 1555 1555 2.06 SSBOND 13 CYS I 104 CYS I 109 1555 1555 2.08 SSBOND 14 CYS M 168 CYS M 237 1555 1555 2.01 SSBOND 15 CYS B 22 CYS B 96 1555 1555 2.08 SSBOND 16 CYS B 104 CYS B 109 1555 1555 2.14 CISPEP 1 SER X 9 PRO X 10 0 -6.16 CISPEP 2 SER Z 9 PRO Z 10 0 -6.77 CRYST1 79.051 84.735 102.829 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 0.012650 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011801 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009725 0.00000