HEADER IMMUNE SYSTEM 30-APR-25 9R2E TITLE STRUCTURE OF ARGX-121 FAB FRAGMENT IN COMPLEX WITH THE FC FRAGMENT OF TITLE 2 IGA1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARGX-121 FAB FRAGMENT HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ARGX-121 FAB FRAGMENT LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ISOFORM 1 OF IMMUNOGLOBULIN HEAVY CONSTANT ALPHA 1; COMPND 11 CHAIN: P, Q; COMPND 12 SYNONYM: IG ALPHA-1 CHAIN C REGION,IG ALPHA-1 CHAIN C REGION BUR,IG COMPND 13 ALPHA-1 CHAIN C REGION TRO; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: IGHA1; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, IMMUNE SYSTEM, IGA MEDIATED AUTOIMMUNITY, IMMUNOGLOBULIN, KEYWDS 2 PROTEROS BIOSTRUCTURES GMBH EXPDTA X-RAY DIFFRACTION AUTHOR E.PANNECOUCKE,S.VOET,L.DEWEIRDT,J.VERBEIREN,S.GABRIELS,M.PROVOST, AUTHOR 2 R.FREIER,J.KOENIG,A.LAMMENS,K.SILENCE REVDAT 1 14-MAY-25 9R2E 0 JRNL AUTH S.VOET,M.PROVOST,L.DEWEIRDT,J.VERBEIREN,S.GABRIELS, JRNL AUTH 2 K.SILENCE,E.PANNECOUCKE JRNL TITL STRUCTURE OF ARGX-121 FAB FRAGMENT IN COMPLEX WITH THE FC JRNL TITL 2 FRAGMENT OF IGA1 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 116.16 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 3 NUMBER OF REFLECTIONS : 55813 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2937 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.54 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.58 REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.26 REMARK 3 BIN R VALUE (WORKING SET) : 0.3280 REMARK 3 BIN FREE R VALUE SET COUNT : NULL REMARK 3 BIN FREE R VALUE : 0.3380 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 9611 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 54 REMARK 3 SOLVENT ATOMS : 377 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.97 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.69000 REMARK 3 B22 (A**2) : -0.90000 REMARK 3 B33 (A**2) : 1.59000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.13000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : NULL REMARK 3 ION PROBE RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9R2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-APR-25. REMARK 100 THE DEPOSITION ID IS D_1292147446. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-JAN-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL 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) : 0.885603 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X CDTE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC, XDS JUN 30, 2023 REMARK 200 DATA SCALING SOFTWARE : AUTOPROC 1.1.7, AIMLESS 0.7.13 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59436 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.539 REMARK 200 RESOLUTION RANGE LOW (A) : 116.160 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 200 DATA REDUNDANCY : 2.800 REMARK 200 R MERGE (I) : 0.12900 REMARK 200 R SYM (I) : 0.12900 REMARK 200 FOR THE DATA SET : 4.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.80 REMARK 200 R MERGE FOR SHELL (I) : 1.59200 REMARK 200 R SYM FOR SHELL (I) : 1.59200 REMARK 200 FOR SHELL : 1.300 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 (%): 61.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (W/V) PEG8000, 20% (V/V) GLYCEROL, REMARK 280 0.16 M MGACETATE, 0.08 M NA CACODYLATE PH 6.50, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.64550 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 116.15600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.64550 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 116.15600 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 APPLY THE FOLLOWING TO CHAINS: H, L, P, Q, A, 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 MG MG P 501 LIES ON A SPECIAL POSITION. REMARK 375 MG MG B 301 LIES ON A SPECIAL POSITION. 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 MET H -17 REMARK 465 GLY H -16 REMARK 465 TRP H -15 REMARK 465 SER H -14 REMARK 465 CYS H -13 REMARK 465 ILE H -12 REMARK 465 ILE H -11 REMARK 465 LEU H -10 REMARK 465 PHE H -9 REMARK 465 LEU H -8 REMARK 465 VAL H -7 REMARK 465 ALA H -6 REMARK 465 THR H -5 REMARK 465 ALA H -4 REMARK 465 THR H -3 REMARK 465 GLY H -2 REMARK 465 VAL H -1 REMARK 465 HIS H 0 REMARK 465 SER H 1 REMARK 465 HIS H 226 REMARK 465 MET L -18 REMARK 465 GLY L -17 REMARK 465 TRP L -16 REMARK 465 SER L -15 REMARK 465 CYS L -14 REMARK 465 ILE L -13 REMARK 465 ILE L -12 REMARK 465 LEU L -11 REMARK 465 PHE L -10 REMARK 465 LEU L -9 REMARK 465 VAL L -8 REMARK 465 ALA L -7 REMARK 465 THR L -6 REMARK 465 ALA L -5 REMARK 465 THR L -4 REMARK 465 GLY L -3 REMARK 465 VAL L -2 REMARK 465 HIS L -1 REMARK 465 SER L 0 REMARK 465 GLN L 1 REMARK 465 SER L 216 REMARK 465 LEU P 271 REMARK 465 ARG P 272 REMARK 465 ASP P 273 REMARK 465 ALA P 274 REMARK 465 SER P 275 REMARK 465 GLY P 276 REMARK 465 ARG P 296 REMARK 465 ASP P 297 REMARK 465 LEU P 298 REMARK 465 GLY P 453 REMARK 465 LYS P 454 REMARK 465 LEU Q 271 REMARK 465 ARG Q 272 REMARK 465 ASP Q 297 REMARK 465 LEU Q 298 REMARK 465 CYS Q 299 REMARK 465 GLY Q 453 REMARK 465 LYS Q 454 REMARK 465 MET A -17 REMARK 465 GLY A -16 REMARK 465 TRP A -15 REMARK 465 SER A -14 REMARK 465 CYS A -13 REMARK 465 ILE A -12 REMARK 465 ILE A -11 REMARK 465 LEU A -10 REMARK 465 PHE A -9 REMARK 465 LEU A -8 REMARK 465 VAL A -7 REMARK 465 ALA A -6 REMARK 465 THR A -5 REMARK 465 ALA A -4 REMARK 465 THR A -3 REMARK 465 GLY A -2 REMARK 465 VAL A -1 REMARK 465 HIS A 0 REMARK 465 SER A 1 REMARK 465 THR A 225 REMARK 465 HIS A 226 REMARK 465 MET B -18 REMARK 465 GLY B -17 REMARK 465 TRP B -16 REMARK 465 SER B -15 REMARK 465 CYS B -14 REMARK 465 ILE B -13 REMARK 465 ILE B -12 REMARK 465 LEU B -11 REMARK 465 PHE B -10 REMARK 465 LEU B -9 REMARK 465 VAL B -8 REMARK 465 ALA B -7 REMARK 465 THR B -6 REMARK 465 ALA B -5 REMARK 465 THR B -4 REMARK 465 GLY B -3 REMARK 465 VAL B -2 REMARK 465 HIS B -1 REMARK 465 SER B 0 REMARK 465 GLN B 1 REMARK 465 SER B 216 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 LYS H 44 NZ REMARK 480 SER H 50 OG REMARK 480 LYS H 66 CE NZ REMARK 480 LYS H 135 CG CD CE NZ REMARK 480 SER H 136 OG REMARK 480 SER H 138 OG REMARK 480 ILE H 201 CD1 REMARK 480 LYS H 212 NZ REMARK 480 LYS H 224 CD CE NZ REMARK 480 LYS L 47 CE NZ REMARK 480 LYS L 160 NZ REMARK 480 GLU P 261 CG CD OE1 OE2 REMARK 480 LEU P 264 CD1 CD2 REMARK 480 LEU P 268 CD1 CD2 REMARK 480 THR P 269 OG1 CG2 REMARK 480 VAL P 277 CG1 CG2 REMARK 480 SER P 285 OG REMARK 480 LYS P 287 CG CD CE NZ REMARK 480 GLU P 295 CG CD OE1 OE2 REMARK 480 TYR P 302 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 SER P 305 OG REMARK 480 LYS P 319 CE NZ REMARK 480 LYS P 331 CD CE NZ REMARK 480 ASN P 343 CG OD1 ND2 REMARK 480 ARG P 392 CD NE CZ NH1 NH2 REMARK 480 GLN P 406 CD OE1 NE2 REMARK 480 ILE P 416 CD1 REMARK 480 LYS P 425 NZ REMARK 480 ARG P 450 CZ NH1 NH2 REMARK 480 CYS Q 242 SG REMARK 480 ARG Q 245 NE CZ NH1 NH2 REMARK 480 LEU Q 248 CD1 CD2 REMARK 480 GLU Q 261 CG CD OE1 OE2 REMARK 480 THR Q 267 OG1 CG2 REMARK 480 LEU Q 268 CD1 CD2 REMARK 480 THR Q 269 OG1 CG2 REMARK 480 VAL Q 277 CG1 CG2 REMARK 480 THR Q 278 OG1 CG2 REMARK 480 SER Q 285 OG REMARK 480 LYS Q 287 CD CE NZ REMARK 480 SER Q 288 OG REMARK 480 GLN Q 291 CD OE1 NE2 REMARK 480 GLU Q 295 CG CD OE1 OE2 REMARK 480 ARG Q 296 CD NE CZ NH1 NH2 REMARK 480 TYR Q 302 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 SER Q 305 OG REMARK 480 LYS Q 319 CD CE NZ REMARK 480 LYS Q 331 CD CE NZ REMARK 480 ASN Q 343 CG OD1 ND2 REMARK 480 LYS Q 377 NZ REMARK 480 ARG Q 392 NE CZ NH1 NH2 REMARK 480 GLN Q 406 CD OE1 NE2 REMARK 480 LYS Q 425 CD CE NZ REMARK 480 ILE Q 448 CD1 REMARK 480 LEU Q 451 CD1 CD2 REMARK 480 LYS A 66 CE NZ REMARK 480 LYS A 77 NZ REMARK 480 GLN A 111 CD OE1 NE2 REMARK 480 LYS A 135 CD CE NZ REMARK 480 THR A 137 OG1 CG2 REMARK 480 LYS A 212 CE NZ REMARK 480 LYS A 224 CD CE NZ REMARK 480 ILE B 99 CD1 REMARK 480 LYS B 106 CE NZ REMARK 480 LYS B 160 NZ REMARK 480 ARG B 193 NE CZ NH1 NH2 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 L 470 O HOH L 470 2656 0.72 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 TYR H 55 -45.12 72.31 REMARK 500 ASP H 101 -130.91 -94.30 REMARK 500 ALA H 103 41.24 -141.72 REMARK 500 LYS H 135 123.27 -36.75 REMARK 500 THR H 137 74.25 31.73 REMARK 500 ASP H 150 62.96 61.84 REMARK 500 THR H 166 -41.11 -134.38 REMARK 500 ASP L 28 -89.69 -126.28 REMARK 500 TYR L 34 46.31 -98.83 REMARK 500 VAL L 53 -57.46 70.22 REMARK 500 ASP L 155 -123.49 58.26 REMARK 500 ASN L 174 -11.61 77.16 REMARK 500 SER P 285 66.71 -117.73 REMARK 500 TYR P 302 85.17 70.09 REMARK 500 GLU P 363 -129.71 -116.46 REMARK 500 SER P 405 149.15 -171.34 REMARK 500 ALA P 442 -51.70 69.30 REMARK 500 LEU P 451 40.96 -91.06 REMARK 500 THR Q 282 -72.52 -81.54 REMARK 500 SER Q 288 71.59 52.05 REMARK 500 GLU Q 363 -109.47 -106.52 REMARK 500 SER Q 405 133.70 -173.32 REMARK 500 ALA Q 442 -53.03 71.16 REMARK 500 VAL A 49 -61.02 -108.57 REMARK 500 TYR A 55 -60.03 72.60 REMARK 500 ARG A 68 -57.86 -128.66 REMARK 500 ASP A 101 -127.26 -89.51 REMARK 500 LYS A 135 99.90 -61.52 REMARK 500 ASP A 150 64.90 63.29 REMARK 500 ASP B 28 -94.56 -127.90 REMARK 500 TYR B 34 53.79 -101.58 REMARK 500 LEU B 49 -61.33 -97.42 REMARK 500 VAL B 53 -53.27 74.04 REMARK 500 ASP B 155 -120.58 58.54 REMARK 500 ASN B 174 -18.00 81.66 REMARK 500 SER B 191 35.44 -96.47 REMARK 500 THR B 213 47.47 -105.40 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 B 474 DISTANCE = 6.63 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 MG L 302 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS L 192 NE2 REMARK 620 2 HIS L 192 NE2 0.0 REMARK 620 3 HOH L 463 O 116.1 116.1 REMARK 620 4 HOH L 470 O 98.7 98.7 134.2 REMARK 620 5 HOH L 470 O 96.8 96.8 125.2 14.5 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG P 501 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU P 313 OE2 REMARK 620 2 GLU P 313 OE2 0.0 REMARK 620 3 HIS P 317 NE2 78.6 78.6 REMARK 620 4 HIS P 317 NE2 78.6 78.6 0.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B 301 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 192 NE2 REMARK 620 2 HIS B 192 NE2 0.0 REMARK 620 N 1 DBREF 9R2E H -17 226 PDB 9R2E 9R2E -17 226 DBREF 9R2E L -18 216 PDB 9R2E 9R2E -18 216 DBREF 9R2E P 242 454 UNP P01876 IGHA1_HUMAN 123 335 DBREF 9R2E Q 242 454 UNP P01876 IGHA1_HUMAN 123 335 DBREF 9R2E A -17 226 PDB 9R2E 9R2E -17 226 DBREF 9R2E B -18 216 PDB 9R2E 9R2E -18 216 SEQRES 1 H 244 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 H 244 ALA THR GLY VAL HIS SER GLU VAL GLN LEU LEU GLU SER SEQRES 3 H 244 GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SEQRES 4 H 244 SER CYS ALA ALA SER GLY PHE THR SER SER ASN TYR LEU SEQRES 5 H 244 MET SER TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU SEQRES 6 H 244 TRP VAL SER SER ILE TYR HIS TYR GLY HIS ASN ALA TYR SEQRES 7 H 244 TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 8 H 244 ASP ASN SER LYS ASN THR LEU TYR LEU GLN MET ASN SER SEQRES 9 H 244 LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS ALA LYS SEQRES 10 H 244 VAL ASP SER ALA TYR ASP PHE GLY SER TRP GLY GLN GLY SEQRES 11 H 244 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 12 H 244 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 13 H 244 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 14 H 244 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 15 H 244 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 16 H 244 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 17 H 244 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 18 H 244 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 19 H 244 VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 235 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 L 235 ALA THR GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO SEQRES 3 L 235 PRO SER VAL SER GLY ALA PRO GLY GLN ARG VAL THR ILE SEQRES 4 L 235 SER CYS ALA GLY THR SER SER ASP ILE GLY GLY ARG THR SEQRES 5 L 235 TYR VAL SER TRP TYR GLN GLN LEU PRO GLY THR ALA PRO SEQRES 6 L 235 LYS LEU LEU ILE TYR LYS VAL THR ILE ARG ALA SER GLY SEQRES 7 L 235 VAL PRO ASP ARG PHE SER GLY SER LYS SER GLY THR SER SEQRES 8 L 235 ALA SER LEU ALA ILE THR GLY LEU GLN ALA GLU ASP GLU SEQRES 9 L 235 ALA ASP TYR TYR CYS ALA SER HIS ARG SER ASN ASN ASN SEQRES 10 L 235 ILE VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLY SEQRES 11 L 235 GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SEQRES 12 L 235 SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL SEQRES 13 L 235 CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL SEQRES 14 L 235 ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL SEQRES 15 L 235 GLU THR THR THR PRO SER LYS GLN SER ASN ASN LYS TYR SEQRES 16 L 235 ALA ALA SER SER TYR LEU SER LEU THR PRO GLU GLN TRP SEQRES 17 L 235 LYS SER HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU SEQRES 18 L 235 GLY SER THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SEQRES 19 L 235 SER SEQRES 1 P 213 CYS HIS PRO ARG LEU SER LEU HIS ARG PRO ALA LEU GLU SEQRES 2 P 213 ASP LEU LEU LEU GLY SER GLU ALA ASN LEU THR CYS THR SEQRES 3 P 213 LEU THR GLY LEU ARG ASP ALA SER GLY VAL THR PHE THR SEQRES 4 P 213 TRP THR PRO SER SER GLY LYS SER ALA VAL GLN GLY PRO SEQRES 5 P 213 PRO GLU ARG ASP LEU CYS GLY CYS TYR SER VAL SER SER SEQRES 6 P 213 VAL LEU PRO GLY CYS ALA GLU PRO TRP ASN HIS GLY LYS SEQRES 7 P 213 THR PHE THR CYS THR ALA ALA TYR PRO GLU SER LYS THR SEQRES 8 P 213 PRO LEU THR ALA THR LEU SER LYS SER GLY ASN THR PHE SEQRES 9 P 213 ARG PRO GLU VAL HIS LEU LEU PRO PRO PRO SER GLU GLU SEQRES 10 P 213 LEU ALA LEU ASN GLU LEU VAL THR LEU THR CYS LEU ALA SEQRES 11 P 213 ARG GLY PHE SER PRO LYS ASP VAL LEU VAL ARG TRP LEU SEQRES 12 P 213 GLN GLY SER GLN GLU LEU PRO ARG GLU LYS TYR LEU THR SEQRES 13 P 213 TRP ALA SER ARG GLN GLU PRO SER GLN GLY THR THR THR SEQRES 14 P 213 PHE ALA VAL THR SER ILE LEU ARG VAL ALA ALA GLU ASP SEQRES 15 P 213 TRP LYS LYS GLY ASP THR PHE SER CYS MET VAL GLY HIS SEQRES 16 P 213 GLU ALA LEU PRO LEU ALA PHE THR GLN LYS THR ILE ASP SEQRES 17 P 213 ARG LEU ALA GLY LYS SEQRES 1 Q 213 CYS HIS PRO ARG LEU SER LEU HIS ARG PRO ALA LEU GLU SEQRES 2 Q 213 ASP LEU LEU LEU GLY SER GLU ALA ASN LEU THR CYS THR SEQRES 3 Q 213 LEU THR GLY LEU ARG ASP ALA SER GLY VAL THR PHE THR SEQRES 4 Q 213 TRP THR PRO SER SER GLY LYS SER ALA VAL GLN GLY PRO SEQRES 5 Q 213 PRO GLU ARG ASP LEU CYS GLY CYS TYR SER VAL SER SER SEQRES 6 Q 213 VAL LEU PRO GLY CYS ALA GLU PRO TRP ASN HIS GLY LYS SEQRES 7 Q 213 THR PHE THR CYS THR ALA ALA TYR PRO GLU SER LYS THR SEQRES 8 Q 213 PRO LEU THR ALA THR LEU SER LYS SER GLY ASN THR PHE SEQRES 9 Q 213 ARG PRO GLU VAL HIS LEU LEU PRO PRO PRO SER GLU GLU SEQRES 10 Q 213 LEU ALA LEU ASN GLU LEU VAL THR LEU THR CYS LEU ALA SEQRES 11 Q 213 ARG GLY PHE SER PRO LYS ASP VAL LEU VAL ARG TRP LEU SEQRES 12 Q 213 GLN GLY SER GLN GLU LEU PRO ARG GLU LYS TYR LEU THR SEQRES 13 Q 213 TRP ALA SER ARG GLN GLU PRO SER GLN GLY THR THR THR SEQRES 14 Q 213 PHE ALA VAL THR SER ILE LEU ARG VAL ALA ALA GLU ASP SEQRES 15 Q 213 TRP LYS LYS GLY ASP THR PHE SER CYS MET VAL GLY HIS SEQRES 16 Q 213 GLU ALA LEU PRO LEU ALA PHE THR GLN LYS THR ILE ASP SEQRES 17 Q 213 ARG LEU ALA GLY LYS SEQRES 1 A 244 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 A 244 ALA THR GLY VAL HIS SER GLU VAL GLN LEU LEU GLU SER SEQRES 3 A 244 GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SEQRES 4 A 244 SER CYS ALA ALA SER GLY PHE THR SER SER ASN TYR LEU SEQRES 5 A 244 MET SER TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU SEQRES 6 A 244 TRP VAL SER SER ILE TYR HIS TYR GLY HIS ASN ALA TYR SEQRES 7 A 244 TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 8 A 244 ASP ASN SER LYS ASN THR LEU TYR LEU GLN MET ASN SER SEQRES 9 A 244 LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS ALA LYS SEQRES 10 A 244 VAL ASP SER ALA TYR ASP PHE GLY SER TRP GLY GLN GLY SEQRES 11 A 244 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 12 A 244 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 13 A 244 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 14 A 244 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 15 A 244 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 16 A 244 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 17 A 244 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 18 A 244 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 19 A 244 VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 B 235 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 B 235 ALA THR GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO SEQRES 3 B 235 PRO SER VAL SER GLY ALA PRO GLY GLN ARG VAL THR ILE SEQRES 4 B 235 SER CYS ALA GLY THR SER SER ASP ILE GLY GLY ARG THR SEQRES 5 B 235 TYR VAL SER TRP TYR GLN GLN LEU PRO GLY THR ALA PRO SEQRES 6 B 235 LYS LEU LEU ILE TYR LYS VAL THR ILE ARG ALA SER GLY SEQRES 7 B 235 VAL PRO ASP ARG PHE SER GLY SER LYS SER GLY THR SER SEQRES 8 B 235 ALA SER LEU ALA ILE THR GLY LEU GLN ALA GLU ASP GLU SEQRES 9 B 235 ALA ASP TYR TYR CYS ALA SER HIS ARG SER ASN ASN ASN SEQRES 10 B 235 ILE VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLY SEQRES 11 B 235 GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SEQRES 12 B 235 SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL SEQRES 13 B 235 CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL SEQRES 14 B 235 ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL SEQRES 15 B 235 GLU THR THR THR PRO SER LYS GLN SER ASN ASN LYS TYR SEQRES 16 B 235 ALA ALA SER SER TYR LEU SER LEU THR PRO GLU GLN TRP SEQRES 17 B 235 LYS SER HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU SEQRES 18 B 235 GLY SER THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SEQRES 19 B 235 SER HET EDO H 301 4 HET EDO H 302 4 HET PEG H 303 7 HET PEG L 301 7 HET MG L 302 1 HET MG P 501 1 HET PEG A 301 7 HET EDO A 302 4 HET PEG A 303 7 HET PEG A 304 7 HET EDO A 305 4 HET MG B 301 1 HETNAM EDO 1,2-ETHANEDIOL HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM MG MAGNESIUM ION HETSYN EDO ETHYLENE GLYCOL FORMUL 7 EDO 4(C2 H6 O2) FORMUL 9 PEG 5(C4 H10 O3) FORMUL 11 MG 3(MG 2+) FORMUL 19 HOH *377(H2 O) HELIX 1 AA1 THR H 29 TYR H 33 5 5 HELIX 2 AA2 ARG H 88 THR H 92 5 5 HELIX 3 AA3 SER H 162 ALA H 164 5 3 HELIX 4 AA4 SER H 193 LEU H 195 5 3 HELIX 5 AA5 LYS H 207 ASN H 210 5 4 HELIX 6 AA6 GLN L 81 GLU L 85 5 5 HELIX 7 AA7 SER L 125 ALA L 131 1 7 HELIX 8 AA8 THR L 185 SER L 191 1 7 HELIX 9 AA9 ALA P 252 GLY P 259 1 8 HELIX 10 AB1 CYS P 311 GLY P 318 1 8 HELIX 11 AB2 PRO P 355 ASN P 362 1 8 HELIX 12 AB3 PRO P 391 TYR P 395 5 5 HELIX 13 AB4 ALA P 421 LYS P 426 1 6 HELIX 14 AB5 ALA Q 252 GLY Q 259 1 8 HELIX 15 AB6 CYS Q 311 GLY Q 318 1 8 HELIX 16 AB7 PRO Q 355 ASN Q 362 1 8 HELIX 17 AB8 PRO Q 391 GLU Q 393 5 3 HELIX 18 AB9 ALA Q 421 GLY Q 427 1 7 HELIX 19 AC1 THR A 29 TYR A 33 5 5 HELIX 20 AC2 ARG A 88 THR A 92 5 5 HELIX 21 AC3 SER A 162 ALA A 164 5 3 HELIX 22 AC4 LYS A 207 ASN A 210 5 4 HELIX 23 AC5 GLN B 81 GLU B 85 5 5 HELIX 24 AC6 SER B 125 ALA B 131 1 7 HELIX 25 AC7 THR B 185 SER B 191 1 7 SHEET 1 AA1 4 GLN H 4 SER H 8 0 SHEET 2 AA1 4 LEU H 19 SER H 26 -1 O SER H 22 N SER H 8 SHEET 3 AA1 4 THR H 79 MET H 84 -1 O LEU H 82 N LEU H 21 SHEET 4 AA1 4 PHE H 69 ASP H 74 -1 N THR H 70 O GLN H 83 SHEET 1 AA2 6 LEU H 12 VAL H 13 0 SHEET 2 AA2 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 13 SHEET 3 AA2 6 ALA H 93 VAL H 100 -1 N ALA H 93 O VAL H 115 SHEET 4 AA2 6 MET H 35 GLN H 40 -1 N VAL H 38 O TYR H 96 SHEET 5 AA2 6 LEU H 46 ILE H 52 -1 O GLU H 47 N ARG H 39 SHEET 6 AA2 6 ALA H 59 TYR H 61 -1 O TYR H 60 N SER H 51 SHEET 1 AA3 4 LEU H 12 VAL H 13 0 SHEET 2 AA3 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 13 SHEET 3 AA3 4 ALA H 93 VAL H 100 -1 N ALA H 93 O VAL H 115 SHEET 4 AA3 4 PHE H 106 TRP H 109 -1 O SER H 108 N LYS H 99 SHEET 1 AA4 4 SER H 126 LEU H 130 0 SHEET 2 AA4 4 THR H 141 TYR H 151 -1 O LYS H 149 N SER H 126 SHEET 3 AA4 4 TYR H 182 PRO H 191 -1 O TYR H 182 N TYR H 151 SHEET 4 AA4 4 VAL H 169 THR H 171 -1 N HIS H 170 O VAL H 187 SHEET 1 AA5 4 SER H 126 LEU H 130 0 SHEET 2 AA5 4 THR H 141 TYR H 151 -1 O LYS H 149 N SER H 126 SHEET 3 AA5 4 TYR H 182 PRO H 191 -1 O TYR H 182 N TYR H 151 SHEET 4 AA5 4 VAL H 175 LEU H 176 -1 N VAL H 175 O SER H 183 SHEET 1 AA6 3 THR H 157 TRP H 160 0 SHEET 2 AA6 3 ILE H 201 HIS H 206 -1 O ASN H 203 N SER H 159 SHEET 3 AA6 3 THR H 211 LYS H 216 -1 O VAL H 213 N VAL H 204 SHEET 1 AA7 6 SER L 9 GLY L 12 0 SHEET 2 AA7 6 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AA7 6 ALA L 86 HIS L 93 -1 N TYR L 88 O THR L 105 SHEET 4 AA7 6 VAL L 35 GLN L 40 -1 N TYR L 38 O TYR L 89 SHEET 5 AA7 6 LYS L 47 TYR L 51 -1 O LEU L 49 N TRP L 37 SHEET 6 AA7 6 ILE L 55 ARG L 56 -1 O ILE L 55 N TYR L 51 SHEET 1 AA8 4 SER L 9 GLY L 12 0 SHEET 2 AA8 4 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AA8 4 ALA L 86 HIS L 93 -1 N TYR L 88 O THR L 105 SHEET 4 AA8 4 ILE L 99 PHE L 101 -1 O VAL L 100 N SER L 92 SHEET 1 AA9 3 VAL L 18 ALA L 23 0 SHEET 2 AA9 3 SER L 72 ILE L 77 -1 O ILE L 77 N VAL L 18 SHEET 3 AA9 3 PHE L 64 SER L 69 -1 N SER L 65 O ALA L 76 SHEET 1 AB1 4 SER L 118 PHE L 122 0 SHEET 2 AB1 4 ALA L 134 PHE L 143 -1 O SER L 141 N SER L 118 SHEET 3 AB1 4 TYR L 176 LEU L 184 -1 O SER L 180 N CYS L 138 SHEET 4 AB1 4 VAL L 163 THR L 165 -1 N GLU L 164 O TYR L 181 SHEET 1 AB2 4 SER L 118 PHE L 122 0 SHEET 2 AB2 4 ALA L 134 PHE L 143 -1 O SER L 141 N SER L 118 SHEET 3 AB2 4 TYR L 176 LEU L 184 -1 O SER L 180 N CYS L 138 SHEET 4 AB2 4 SER L 169 LYS L 170 -1 N SER L 169 O ALA L 177 SHEET 1 AB3 4 SER L 157 VAL L 159 0 SHEET 2 AB3 4 THR L 149 ALA L 154 -1 N ALA L 154 O SER L 157 SHEET 3 AB3 4 TYR L 195 HIS L 201 -1 O GLN L 198 N ALA L 151 SHEET 4 AB3 4 SER L 204 VAL L 210 -1 O VAL L 210 N TYR L 195 SHEET 1 AB4 4 LEU P 246 HIS P 249 0 SHEET 2 AB4 4 LEU P 264 LEU P 268 -1 O THR P 265 N HIS P 249 SHEET 3 AB4 4 VAL P 304 LEU P 308 -1 O VAL P 304 N LEU P 268 SHEET 4 AB4 4 VAL P 290 GLN P 291 -1 N VAL P 290 O VAL P 307 SHEET 1 AB5 3 THR P 278 TRP P 281 0 SHEET 2 AB5 3 PHE P 321 ALA P 326 -1 O THR P 324 N THR P 280 SHEET 3 AB5 3 THR P 337 LEU P 338 -1 O LEU P 338 N PHE P 321 SHEET 1 AB6 4 GLU P 348 LEU P 352 0 SHEET 2 AB6 4 LEU P 364 PHE P 374 -1 O ARG P 372 N GLU P 348 SHEET 3 AB6 4 PHE P 411 ALA P 420 -1 O SER P 415 N CYS P 369 SHEET 4 AB6 4 LEU P 396 THR P 397 -1 N LEU P 396 O ILE P 416 SHEET 1 AB7 4 GLU P 348 LEU P 352 0 SHEET 2 AB7 4 LEU P 364 PHE P 374 -1 O ARG P 372 N GLU P 348 SHEET 3 AB7 4 PHE P 411 ALA P 420 -1 O SER P 415 N CYS P 369 SHEET 4 AB7 4 ARG P 401 GLN P 402 -1 N ARG P 401 O ALA P 412 SHEET 1 AB8 4 GLN P 388 GLU P 389 0 SHEET 2 AB8 4 LEU P 380 GLN P 385 -1 N GLN P 385 O GLN P 388 SHEET 3 AB8 4 PHE P 430 GLY P 435 -1 O MET P 433 N ARG P 382 SHEET 4 AB8 4 PHE P 443 ILE P 448 -1 O ILE P 448 N PHE P 430 SHEET 1 AB9 4 ARG Q 245 HIS Q 249 0 SHEET 2 AB9 4 LEU Q 264 THR Q 269 -1 O THR Q 265 N HIS Q 249 SHEET 3 AB9 4 SER Q 303 LEU Q 308 -1 O SER Q 306 N CYS Q 266 SHEET 4 AB9 4 VAL Q 290 GLU Q 295 -1 N VAL Q 290 O VAL Q 307 SHEET 1 AC1 3 THR Q 278 TRP Q 281 0 SHEET 2 AC1 3 PHE Q 321 ALA Q 326 -1 O ALA Q 326 N THR Q 278 SHEET 3 AC1 3 THR Q 337 LEU Q 338 -1 O LEU Q 338 N PHE Q 321 SHEET 1 AC2 4 GLU Q 348 LEU Q 352 0 SHEET 2 AC2 4 LEU Q 364 PHE Q 374 -1 O ARG Q 372 N GLU Q 348 SHEET 3 AC2 4 PHE Q 411 ALA Q 420 -1 O SER Q 415 N CYS Q 369 SHEET 4 AC2 4 TYR Q 395 THR Q 397 -1 N LEU Q 396 O ILE Q 416 SHEET 1 AC3 4 GLU Q 348 LEU Q 352 0 SHEET 2 AC3 4 LEU Q 364 PHE Q 374 -1 O ARG Q 372 N GLU Q 348 SHEET 3 AC3 4 PHE Q 411 ALA Q 420 -1 O SER Q 415 N CYS Q 369 SHEET 4 AC3 4 ARG Q 401 GLN Q 402 -1 N ARG Q 401 O ALA Q 412 SHEET 1 AC4 4 GLN Q 388 GLU Q 389 0 SHEET 2 AC4 4 LEU Q 380 GLN Q 385 -1 N GLN Q 385 O GLN Q 388 SHEET 3 AC4 4 PHE Q 430 GLY Q 435 -1 O MET Q 433 N ARG Q 382 SHEET 4 AC4 4 PHE Q 443 ILE Q 448 -1 O THR Q 444 N VAL Q 434 SHEET 1 AC5 4 GLN A 4 SER A 8 0 SHEET 2 AC5 4 LEU A 19 SER A 26 -1 O SER A 22 N SER A 8 SHEET 3 AC5 4 THR A 79 MET A 84 -1 O MET A 84 N LEU A 19 SHEET 4 AC5 4 THR A 70 ASP A 74 -1 N THR A 70 O GLN A 83 SHEET 1 AC6 6 LEU A 12 VAL A 13 0 SHEET 2 AC6 6 THR A 113 VAL A 117 1 O THR A 116 N VAL A 13 SHEET 3 AC6 6 ALA A 93 VAL A 100 -1 N TYR A 95 O THR A 113 SHEET 4 AC6 6 MET A 35 GLN A 40 -1 N VAL A 38 O TYR A 96 SHEET 5 AC6 6 LEU A 46 ILE A 52 -1 O GLU A 47 N ARG A 39 SHEET 6 AC6 6 ALA A 59 TYR A 61 -1 O TYR A 60 N SER A 51 SHEET 1 AC7 4 LEU A 12 VAL A 13 0 SHEET 2 AC7 4 THR A 113 VAL A 117 1 O THR A 116 N VAL A 13 SHEET 3 AC7 4 ALA A 93 VAL A 100 -1 N TYR A 95 O THR A 113 SHEET 4 AC7 4 PHE A 106 TRP A 109 -1 O SER A 108 N LYS A 99 SHEET 1 AC8 4 SER A 126 LEU A 130 0 SHEET 2 AC8 4 THR A 141 TYR A 151 -1 O LYS A 149 N SER A 126 SHEET 3 AC8 4 TYR A 182 PRO A 191 -1 O VAL A 188 N LEU A 144 SHEET 4 AC8 4 VAL A 169 THR A 171 -1 N HIS A 170 O VAL A 187 SHEET 1 AC9 4 SER A 126 LEU A 130 0 SHEET 2 AC9 4 THR A 141 TYR A 151 -1 O LYS A 149 N SER A 126 SHEET 3 AC9 4 TYR A 182 PRO A 191 -1 O VAL A 188 N LEU A 144 SHEET 4 AC9 4 VAL A 175 LEU A 176 -1 N VAL A 175 O SER A 183 SHEET 1 AD1 3 THR A 157 TRP A 160 0 SHEET 2 AD1 3 ILE A 201 HIS A 206 -1 O ASN A 203 N SER A 159 SHEET 3 AD1 3 THR A 211 LYS A 216 -1 O VAL A 213 N VAL A 204 SHEET 1 AD2 6 SER B 9 GLY B 12 0 SHEET 2 AD2 6 THR B 105 VAL B 109 1 O THR B 108 N VAL B 10 SHEET 3 AD2 6 ASP B 87 HIS B 93 -1 N TYR B 88 O THR B 105 SHEET 4 AD2 6 VAL B 35 GLN B 40 -1 N TYR B 38 O TYR B 89 SHEET 5 AD2 6 LYS B 47 TYR B 51 -1 O LEU B 49 N TRP B 37 SHEET 6 AD2 6 ILE B 55 ARG B 56 -1 O ILE B 55 N TYR B 51 SHEET 1 AD3 4 SER B 9 GLY B 12 0 SHEET 2 AD3 4 THR B 105 VAL B 109 1 O THR B 108 N VAL B 10 SHEET 3 AD3 4 ASP B 87 HIS B 93 -1 N TYR B 88 O THR B 105 SHEET 4 AD3 4 ILE B 99 PHE B 101 -1 O VAL B 100 N SER B 92 SHEET 1 AD4 3 VAL B 18 ALA B 23 0 SHEET 2 AD4 3 SER B 72 ILE B 77 -1 O ILE B 77 N VAL B 18 SHEET 3 AD4 3 PHE B 64 SER B 69 -1 N SER B 65 O ALA B 76 SHEET 1 AD5 4 SER B 118 PHE B 122 0 SHEET 2 AD5 4 ALA B 134 PHE B 143 -1 O VAL B 137 N PHE B 122 SHEET 3 AD5 4 TYR B 176 LEU B 184 -1 O TYR B 176 N PHE B 143 SHEET 4 AD5 4 VAL B 163 THR B 165 -1 N GLU B 164 O TYR B 181 SHEET 1 AD6 4 SER B 118 PHE B 122 0 SHEET 2 AD6 4 ALA B 134 PHE B 143 -1 O VAL B 137 N PHE B 122 SHEET 3 AD6 4 TYR B 176 LEU B 184 -1 O TYR B 176 N PHE B 143 SHEET 4 AD6 4 SER B 169 LYS B 170 -1 N SER B 169 O ALA B 177 SHEET 1 AD7 4 SER B 157 VAL B 159 0 SHEET 2 AD7 4 THR B 149 ALA B 154 -1 N ALA B 154 O SER B 157 SHEET 3 AD7 4 TYR B 195 HIS B 201 -1 O GLN B 198 N ALA B 151 SHEET 4 AD7 4 SER B 204 VAL B 210 -1 O VAL B 206 N VAL B 199 SSBOND 1 CYS H 23 CYS H 97 1555 1555 2.04 SSBOND 2 CYS H 146 CYS H 202 1555 1555 2.04 SSBOND 3 CYS H 222 CYS L 215 1555 1555 2.05 SSBOND 4 CYS L 22 CYS L 90 1555 1555 2.06 SSBOND 5 CYS L 138 CYS L 197 1555 1555 2.05 SSBOND 6 CYS P 266 CYS P 323 1555 1555 2.03 SSBOND 7 CYS P 299 CYS P 301 1555 1555 2.04 SSBOND 8 CYS P 369 CYS P 432 1555 1555 2.05 SSBOND 9 CYS Q 369 CYS Q 432 1555 1555 2.04 SSBOND 10 CYS A 23 CYS A 97 1555 1555 2.03 SSBOND 11 CYS A 146 CYS A 202 1555 1555 2.04 SSBOND 12 CYS A 222 CYS B 215 1555 1555 2.04 SSBOND 13 CYS B 22 CYS B 90 1555 1555 2.05 SSBOND 14 CYS B 138 CYS B 197 1555 1555 2.04 LINK NE2 HIS L 192 MG MG L 302 1555 1555 2.22 LINK NE2 HIS L 192 MG MG L 302 1555 2656 2.38 LINK MG MG L 302 O HOH L 463 1555 2656 2.38 LINK MG MG L 302 O HOH L 470 1555 1555 2.80 LINK MG MG L 302 O HOH L 470 1555 2656 2.56 LINK OE2 GLU P 313 MG MG P 501 1555 1555 2.03 LINK OE2 GLU P 313 MG MG P 501 1555 2556 2.03 LINK NE2 HIS P 317 MG MG P 501 1555 1555 2.47 LINK NE2 HIS P 317 MG MG P 501 1555 2556 2.47 LINK NE2 HIS B 192 MG MG B 301 1555 1555 2.18 LINK NE2 HIS B 192 MG MG B 301 1555 2655 2.18 CISPEP 1 PHE H 152 PRO H 153 0 -5.00 CISPEP 2 GLU H 154 PRO H 155 0 -3.99 CISPEP 3 TYR L 144 PRO L 145 0 -8.20 CISPEP 4 PHE A 152 PRO A 153 0 -7.02 CISPEP 5 GLU A 154 PRO A 155 0 -5.26 CISPEP 6 TYR B 144 PRO B 145 0 -6.56 CRYST1 77.291 232.312 105.519 90.00 90.35 90.00 C 1 2 1 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 0.012938 0.000000 0.000079 0.00000 SCALE2 0.000000 0.004305 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009477 0.00000