HEADER IMMUNE SYSTEM 12-DEC-24 9MI6 TITLE CRYSTAL STRUCTURE OF HUMAN FCRN IN COMPLEX WITH NIPOCALIMAB FAB TITLE 2 FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG RECEPTOR FCRN LARGE SUBUNIT P51; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FCRN,IGG FC FRAGMENT RECEPTOR TRANSPORTER ALPHA CHAIN, COMPND 5 NEONATAL FC RECEPTOR; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: NIPOCALIMAB FAB HEAVY CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES; COMPND 15 OTHER_DETAILS: GENERATED BY PAPAIN DIGESTION OF NIPOCALIMAB IGG; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: NIPOCALIMAB FAB LIGHT CHAIN; COMPND 18 CHAIN: L; COMPND 19 ENGINEERED: YES; COMPND 20 OTHER_DETAILS: GENERATED BY PAPAIN DIGESTION OF NIPOCALIMAB IGG SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FCGRT, FCRN; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: B2M, CDABP0092, HDCMA22P; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NEONATAL FC RECEPTOR, FCRN, INHIBITOR, BETA 2 MICROGLOBULIN, B2M, KEYWDS 2 COMPLEX(ANTIBODY-ANTIGEN), IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.XU,J.MEADOR REVDAT 2 26-FEB-25 9MI6 1 JRNL REVDAT 1 12-FEB-25 9MI6 0 JRNL AUTH N.P.SETH,R.XU,M.DUPRIE,A.CHOUDHURY,S.SIHAPONG,S.TYLER, JRNL AUTH 2 J.MEADOR,W.AVERY,E.COCHRAN,T.DALY,J.BROWN,L.RUTITZKY, JRNL AUTH 3 L.MARKOWITZ,S.KUMAR,T.BEAVERS,S.BHATTACHARYA,H.CHEN,V.PARGE, JRNL AUTH 4 K.PRICE,Y.WANG,S.SUKUMARAN,Y.PAO,K.ABOUZAHR,F.ELWOOD, JRNL AUTH 5 J.DUFFNER,S.ROY,P.NARAYANASWAMI,J.J.HUBBARD,L.E.LING JRNL TITL NIPOCALIMAB, AN IMMUNOSELECTIVE FCRN BLOCKER THAT LOWERS IGG JRNL TITL 2 AND HAS UNIQUE MOLECULAR PROPERTIES. JRNL REF MABS V. 17 61191 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 39936406 JRNL DOI 10.1080/19420862.2025.2461191 REMARK 2 REMARK 2 RESOLUTION. 2.41 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17.1_3660 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) : 2.41 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.48 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9 REMARK 3 NUMBER OF REFLECTIONS : 46480 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 2304 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 44.4800 - 6.0700 0.97 2903 155 0.1595 0.1735 REMARK 3 2 6.0700 - 4.8200 0.96 2774 149 0.1530 0.1978 REMARK 3 3 4.8200 - 4.2100 0.99 2896 146 0.1357 0.1629 REMARK 3 4 4.2100 - 3.8200 0.93 2688 143 0.1747 0.1909 REMARK 3 5 3.8200 - 3.5500 0.98 2807 142 0.1978 0.2626 REMARK 3 6 3.5500 - 3.3400 0.98 2831 146 0.2250 0.2744 REMARK 3 7 3.3400 - 3.1700 0.98 2809 145 0.2430 0.2782 REMARK 3 8 3.1700 - 3.0400 0.90 2591 138 0.2517 0.3315 REMARK 3 9 3.0400 - 2.9200 0.96 2726 142 0.2527 0.3085 REMARK 3 10 2.9200 - 2.8200 0.97 2789 142 0.2495 0.3406 REMARK 3 11 2.8200 - 2.7300 0.97 2788 133 0.2512 0.2885 REMARK 3 12 2.7300 - 2.6500 0.97 2776 159 0.2827 0.3382 REMARK 3 13 2.6500 - 2.5800 0.98 2781 143 0.2931 0.3552 REMARK 3 14 2.5800 - 2.5200 0.91 2631 122 0.3015 0.3324 REMARK 3 15 2.5200 - 2.4600 0.95 2716 146 0.3084 0.3633 REMARK 3 16 2.4600 - 2.4100 0.95 2670 153 0.3174 0.3644 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.399 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.689 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 39.95 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.13 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 : 0.005 6230 REMARK 3 ANGLE : 0.736 8470 REMARK 3 CHIRALITY : 0.044 922 REMARK 3 PLANARITY : 0.005 1092 REMARK 3 DIHEDRAL : 19.673 2231 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 174.3031 92.3186 21.4260 REMARK 3 T TENSOR REMARK 3 T11: 0.3494 T22: 0.3525 REMARK 3 T33: 0.2814 T12: 0.0164 REMARK 3 T13: -0.0211 T23: -0.0146 REMARK 3 L TENSOR REMARK 3 L11: 0.8904 L22: 0.0224 REMARK 3 L33: 0.5450 L12: -0.0291 REMARK 3 L13: 0.5160 L23: -0.0573 REMARK 3 S TENSOR REMARK 3 S11: -0.0162 S12: -0.0001 S13: 0.0127 REMARK 3 S21: 0.0027 S22: 0.0097 S23: 0.0012 REMARK 3 S31: -0.0799 S32: -0.0007 S33: -0.0041 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 9MI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000291023. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-MAY-17 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 : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : SI(111) AND SI(220) DOUBLE REMARK 200 CRYSTAL 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 : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46599 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.410 REMARK 200 RESOLUTION RANGE LOW (A) : 44.480 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.14400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.7800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.95600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.020 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 (%): 65.43 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 1000, 10% PEG 8000, PH 7.5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K 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 91.64100 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.82200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.64100 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.82200 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L 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 HOH A 468 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 ALA A 1 REMARK 465 GLU A 2 REMARK 465 SER A 3 REMARK 465 PRO A 270 REMARK 465 ALA A 271 REMARK 465 LYS A 272 REMARK 465 SER A 273 REMARK 465 SER A 274 REMARK 465 HIS A 275 REMARK 465 HIS A 276 REMARK 465 HIS A 277 REMARK 465 HIS A 278 REMARK 465 HIS A 279 REMARK 465 HIS A 280 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 SER H 135 REMARK 465 GLY H 136 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 SER L 216 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 TRP A 59 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 59 CZ3 CH2 REMARK 470 LYS H 217 CE NZ 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 LEU A 5 47.58 -87.32 REMARK 500 ALA A 108 89.48 -155.36 REMARK 500 PHE A 117 -3.21 -141.79 REMARK 500 ARG A 169 -8.85 -146.93 REMARK 500 PRO A 191 108.70 -51.53 REMARK 500 ALA A 219 -1.55 -142.09 REMARK 500 TRP B 60 -5.40 74.91 REMARK 500 ASP H 147 68.23 65.29 REMARK 500 ASP L 53 -42.61 72.30 REMARK 500 SER L 54 18.95 -148.64 REMARK 500 ALA L 86 -176.97 -171.60 REMARK 500 ASP L 155 -99.72 54.88 REMARK 500 ASN L 174 -10.86 73.25 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MI6 A 1 274 UNP P55899 FCGRN_HUMAN 24 297 DBREF 9MI6 B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 9MI6 H 1 220 PDB 9MI6 9MI6 1 220 DBREF 9MI6 L 1 216 PDB 9MI6 9MI6 1 216 SEQADV 9MI6 HIS A 275 UNP P55899 EXPRESSION TAG SEQADV 9MI6 HIS A 276 UNP P55899 EXPRESSION TAG SEQADV 9MI6 HIS A 277 UNP P55899 EXPRESSION TAG SEQADV 9MI6 HIS A 278 UNP P55899 EXPRESSION TAG SEQADV 9MI6 HIS A 279 UNP P55899 EXPRESSION TAG SEQADV 9MI6 HIS A 280 UNP P55899 EXPRESSION TAG SEQRES 1 A 280 ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA SEQRES 2 A 280 VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL SEQRES 3 A 280 SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN SEQRES 4 A 280 SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL SEQRES 5 A 280 TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR SEQRES 6 A 280 THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA SEQRES 7 A 280 PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN SEQRES 8 A 280 GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER SEQRES 9 A 280 VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE SEQRES 10 A 280 MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP SEQRES 11 A 280 TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN SEQRES 12 A 280 GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU SEQRES 13 A 280 PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG SEQRES 14 A 280 GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET SEQRES 15 A 280 ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL SEQRES 16 A 280 LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU SEQRES 17 A 280 GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR SEQRES 18 A 280 GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE SEQRES 19 A 280 HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU SEQRES 20 A 280 HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA SEQRES 21 A 280 GLN PRO LEU ARG VAL GLU LEU GLU SER PRO ALA LYS SER SEQRES 22 A 280 SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS SEQRES 2 B 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR SEQRES 3 B 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU SEQRES 4 B 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER SEQRES 5 B 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU SEQRES 6 B 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR SEQRES 7 B 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS SEQRES 8 B 99 ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 H 220 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 220 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 220 PHE THR PHE SER THR TYR ALA MET GLY TRP VAL ARG GLN SEQRES 4 H 220 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE GLY SEQRES 5 H 220 ALA SER GLY SER GLN THR ARG TYR ALA ASP SER VAL LYS SEQRES 6 H 220 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 220 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 220 ALA VAL TYR TYR CYS ALA ARG LEU ALA ILE GLY ASP SER SEQRES 9 H 220 TYR TRP GLY GLN GLY THR MET VAL THR VAL SER SER ALA SEQRES 10 H 220 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 H 220 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 H 220 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 220 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 220 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 220 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 H 220 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 H 220 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 1 L 216 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 L 216 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR GLY SEQRES 3 L 216 SER ASP VAL GLY SER TYR ASN LEU VAL SER TRP TYR GLN SEQRES 4 L 216 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR GLY SEQRES 5 L 216 ASP SER GLU ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 L 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 L 216 SER TYR ALA GLY SER GLY ILE TYR VAL PHE GLY THR GLY SEQRES 9 L 216 THR LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO THR GLU CYS SER HET NAG A 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 5 NAG C8 H15 N O6 FORMUL 6 HOH *265(H2 O) HELIX 1 AA1 GLY A 49 GLU A 54 5 6 HELIX 2 AA2 TRP A 59 GLY A 83 1 25 HELIX 3 AA3 TRP A 131 GLN A 144 1 14 HELIX 4 AA4 LYS A 146 PHE A 157 1 12 HELIX 5 AA5 PHE A 157 GLU A 168 1 12 HELIX 6 AA6 GLY A 170 GLU A 175 1 6 HELIX 7 AA7 ASP A 246 HIS A 248 5 3 HELIX 8 AA8 THR H 28 TYR H 32 5 5 HELIX 9 AA9 ASP H 62 LYS H 65 5 4 HELIX 10 AB1 ARG H 87 THR H 91 5 5 HELIX 11 AB2 SER H 159 ALA H 161 5 3 HELIX 12 AB3 SER H 190 LEU H 192 5 3 HELIX 13 AB4 LYS H 204 ASN H 207 5 4 HELIX 14 AB5 GLN L 81 GLU L 85 5 5 HELIX 15 AB6 SER L 125 ALA L 131 1 7 HELIX 16 AB7 THR L 185 SER L 191 1 7 SHEET 1 AA1 8 GLU A 46 PRO A 47 0 SHEET 2 AA1 8 GLN A 33 ASN A 39 -1 N SER A 37 O GLU A 46 SHEET 3 AA1 8 PHE A 24 LEU A 30 -1 N VAL A 26 O TYR A 38 SHEET 4 AA1 8 SER A 6 VAL A 14 -1 N HIS A 10 O SER A 27 SHEET 5 AA1 8 THR A 89 LEU A 98 -1 O LEU A 94 N TYR A 9 SHEET 6 AA1 8 SER A 104 LEU A 112 -1 O THR A 107 N GLY A 95 SHEET 7 AA1 8 GLU A 115 ASP A 121 -1 O GLU A 115 N LEU A 112 SHEET 8 AA1 8 THR A 126 GLY A 128 -1 O THR A 126 N ASP A 121 SHEET 1 AA2 4 SER A 181 SER A 190 0 SHEET 2 AA2 4 PHE A 193 PHE A 203 -1 O THR A 197 N LYS A 185 SHEET 3 AA2 4 PHE A 234 LYS A 243 -1 O LEU A 240 N LEU A 196 SHEET 4 AA2 4 GLN A 223 PRO A 228 -1 N GLY A 227 O HIS A 235 SHEET 1 AA3 4 LEU A 217 GLY A 220 0 SHEET 2 AA3 4 LEU A 208 ARG A 214 -1 N PHE A 212 O GLY A 220 SHEET 3 AA3 4 TYR A 250 HIS A 256 -1 O CYS A 251 N LEU A 213 SHEET 4 AA3 4 LEU A 263 GLU A 266 -1 O VAL A 265 N CYS A 252 SHEET 1 AA4 4 LYS B 6 SER B 11 0 SHEET 2 AA4 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 AA4 4 PHE B 62 PHE B 70 -1 O LEU B 64 N VAL B 27 SHEET 4 AA4 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 AA5 4 LYS B 6 SER B 11 0 SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O LEU B 64 N VAL B 27 SHEET 4 AA5 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 AA6 4 GLU B 44 ARG B 45 0 SHEET 2 AA6 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 AA6 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38 SHEET 4 AA6 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82 SHEET 1 AA7 4 GLN H 3 SER H 7 0 SHEET 2 AA7 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA7 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA7 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AA8 6 LEU H 11 VAL H 12 0 SHEET 2 AA8 6 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12 SHEET 3 AA8 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 110 SHEET 4 AA8 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA8 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA8 6 THR H 58 TYR H 60 -1 O ARG H 59 N SER H 50 SHEET 1 AA9 4 LEU H 11 VAL H 12 0 SHEET 2 AA9 4 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12 SHEET 3 AA9 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 110 SHEET 4 AA9 4 TYR H 105 TRP H 106 -1 O TYR H 105 N ARG H 98 SHEET 1 AB1 4 SER H 123 LEU H 127 0 SHEET 2 AB1 4 THR H 138 TYR H 148 -1 O GLY H 142 N LEU H 127 SHEET 3 AB1 4 TYR H 179 PRO H 188 -1 O TYR H 179 N TYR H 148 SHEET 4 AB1 4 VAL H 166 THR H 168 -1 N HIS H 167 O VAL H 184 SHEET 1 AB2 4 SER H 123 LEU H 127 0 SHEET 2 AB2 4 THR H 138 TYR H 148 -1 O GLY H 142 N LEU H 127 SHEET 3 AB2 4 TYR H 179 PRO H 188 -1 O TYR H 179 N TYR H 148 SHEET 4 AB2 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180 SHEET 1 AB3 3 THR H 154 TRP H 157 0 SHEET 2 AB3 3 ILE H 198 HIS H 203 -1 O ASN H 200 N SER H 156 SHEET 3 AB3 3 THR H 208 LYS H 213 -1 O VAL H 210 N VAL H 201 SHEET 1 AB4 5 SER L 9 GLY L 12 0 SHEET 2 AB4 5 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AB4 5 ASP L 87 TYR L 93 -1 N TYR L 88 O THR L 105 SHEET 4 AB4 5 LEU L 34 GLN L 40 -1 N SER L 36 O SER L 91 SHEET 5 AB4 5 LYS L 47 ILE L 50 -1 O MET L 49 N TRP L 37 SHEET 1 AB5 4 SER L 9 GLY L 12 0 SHEET 2 AB5 4 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AB5 4 ASP L 87 TYR L 93 -1 N TYR L 88 O THR L 105 SHEET 4 AB5 4 TYR L 99 PHE L 101 -1 O VAL L 100 N SER L 92 SHEET 1 AB6 3 ILE L 18 THR L 23 0 SHEET 2 AB6 3 THR L 72 ILE L 77 -1 O LEU L 75 N ILE L 20 SHEET 3 AB6 3 PHE L 64 SER L 69 -1 N SER L 65 O THR L 76 SHEET 1 AB7 4 SER L 118 PHE L 122 0 SHEET 2 AB7 4 ALA L 134 PHE L 143 -1 O LEU L 139 N THR L 120 SHEET 3 AB7 4 TYR L 176 LEU L 184 -1 O LEU L 182 N LEU L 136 SHEET 4 AB7 4 VAL L 163 THR L 165 -1 N GLU L 164 O TYR L 181 SHEET 1 AB8 4 SER L 118 PHE L 122 0 SHEET 2 AB8 4 ALA L 134 PHE L 143 -1 O LEU L 139 N THR L 120 SHEET 3 AB8 4 TYR L 176 LEU L 184 -1 O LEU L 182 N LEU L 136 SHEET 4 AB8 4 SER L 169 LYS L 170 -1 N SER L 169 O ALA L 177 SHEET 1 AB9 4 SER L 157 VAL L 159 0 SHEET 2 AB9 4 THR L 149 ALA L 154 -1 N ALA L 154 O SER L 157 SHEET 3 AB9 4 TYR L 195 HIS L 201 -1 O GLN L 198 N ALA L 151 SHEET 4 AB9 4 SER L 204 VAL L 210 -1 O VAL L 206 N VAL L 199 SSBOND 1 CYS A 96 CYS A 159 1555 1555 2.05 SSBOND 2 CYS A 198 CYS A 252 1555 1555 2.03 SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.02 SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.05 SSBOND 5 CYS H 143 CYS H 199 1555 1555 2.03 SSBOND 6 CYS L 22 CYS L 90 1555 1555 2.05 SSBOND 7 CYS L 138 CYS L 197 1555 1555 2.04 LINK ND2 ASN A 102 C1 NAG A 301 1555 1555 1.47 CISPEP 1 GLY A 86 PRO A 87 0 -3.33 CISPEP 2 TYR A 204 PRO A 205 0 2.17 CISPEP 3 HIS B 31 PRO B 32 0 -3.78 CISPEP 4 PHE H 149 PRO H 150 0 -1.14 CISPEP 5 GLU H 151 PRO H 152 0 2.18 CISPEP 6 TYR L 144 PRO L 145 0 3.23 CRYST1 183.282 67.644 105.303 90.00 104.88 90.00 C 1 2 1 4 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 0.005456 0.000000 0.001450 0.00000 SCALE2 0.000000 0.014783 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009826 0.00000