HEADER PROTEIN BINDING 22-AUG-24 9GJV TITLE FAB FRAGMENT OF AN ANTIBODY THAT RECOGNISES ALPHA-1 ANTITRYPSIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 9C5 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: FAB 9C5 LIGHT CHAIN; COMPND 6 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_TAXID: 10090 KEYWDS FAB FRAGMENT, ANTITRYPSIN, SERPIN, ANTIBODY, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR I.ALDOBIYAN,D.A.LOMAS,J.A.IRVING REVDAT 1 03-SEP-25 9GJV 0 JRNL AUTH I.ALDOBIYAN,J.A.IRVING,D.A.LOMAS JRNL TITL THE STRUCTURE OF PATHOGENIC ALPHA-1 ANTITRYPSIN AGGREGATES JRNL TITL 2 IN HUMAN LIVER JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.20 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 20032 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.245 REMARK 3 R VALUE (WORKING SET) : 0.244 REMARK 3 FREE R VALUE : 0.262 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1003 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 54.9900 - 4.2100 0.95 2805 149 0.1898 0.1895 REMARK 3 2 4.2100 - 3.3400 0.97 2748 143 0.2248 0.2527 REMARK 3 3 3.3400 - 2.9200 0.97 2690 138 0.2739 0.3017 REMARK 3 4 2.9200 - 2.6500 0.98 2684 155 0.3084 0.3261 REMARK 3 5 2.6500 - 2.4600 0.98 2696 145 0.3675 0.4121 REMARK 3 6 2.4600 - 2.3200 0.99 2714 129 0.3602 0.3895 REMARK 3 7 2.3200 - 2.2000 0.99 2692 144 0.3605 0.4390 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) : 0.420 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.450 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.002 3347 REMARK 3 ANGLE : 0.505 4613 REMARK 3 CHIRALITY : 0.042 540 REMARK 3 PLANARITY : 0.004 603 REMARK 3 DIHEDRAL : 12.314 1157 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.9808 -2.5946 -28.0505 REMARK 3 T TENSOR REMARK 3 T11: 0.4286 T22: 0.8396 REMARK 3 T33: 0.7697 T12: -0.0160 REMARK 3 T13: -0.0138 T23: -0.0667 REMARK 3 L TENSOR REMARK 3 L11: 1.0319 L22: 4.9756 REMARK 3 L33: 4.4702 L12: 1.2371 REMARK 3 L13: 0.3671 L23: -1.9499 REMARK 3 S TENSOR REMARK 3 S11: 0.0146 S12: 0.7545 S13: 0.2184 REMARK 3 S21: 0.5220 S22: -0.3290 S23: -1.0782 REMARK 3 S31: -0.5104 S32: 1.7956 S33: 0.3177 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 33 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.4348 -12.2091 -24.9364 REMARK 3 T TENSOR REMARK 3 T11: 0.7731 T22: 0.7383 REMARK 3 T33: 0.7722 T12: 0.2170 REMARK 3 T13: -0.1659 T23: -0.2299 REMARK 3 L TENSOR REMARK 3 L11: 1.1097 L22: 7.6631 REMARK 3 L33: 8.2892 L12: 0.2394 REMARK 3 L13: 1.0489 L23: -2.2124 REMARK 3 S TENSOR REMARK 3 S11: 0.0811 S12: 0.5711 S13: -0.5441 REMARK 3 S21: -0.1508 S22: 0.1903 S23: -1.2814 REMARK 3 S31: 1.0371 S32: 0.9362 S33: -0.2956 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 76 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.9666 -3.6490 -27.9924 REMARK 3 T TENSOR REMARK 3 T11: 0.3796 T22: 0.5666 REMARK 3 T33: 0.5098 T12: 0.0868 REMARK 3 T13: -0.0377 T23: -0.1315 REMARK 3 L TENSOR REMARK 3 L11: 2.6741 L22: 5.3335 REMARK 3 L33: 3.5413 L12: -1.5665 REMARK 3 L13: 0.6175 L23: -0.4487 REMARK 3 S TENSOR REMARK 3 S11: -0.0256 S12: -0.2381 S13: 0.1814 REMARK 3 S21: 0.3206 S22: 0.2725 S23: -0.8908 REMARK 3 S31: 0.3427 S32: 0.6020 S33: -0.1455 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 119 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.8750 28.6082 -22.7433 REMARK 3 T TENSOR REMARK 3 T11: 0.4946 T22: 0.4358 REMARK 3 T33: 0.4481 T12: 0.1068 REMARK 3 T13: -0.0402 T23: 0.0522 REMARK 3 L TENSOR REMARK 3 L11: 5.0223 L22: 4.8066 REMARK 3 L33: 1.7596 L12: 0.0213 REMARK 3 L13: 2.1399 L23: -1.9528 REMARK 3 S TENSOR REMARK 3 S11: 0.0346 S12: -0.0090 S13: 0.3618 REMARK 3 S21: 0.0110 S22: -0.9257 S23: -0.0897 REMARK 3 S31: -1.2843 S32: -0.9134 S33: 0.8583 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 134 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.2856 20.8316 -25.2523 REMARK 3 T TENSOR REMARK 3 T11: 0.2545 T22: 0.3348 REMARK 3 T33: 0.4448 T12: -0.0293 REMARK 3 T13: 0.0647 T23: -0.0430 REMARK 3 L TENSOR REMARK 3 L11: 3.5251 L22: 5.4547 REMARK 3 L33: 6.8020 L12: -2.4433 REMARK 3 L13: -2.4077 L23: 1.4530 REMARK 3 S TENSOR REMARK 3 S11: 0.3382 S12: -0.2577 S13: 0.5822 REMARK 3 S21: -0.1021 S22: -0.0164 S23: -0.1515 REMARK 3 S31: -0.6125 S32: 0.1178 S33: -0.2443 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.4431 -7.9519 -5.0646 REMARK 3 T TENSOR REMARK 3 T11: 1.2267 T22: 0.5624 REMARK 3 T33: 0.5748 T12: 0.2203 REMARK 3 T13: -0.2396 T23: -0.1018 REMARK 3 L TENSOR REMARK 3 L11: 4.3391 L22: 2.9345 REMARK 3 L33: 5.9310 L12: 0.5502 REMARK 3 L13: 1.5455 L23: -0.9973 REMARK 3 S TENSOR REMARK 3 S11: -0.1079 S12: -0.5538 S13: -0.0775 REMARK 3 S21: 1.8110 S22: 0.4475 S23: -0.5499 REMARK 3 S31: 0.6510 S32: 0.2398 S33: -0.3518 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 103 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.8254 17.5495 -18.9952 REMARK 3 T TENSOR REMARK 3 T11: 0.2895 T22: 0.5309 REMARK 3 T33: 0.4971 T12: -0.0053 REMARK 3 T13: 0.0566 T23: -0.1685 REMARK 3 L TENSOR REMARK 3 L11: 5.8211 L22: 6.7506 REMARK 3 L33: 6.9018 L12: -3.9611 REMARK 3 L13: 1.4070 L23: -1.0690 REMARK 3 S TENSOR REMARK 3 S11: 0.0029 S12: 0.1857 S13: -0.0512 REMARK 3 S21: 0.0164 S22: -0.3666 S23: 0.5744 REMARK 3 S31: 0.2942 S32: -0.6554 S33: 0.2457 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 9GJV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1292141178. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-MAY-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) : 0.8856 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : TOROIDAL MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.13 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20062 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 58.620 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 200 DATA REDUNDANCY : 8.200 REMARK 200 R MERGE (I) : 0.11200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 8.40 REMARK 200 R MERGE FOR SHELL (I) : 1.80200 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 2.82 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 40.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES FREE ACID, PH 7.5, 200 MM REMARK 280 MAGNESIUM CHLORIDE, 25 (%W/V) PEG 3350 CRYOPROTECTANT: 10% REMARK 280 ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP, 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 20.88300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.41950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.30900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.41950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.88300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.30900 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3480 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLN H 3 CG CD OE1 NE2 REMARK 470 LEU H 4 CG CD1 CD2 REMARK 470 GLN H 5 CD OE1 NE2 REMARK 470 LYS H 13 CD CE NZ REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 PHE H 27 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS H 30 CG CD CE NZ REMARK 470 THR H 32 OG1 CG2 REMARK 470 GLU H 42 CG CD OE1 OE2 REMARK 470 ARG H 50 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 64 CG CD OE1 NE2 REMARK 470 ARG H 94 CG CD NE CZ NH1 NH2 REMARK 470 ARG H 96 CG CD NE CZ NH1 NH2 REMARK 470 TYR H 97 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 MET H 99 CG SD CE REMARK 470 TYR H 102 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS H 115 CG CD CE NZ REMARK 470 GLN H 131 CG CD OE1 NE2 REMARK 470 GLN H 171 CG CD OE1 NE2 REMARK 470 GLU H 191 CG CD OE1 OE2 REMARK 470 LYS H 205 CG CD CE NZ REMARK 470 LYS H 208 CE NZ REMARK 470 LEU L 12 CG CD1 CD2 REMARK 470 LYS L 24 CD CE NZ REMARK 470 GLN L 27 CD OE1 NE2 REMARK 470 LYS L 39 CG CD CE NZ REMARK 470 LYS L 45 CG CD CE NZ REMARK 470 LYS L 55 CE NZ REMARK 470 GLU L 81 CG CD OE1 OE2 REMARK 470 GLU L 105 CG CD OE1 OE2 REMARK 470 LYS L 107 CG CD CE NZ REMARK 470 LYS L 147 CE NZ REMARK 470 LEU L 160 CG CD1 CD2 REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 LYS L 183 CE NZ REMARK 470 LYS L 199 CG CD 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 SER L 30 -117.24 60.15 REMARK 500 ALA L 51 -8.77 71.65 REMARK 500 LYS L 55 -72.80 -64.65 REMARK 500 PRO L 95 75.12 -66.54 REMARK 500 ASN L 212 47.53 -83.30 REMARK 500 REMARK 500 REMARK: NULL DBREF 9GJV H 1 215 PDB 9GJV 9GJV 1 215 DBREF 9GJV L 1 214 PDB 9GJV 9GJV 1 214 SEQRES 1 H 218 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 H 218 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA THR GLY SEQRES 3 H 218 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN SEQRES 4 H 218 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 H 218 PRO ALA ASN GLY ASN THR LYS TYR ASP PRO LYS PHE GLN SEQRES 6 H 218 GLY LYS ALA THR LEU THR ALA ASP THR SER SER ASN THR SEQRES 7 H 218 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 H 218 ALA VAL TYR TYR CYS ALA ARG LYS ARG TYR SER MET ASP SEQRES 9 H 218 TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA SEQRES 10 H 218 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SEQRES 11 H 218 SER GLY ALA GLN THR ASN SER MET VAL THR LEU GLY CYS SEQRES 12 H 218 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR SEQRES 13 H 218 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 H 218 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 H 218 SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR SEQRES 16 H 218 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 H 218 VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 L 214 SER ILE VAL MET THR GLN THR PRO LYS PHE LEU LEU VAL SEQRES 2 L 214 SER ALA GLY GLU ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 L 214 GLN SER VAL SER ASN ASP VAL GLY TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ASN ALA SER SEQRES 5 L 214 ASN ARG LYS ASN GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 214 GLY TYR GLY THR ASP PHE THR PHE THR ILE SER THR VAL SEQRES 7 L 214 GLN ALA GLU ASP LEU ALA VAL TYR PHE CYS GLN GLN ASP SEQRES 8 L 214 HIS SER PHE PRO LEU LYS PHE GLY ALA GLY THR LYS LEU SEQRES 9 L 214 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS FORMUL 3 HOH *68(H2 O) HELIX 1 AA1 ASN H 28 THR H 32 5 5 HELIX 2 AA2 PRO H 61 GLN H 64 5 4 HELIX 3 AA3 THR H 83 THR H 87 5 5 HELIX 4 AA4 SER H 156 SER H 158 5 3 HELIX 5 AA5 SER H 186 TRP H 188 5 3 HELIX 6 AA6 PRO H 200 SER H 203 5 4 HELIX 7 AA7 GLN L 79 LEU L 83 5 5 HELIX 8 AA8 SER L 121 GLY L 128 1 8 HELIX 9 AA9 LYS L 183 HIS L 189 1 7 HELIX 10 AB1 ASN L 212 CYS L 214 5 3 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 THR H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O LEU H 82 N VAL H 18 SHEET 4 AA1 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 TYR H 33 GLN H 39 -1 N HIS H 35 O ALA H 93 SHEET 5 AA2 6 LEU H 45 ASP H 52 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 ASN H 56 TYR H 59 -1 O ASN H 56 N ASP H 52 SHEET 1 AA3 4 GLU H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 ASP H 101 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 MET H 135 TYR H 145 -1 O LEU H 141 N TYR H 122 SHEET 3 AA4 4 LEU H 174 PRO H 184 -1 O VAL H 183 N VAL H 136 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 MET H 135 TYR H 145 -1 O LEU H 141 N TYR H 122 SHEET 3 AA5 4 LEU H 174 PRO H 184 -1 O VAL H 183 N VAL H 136 SHEET 4 AA5 4 VAL H 169 GLN H 171 -1 N GLN H 171 O LEU H 174 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 AA6 3 THR H 204 LYS H 209 -1 O LYS H 208 N CYS H 195 SHEET 1 AA7 4 MET L 4 THR L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 TYR L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA8 5 PHE L 10 SER L 14 0 SHEET 2 AA8 5 THR L 102 LYS L 107 1 O GLU L 105 N VAL L 13 SHEET 3 AA8 5 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 5 VAL L 33 GLN L 38 -1 N TYR L 36 O PHE L 87 SHEET 5 AA8 5 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 1 AA9 4 PHE L 10 SER L 14 0 SHEET 2 AA9 4 THR L 102 LYS L 107 1 O GLU L 105 N VAL L 13 SHEET 3 AA9 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 4 LYS L 97 PHE L 98 -1 O LYS L 97 N GLN L 90 SHEET 1 AB1 4 THR L 114 PHE L 118 0 SHEET 2 AB1 4 GLY L 129 PHE L 139 -1 O PHE L 135 N SER L 116 SHEET 3 AB1 4 TYR L 173 THR L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB1 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 AB2 4 SER L 153 ARG L 155 0 SHEET 2 AB2 4 ASN L 145 ILE L 150 -1 N TRP L 148 O ARG L 155 SHEET 3 AB2 4 SER L 191 HIS L 198 -1 O THR L 193 N LYS L 149 SHEET 4 AB2 4 SER L 201 ASN L 210 -1 O ILE L 205 N ALA L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS H 140 CYS H 195 1555 1555 2.03 SSBOND 3 CYS H 215 CYS L 214 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 5 CYS L 134 CYS L 194 1555 1555 2.03 CISPEP 1 PHE H 146 PRO H 147 0 -2.43 CISPEP 2 GLU H 148 PRO H 149 0 1.61 CISPEP 3 TRP H 188 PRO H 189 0 5.40 CISPEP 4 THR L 7 PRO L 8 0 -3.51 CISPEP 5 TYR L 140 PRO L 141 0 4.41 CRYST1 41.766 58.618 158.839 90.00 90.00 90.00 P 21 21 21 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 0.023943 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017060 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006296 0.00000