HEADER PROTEIN BINDING 13-AUG-24 9GGP TITLE ALPHA-1-ANTITRYPSIN IN COMPLEX WITH THE FAB FRAGMENT OF AN ANTI- TITLE 2 POLYMER ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-1-ANTITRYPSIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: ALPHA-1 PROTEASE INHIBITOR,ALPHA-1-ANTIPROTEINASE,SERPIN A1; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: REACTIVE CENTRE LOOP CLEAVED; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB FRAGMENT HEAVY CHAIN OF 2C1 MONOCLONAL ANTIBODY; COMPND 9 CHAIN: H; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FAB FRAGMENT LIGHT CHAIN OF 2C1 MONOCLONAL ANTIBODY; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SERPINA1, AAT, PI, PRO0684, PRO2209; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 ORGAN: SPLEEN; SOURCE 14 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 19 ORGANISM_TAXID: 10090; SOURCE 20 ORGAN: SPLEEN; SOURCE 21 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA KEYWDS SERPIN, FAB FRAGMENT, MONOCLONAL ANTIBODY, SELECTIVE BINDING, KEYWDS 2 EPITOPE, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR S.M.LOWEN,M.LAFFRANCHI,D.A.LOMAS,J.A.IRVING REVDAT 1 14-MAY-25 9GGP 0 JRNL AUTH S.M.LOWEN,C.A.WAUDBY,A.M.JAGGER,I.ALDOBIYAN,M.LAFFRANCHI, JRNL AUTH 2 A.FRA,J.CHRISTODOULOU,J.A.IRVING,D.A.LOMAS JRNL TITL HIGH-RESOLUTION CHARACTERIZATION OF EX VIVO AAT POLYMERS BY JRNL TITL 2 SOLUTION-STATE NMR SPECTROSCOPY. JRNL REF SCI ADV V. 11 U7064 2025 JRNL REFN ESSN 2375-2548 JRNL PMID 40333971 JRNL DOI 10.1126/SCIADV.ADU7064 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.R.EVANS,G.N.MURSHUDOV REMARK 1 TITL HOW GOOD ARE MY DATA AND WHAT IS THE RESOLUTION? REMARK 1 REF ACTA CRYSTALLOGR D BIOL V. 69 1204 2013 REMARK 1 REF 2 CRYSTALLOGR REMARK 1 REFN ESSN 1399-0047 REMARK 1 PMID 23793146 REMARK 1 DOI 10.1107/S0907444913000061 REMARK 1 REFERENCE 2 REMARK 1 AUTH W.KABSCH REMARK 1 TITL INTEGRATION, SCALING, SPACE-GROUP ASSIGNMENT AND REMARK 1 TITL 2 POST-REFINEMENT. REMARK 1 REF ACTA CRYSTALLOGR D BIOL V. 66 133 2010 REMARK 1 REF 2 CRYSTALLOGR REMARK 1 REFN ESSN 1399-0047 REMARK 1 PMID 20124693 REMARK 1 DOI 10.1107/S0907444909047374 REMARK 2 REMARK 2 RESOLUTION. 1.84 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 81305 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.460 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 39.9000 - 4.4300 0.99 5925 149 0.1489 0.1640 REMARK 3 2 4.4300 - 3.5200 1.00 5770 146 0.1356 0.1562 REMARK 3 3 3.5200 - 3.0700 1.00 5705 144 0.1618 0.1901 REMARK 3 4 3.0700 - 2.7900 1.00 5693 144 0.1766 0.2131 REMARK 3 5 2.7900 - 2.5900 1.00 5680 143 0.1856 0.2615 REMARK 3 6 2.5900 - 2.4400 1.00 5633 142 0.1807 0.2064 REMARK 3 7 2.4400 - 2.3200 1.00 5646 142 0.1774 0.2370 REMARK 3 8 2.3200 - 2.2200 1.00 5624 142 0.1830 0.2622 REMARK 3 9 2.2200 - 2.1300 1.00 5619 142 0.1907 0.2220 REMARK 3 10 2.1300 - 2.0600 1.00 5617 141 0.2098 0.2408 REMARK 3 11 2.0600 - 1.9900 1.00 5608 142 0.2242 0.2703 REMARK 3 12 1.9900 - 1.9400 1.00 5576 140 0.2444 0.2694 REMARK 3 13 1.9400 - 1.8900 1.00 5623 143 0.2888 0.3569 REMARK 3 14 1.8900 - 1.8400 1.00 5586 140 0.3512 0.3716 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.30 REMARK 3 SHRINKAGE RADIUS : 1.20 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.239 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.497 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 29.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.00 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 : 0.007 6396 REMARK 3 ANGLE : 0.851 8716 REMARK 3 CHIRALITY : 0.057 996 REMARK 3 PLANARITY : 0.007 1116 REMARK 3 DIHEDRAL : 12.947 2309 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 9GGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1292140972. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.1 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8731 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : KB MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81380 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840 REMARK 200 RESOLUTION RANGE LOW (A) : 44.360 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.00 REMARK 200 R MERGE (I) : 0.17700 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) : 1.84 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 13.50 REMARK 200 R MERGE FOR SHELL (I) : 2.86900 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: PLATE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM CITRATE DIBASIC 20% W/V REMARK 280 POLYETHYLENE GLYCOL 3,350 PH 5.1, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 70.47300 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.77700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.47300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.77700 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10980 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 32670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL 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 703 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 459 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 A -9 REMARK 465 ARG A -8 REMARK 465 GLY A -7 REMARK 465 SER A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 HIS A -1 REMARK 465 HIS A 0 REMARK 465 THR A 1 REMARK 465 ASP A 2 REMARK 465 PRO A 3 REMARK 465 GLN A 4 REMARK 465 GLY A 5 REMARK 465 ASP A 6 REMARK 465 ALA A 7 REMARK 465 ALA A 8 REMARK 465 GLN A 9 REMARK 465 LYS A 10 REMARK 465 THR A 11 REMARK 465 ASP A 12 REMARK 465 THR A 13 REMARK 465 SER A 14 REMARK 465 HIS A 15 REMARK 465 HIS A 16 REMARK 465 ASP A 17 REMARK 465 GLN A 18 REMARK 465 ASP A 19 REMARK 465 HIS A 20 REMARK 465 PRO A 21 REMARK 465 THR A 22 REMARK 465 PHE A 23 REMARK 465 SER A 45 REMARK 465 ALA A 355 REMARK 465 ILE A 356 REMARK 465 PRO A 357 REMARK 465 MET A 358 REMARK 465 SER A 359 REMARK 465 ILE A 360 REMARK 465 PRO A 361 REMARK 465 PRO A 362 REMARK 465 GLU A 363 REMARK 465 VAL A 364 REMARK 465 LYS A 365 REMARK 465 PHE A 366 REMARK 465 ASN A 367 REMARK 465 LYS A 368 REMARK 465 PRO A 369 REMARK 465 PHE A 370 REMARK 465 VAL A 371 REMARK 465 PHE A 372 REMARK 465 LEU A 373 REMARK 465 MET A 374 REMARK 465 ILE A 375 REMARK 465 GLU A 376 REMARK 465 GLN A 377 REMARK 465 ASN A 378 REMARK 465 THR A 379 REMARK 465 LYS A 380 REMARK 465 SER A 381 REMARK 465 PRO A 382 REMARK 465 LEU A 383 REMARK 465 PHE A 384 REMARK 465 MET A 385 REMARK 465 GLY A 386 REMARK 465 LYS A 387 REMARK 465 VAL A 388 REMARK 465 VAL A 389 REMARK 465 ASN A 390 REMARK 465 PRO A 391 REMARK 465 THR A 392 REMARK 465 GLN A 393 REMARK 465 LYS A 394 REMARK 465 MET B -9 REMARK 465 ARG B -8 REMARK 465 GLY B -7 REMARK 465 SER B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 REMARK 465 HIS B -3 REMARK 465 HIS B -2 REMARK 465 HIS B -1 REMARK 465 HIS B 0 REMARK 465 THR B 1 REMARK 465 ASP B 2 REMARK 465 PRO B 3 REMARK 465 GLN B 4 REMARK 465 GLY B 5 REMARK 465 ASP B 6 REMARK 465 ALA B 7 REMARK 465 ALA B 8 REMARK 465 GLN B 9 REMARK 465 LYS B 10 REMARK 465 THR B 11 REMARK 465 ASP B 12 REMARK 465 THR B 13 REMARK 465 SER B 14 REMARK 465 HIS B 15 REMARK 465 HIS B 16 REMARK 465 ASP B 17 REMARK 465 GLN B 18 REMARK 465 ASP B 19 REMARK 465 HIS B 20 REMARK 465 PRO B 21 REMARK 465 THR B 22 REMARK 465 PHE B 23 REMARK 465 ASN B 24 REMARK 465 LYS B 25 REMARK 465 ILE B 26 REMARK 465 THR B 27 REMARK 465 PRO B 28 REMARK 465 ASN B 29 REMARK 465 LEU B 30 REMARK 465 ALA B 31 REMARK 465 GLU B 32 REMARK 465 PHE B 33 REMARK 465 ALA B 34 REMARK 465 PHE B 35 REMARK 465 SER B 36 REMARK 465 LEU B 37 REMARK 465 TYR B 38 REMARK 465 ARG B 39 REMARK 465 GLN B 40 REMARK 465 LEU B 41 REMARK 465 ALA B 42 REMARK 465 HIS B 43 REMARK 465 GLN B 44 REMARK 465 SER B 45 REMARK 465 ASN B 46 REMARK 465 SER B 47 REMARK 465 THR B 48 REMARK 465 ASN B 49 REMARK 465 ILE B 50 REMARK 465 PHE B 51 REMARK 465 PHE B 52 REMARK 465 SER B 53 REMARK 465 PRO B 54 REMARK 465 VAL B 55 REMARK 465 SER B 56 REMARK 465 ILE B 57 REMARK 465 ALA B 58 REMARK 465 THR B 59 REMARK 465 ALA B 60 REMARK 465 PHE B 61 REMARK 465 ALA B 62 REMARK 465 MET B 63 REMARK 465 LEU B 64 REMARK 465 SER B 65 REMARK 465 LEU B 66 REMARK 465 GLY B 67 REMARK 465 THR B 68 REMARK 465 LYS B 69 REMARK 465 ALA B 70 REMARK 465 ASP B 71 REMARK 465 THR B 72 REMARK 465 HIS B 73 REMARK 465 ASP B 74 REMARK 465 GLU B 75 REMARK 465 ILE B 76 REMARK 465 LEU B 77 REMARK 465 GLU B 78 REMARK 465 GLY B 79 REMARK 465 LEU B 80 REMARK 465 ASN B 81 REMARK 465 PHE B 82 REMARK 465 ASN B 83 REMARK 465 LEU B 84 REMARK 465 THR B 85 REMARK 465 GLU B 86 REMARK 465 ILE B 87 REMARK 465 PRO B 88 REMARK 465 GLU B 89 REMARK 465 ALA B 90 REMARK 465 GLN B 91 REMARK 465 ILE B 92 REMARK 465 HIS B 93 REMARK 465 GLU B 94 REMARK 465 GLY B 95 REMARK 465 PHE B 96 REMARK 465 GLN B 97 REMARK 465 GLU B 98 REMARK 465 LEU B 99 REMARK 465 LEU B 100 REMARK 465 ARG B 101 REMARK 465 THR B 102 REMARK 465 LEU B 103 REMARK 465 ASN B 104 REMARK 465 GLN B 105 REMARK 465 PRO B 106 REMARK 465 ASP B 107 REMARK 465 SER B 108 REMARK 465 GLN B 109 REMARK 465 LEU B 110 REMARK 465 GLN B 111 REMARK 465 LEU B 112 REMARK 465 THR B 113 REMARK 465 THR B 114 REMARK 465 GLY B 115 REMARK 465 ASN B 116 REMARK 465 GLY B 117 REMARK 465 LEU B 118 REMARK 465 PHE B 119 REMARK 465 LEU B 120 REMARK 465 SER B 121 REMARK 465 GLU B 122 REMARK 465 GLY B 123 REMARK 465 LEU B 124 REMARK 465 LYS B 125 REMARK 465 LEU B 126 REMARK 465 VAL B 127 REMARK 465 ASP B 128 REMARK 465 LYS B 129 REMARK 465 PHE B 130 REMARK 465 LEU B 131 REMARK 465 GLU B 132 REMARK 465 ASP B 133 REMARK 465 VAL B 134 REMARK 465 LYS B 135 REMARK 465 LYS B 136 REMARK 465 LEU B 137 REMARK 465 TYR B 138 REMARK 465 HIS B 139 REMARK 465 SER B 140 REMARK 465 GLU B 141 REMARK 465 ALA B 142 REMARK 465 PHE B 143 REMARK 465 THR B 144 REMARK 465 VAL B 145 REMARK 465 ASN B 146 REMARK 465 PHE B 147 REMARK 465 GLY B 148 REMARK 465 ASP B 149 REMARK 465 THR B 150 REMARK 465 GLU B 151 REMARK 465 GLU B 152 REMARK 465 ALA B 153 REMARK 465 LYS B 154 REMARK 465 LYS B 155 REMARK 465 GLN B 156 REMARK 465 ILE B 157 REMARK 465 ASN B 158 REMARK 465 ASP B 159 REMARK 465 TYR B 160 REMARK 465 VAL B 161 REMARK 465 GLU B 162 REMARK 465 LYS B 163 REMARK 465 GLY B 164 REMARK 465 THR B 165 REMARK 465 GLN B 166 REMARK 465 GLY B 167 REMARK 465 LYS B 168 REMARK 465 ILE B 169 REMARK 465 VAL B 170 REMARK 465 ASP B 171 REMARK 465 LEU B 172 REMARK 465 VAL B 173 REMARK 465 LYS B 174 REMARK 465 GLU B 175 REMARK 465 LEU B 176 REMARK 465 ASP B 177 REMARK 465 ARG B 178 REMARK 465 ASP B 179 REMARK 465 THR B 180 REMARK 465 VAL B 181 REMARK 465 PHE B 182 REMARK 465 ALA B 183 REMARK 465 LEU B 184 REMARK 465 VAL B 185 REMARK 465 ASN B 186 REMARK 465 TYR B 187 REMARK 465 ILE B 188 REMARK 465 PHE B 189 REMARK 465 PHE B 190 REMARK 465 LYS B 191 REMARK 465 GLY B 192 REMARK 465 LYS B 193 REMARK 465 TRP B 194 REMARK 465 GLU B 195 REMARK 465 ARG B 196 REMARK 465 PRO B 197 REMARK 465 PHE B 198 REMARK 465 GLU B 199 REMARK 465 VAL B 200 REMARK 465 LYS B 201 REMARK 465 ASP B 202 REMARK 465 THR B 203 REMARK 465 GLU B 204 REMARK 465 GLU B 205 REMARK 465 GLU B 206 REMARK 465 ASP B 207 REMARK 465 PHE B 208 REMARK 465 HIS B 209 REMARK 465 VAL B 210 REMARK 465 ASP B 211 REMARK 465 GLN B 212 REMARK 465 VAL B 213 REMARK 465 THR B 214 REMARK 465 THR B 215 REMARK 465 VAL B 216 REMARK 465 LYS B 217 REMARK 465 VAL B 218 REMARK 465 PRO B 219 REMARK 465 MET B 220 REMARK 465 MET B 221 REMARK 465 LYS B 222 REMARK 465 ARG B 223 REMARK 465 LEU B 224 REMARK 465 GLY B 225 REMARK 465 MET B 226 REMARK 465 PHE B 227 REMARK 465 ASN B 228 REMARK 465 ILE B 229 REMARK 465 GLN B 230 REMARK 465 HIS B 231 REMARK 465 CYS B 232 REMARK 465 LYS B 233 REMARK 465 LYS B 234 REMARK 465 LEU B 235 REMARK 465 SER B 236 REMARK 465 SER B 237 REMARK 465 TRP B 238 REMARK 465 VAL B 239 REMARK 465 LEU B 240 REMARK 465 LEU B 241 REMARK 465 MET B 242 REMARK 465 LYS B 243 REMARK 465 TYR B 244 REMARK 465 LEU B 245 REMARK 465 GLY B 246 REMARK 465 ASN B 247 REMARK 465 ALA B 248 REMARK 465 THR B 249 REMARK 465 ALA B 250 REMARK 465 ILE B 251 REMARK 465 PHE B 252 REMARK 465 PHE B 253 REMARK 465 LEU B 254 REMARK 465 PRO B 255 REMARK 465 ASP B 256 REMARK 465 GLU B 257 REMARK 465 GLY B 258 REMARK 465 LYS B 259 REMARK 465 LEU B 260 REMARK 465 GLN B 261 REMARK 465 HIS B 262 REMARK 465 LEU B 263 REMARK 465 GLU B 264 REMARK 465 ASN B 265 REMARK 465 GLU B 266 REMARK 465 LEU B 267 REMARK 465 THR B 268 REMARK 465 HIS B 269 REMARK 465 ASP B 270 REMARK 465 ILE B 271 REMARK 465 ILE B 272 REMARK 465 THR B 273 REMARK 465 LYS B 274 REMARK 465 PHE B 275 REMARK 465 LEU B 276 REMARK 465 GLU B 277 REMARK 465 ASN B 278 REMARK 465 GLU B 279 REMARK 465 ASP B 280 REMARK 465 ARG B 281 REMARK 465 ARG B 282 REMARK 465 SER B 283 REMARK 465 ALA B 284 REMARK 465 SER B 285 REMARK 465 LEU B 286 REMARK 465 HIS B 287 REMARK 465 LEU B 288 REMARK 465 PRO B 289 REMARK 465 LYS B 290 REMARK 465 LEU B 291 REMARK 465 SER B 292 REMARK 465 ILE B 293 REMARK 465 THR B 294 REMARK 465 GLY B 295 REMARK 465 THR B 296 REMARK 465 TYR B 297 REMARK 465 ASP B 298 REMARK 465 LEU B 299 REMARK 465 LYS B 300 REMARK 465 SER B 301 REMARK 465 VAL B 302 REMARK 465 LEU B 303 REMARK 465 GLY B 304 REMARK 465 GLN B 305 REMARK 465 LEU B 306 REMARK 465 GLY B 307 REMARK 465 ILE B 308 REMARK 465 THR B 309 REMARK 465 LYS B 310 REMARK 465 VAL B 311 REMARK 465 PHE B 312 REMARK 465 SER B 313 REMARK 465 ASN B 314 REMARK 465 GLY B 315 REMARK 465 ALA B 316 REMARK 465 ASP B 317 REMARK 465 LEU B 318 REMARK 465 SER B 319 REMARK 465 GLY B 320 REMARK 465 VAL B 321 REMARK 465 THR B 322 REMARK 465 GLU B 323 REMARK 465 GLU B 324 REMARK 465 ALA B 325 REMARK 465 PRO B 326 REMARK 465 LEU B 327 REMARK 465 LYS B 328 REMARK 465 LEU B 329 REMARK 465 SER B 330 REMARK 465 LYS B 331 REMARK 465 ALA B 332 REMARK 465 VAL B 333 REMARK 465 HIS B 334 REMARK 465 LYS B 335 REMARK 465 ALA B 336 REMARK 465 VAL B 337 REMARK 465 LEU B 338 REMARK 465 THR B 339 REMARK 465 ILE B 340 REMARK 465 ASP B 341 REMARK 465 GLU B 342 REMARK 465 LYS B 343 REMARK 465 GLY B 344 REMARK 465 THR B 345 REMARK 465 GLU B 346 REMARK 465 ALA B 347 REMARK 465 ALA B 348 REMARK 465 GLY B 349 REMARK 465 ALA B 350 REMARK 465 MET B 351 REMARK 465 PHE B 352 REMARK 465 LEU B 353 REMARK 465 GLU B 354 REMARK 465 ALA B 355 REMARK 465 ILE B 356 REMARK 465 PRO B 357 REMARK 465 MET B 358 REMARK 465 SER B 359 REMARK 465 LYS B 394 REMARK 465 GLN H 130A REMARK 465 THR H 130B REMARK 465 ASN H 130C 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 LYS A 25 CG CD CE NZ REMARK 470 ASN A 46 CG OD1 ND2 REMARK 470 GLN A 105 CD OE1 NE2 REMARK 470 LYS A 125 CD CE NZ REMARK 470 LYS A 136 CE NZ REMARK 470 LYS A 168 NZ REMARK 470 GLU A 175 CD OE1 OE2 REMARK 470 LYS A 201 CD CE NZ REMARK 470 GLN A 212 CG CD OE1 NE2 REMARK 470 LYS A 222 NZ REMARK 470 GLN A 230 CD OE1 NE2 REMARK 470 LYS A 233 CD CE NZ REMARK 470 LYS A 234 CG CD CE NZ REMARK 470 GLU A 257 CD OE1 OE2 REMARK 470 LYS A 274 CD CE NZ REMARK 470 GLU A 324 CG CD OE1 OE2 REMARK 470 LYS B 380 CE NZ REMARK 470 LYS H 5 CE NZ REMARK 470 LYS H 43 CE NZ REMARK 470 LYS H 75 CE NZ REMARK 470 LYS H 81 CD CE NZ REMARK 470 LYS H 115 CE NZ REMARK 470 ASN H 132 CG OD1 ND2 REMARK 470 ASP L 1 CG OD1 OD2 REMARK 470 GLN L 3 CD OE1 NE2 REMARK 470 LYS L 24 CD CE NZ REMARK 470 LYS L 42 CD CE NZ REMARK 470 LYS L 141 CD CE NZ REMARK 470 ASN L 156 CG OD1 ND2 REMARK 470 GLU L 212 CG CD OE1 OE2 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 ALA A 70 -138.83 51.69 REMARK 500 ASN A 81 34.36 70.89 REMARK 500 ASN B 390 102.71 -162.75 REMARK 500 ASN H 99 144.99 90.19 REMARK 500 THR H 100D -169.37 -100.79 REMARK 500 SER H 112 144.81 -173.11 REMARK 500 THR L 51 -50.11 76.03 REMARK 500 LEU L 94 -143.05 50.68 REMARK 500 ASN L 211 54.44 -107.82 REMARK 500 REMARK 500 REMARK: NULL DBREF 9GGP A 2 394 UNP P01009 A1AT_HUMAN 26 418 DBREF 9GGP B 2 394 UNP P01009 A1AT_HUMAN 26 418 DBREF 9GGP H 1 212 PDB 9GGP 9GGP 1 212 DBREF 9GGP L 1 212 PDB 9GGP 9GGP 1 212 SEQADV 9GGP MET A -9 UNP P01009 INITIATING METHIONINE SEQADV 9GGP ARG A -8 UNP P01009 EXPRESSION TAG SEQADV 9GGP GLY A -7 UNP P01009 EXPRESSION TAG SEQADV 9GGP SER A -6 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS A -5 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS A -4 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS A -3 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS A -2 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS A -1 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS A 0 UNP P01009 EXPRESSION TAG SEQADV 9GGP THR A 1 UNP P01009 EXPRESSION TAG SEQADV 9GGP MET B -9 UNP P01009 INITIATING METHIONINE SEQADV 9GGP ARG B -8 UNP P01009 EXPRESSION TAG SEQADV 9GGP GLY B -7 UNP P01009 EXPRESSION TAG SEQADV 9GGP SER B -6 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS B -5 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS B -4 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS B -3 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS B -2 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS B -1 UNP P01009 EXPRESSION TAG SEQADV 9GGP HIS B 0 UNP P01009 EXPRESSION TAG SEQADV 9GGP THR B 1 UNP P01009 EXPRESSION TAG SEQRES 1 A 404 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO SEQRES 2 A 404 GLN GLY ASP ALA ALA GLN LYS THR ASP THR SER HIS HIS SEQRES 3 A 404 ASP GLN ASP HIS PRO THR PHE ASN LYS ILE THR PRO ASN SEQRES 4 A 404 LEU ALA GLU PHE ALA PHE SER LEU TYR ARG GLN LEU ALA SEQRES 5 A 404 HIS GLN SER ASN SER THR ASN ILE PHE PHE SER PRO VAL SEQRES 6 A 404 SER ILE ALA THR ALA PHE ALA MET LEU SER LEU GLY THR SEQRES 7 A 404 LYS ALA ASP THR HIS ASP GLU ILE LEU GLU GLY LEU ASN SEQRES 8 A 404 PHE ASN LEU THR GLU ILE PRO GLU ALA GLN ILE HIS GLU SEQRES 9 A 404 GLY PHE GLN GLU LEU LEU ARG THR LEU ASN GLN PRO ASP SEQRES 10 A 404 SER GLN LEU GLN LEU THR THR GLY ASN GLY LEU PHE LEU SEQRES 11 A 404 SER GLU GLY LEU LYS LEU VAL ASP LYS PHE LEU GLU ASP SEQRES 12 A 404 VAL LYS LYS LEU TYR HIS SER GLU ALA PHE THR VAL ASN SEQRES 13 A 404 PHE GLY ASP THR GLU GLU ALA LYS LYS GLN ILE ASN ASP SEQRES 14 A 404 TYR VAL GLU LYS GLY THR GLN GLY LYS ILE VAL ASP LEU SEQRES 15 A 404 VAL LYS GLU LEU ASP ARG ASP THR VAL PHE ALA LEU VAL SEQRES 16 A 404 ASN TYR ILE PHE PHE LYS GLY LYS TRP GLU ARG PRO PHE SEQRES 17 A 404 GLU VAL LYS ASP THR GLU GLU GLU ASP PHE HIS VAL ASP SEQRES 18 A 404 GLN VAL THR THR VAL LYS VAL PRO MET MET LYS ARG LEU SEQRES 19 A 404 GLY MET PHE ASN ILE GLN HIS CYS LYS LYS LEU SER SER SEQRES 20 A 404 TRP VAL LEU LEU MET LYS TYR LEU GLY ASN ALA THR ALA SEQRES 21 A 404 ILE PHE PHE LEU PRO ASP GLU GLY LYS LEU GLN HIS LEU SEQRES 22 A 404 GLU ASN GLU LEU THR HIS ASP ILE ILE THR LYS PHE LEU SEQRES 23 A 404 GLU ASN GLU ASP ARG ARG SER ALA SER LEU HIS LEU PRO SEQRES 24 A 404 LYS LEU SER ILE THR GLY THR TYR ASP LEU LYS SER VAL SEQRES 25 A 404 LEU GLY GLN LEU GLY ILE THR LYS VAL PHE SER ASN GLY SEQRES 26 A 404 ALA ASP LEU SER GLY VAL THR GLU GLU ALA PRO LEU LYS SEQRES 27 A 404 LEU SER LYS ALA VAL HIS LYS ALA VAL LEU THR ILE ASP SEQRES 28 A 404 GLU LYS GLY THR GLU ALA ALA GLY ALA MET PHE LEU GLU SEQRES 29 A 404 ALA ILE PRO MET SER ILE PRO PRO GLU VAL LYS PHE ASN SEQRES 30 A 404 LYS PRO PHE VAL PHE LEU MET ILE GLU GLN ASN THR LYS SEQRES 31 A 404 SER PRO LEU PHE MET GLY LYS VAL VAL ASN PRO THR GLN SEQRES 32 A 404 LYS SEQRES 1 B 404 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO SEQRES 2 B 404 GLN GLY ASP ALA ALA GLN LYS THR ASP THR SER HIS HIS SEQRES 3 B 404 ASP GLN ASP HIS PRO THR PHE ASN LYS ILE THR PRO ASN SEQRES 4 B 404 LEU ALA GLU PHE ALA PHE SER LEU TYR ARG GLN LEU ALA SEQRES 5 B 404 HIS GLN SER ASN SER THR ASN ILE PHE PHE SER PRO VAL SEQRES 6 B 404 SER ILE ALA THR ALA PHE ALA MET LEU SER LEU GLY THR SEQRES 7 B 404 LYS ALA ASP THR HIS ASP GLU ILE LEU GLU GLY LEU ASN SEQRES 8 B 404 PHE ASN LEU THR GLU ILE PRO GLU ALA GLN ILE HIS GLU SEQRES 9 B 404 GLY PHE GLN GLU LEU LEU ARG THR LEU ASN GLN PRO ASP SEQRES 10 B 404 SER GLN LEU GLN LEU THR THR GLY ASN GLY LEU PHE LEU SEQRES 11 B 404 SER GLU GLY LEU LYS LEU VAL ASP LYS PHE LEU GLU ASP SEQRES 12 B 404 VAL LYS LYS LEU TYR HIS SER GLU ALA PHE THR VAL ASN SEQRES 13 B 404 PHE GLY ASP THR GLU GLU ALA LYS LYS GLN ILE ASN ASP SEQRES 14 B 404 TYR VAL GLU LYS GLY THR GLN GLY LYS ILE VAL ASP LEU SEQRES 15 B 404 VAL LYS GLU LEU ASP ARG ASP THR VAL PHE ALA LEU VAL SEQRES 16 B 404 ASN TYR ILE PHE PHE LYS GLY LYS TRP GLU ARG PRO PHE SEQRES 17 B 404 GLU VAL LYS ASP THR GLU GLU GLU ASP PHE HIS VAL ASP SEQRES 18 B 404 GLN VAL THR THR VAL LYS VAL PRO MET MET LYS ARG LEU SEQRES 19 B 404 GLY MET PHE ASN ILE GLN HIS CYS LYS LYS LEU SER SER SEQRES 20 B 404 TRP VAL LEU LEU MET LYS TYR LEU GLY ASN ALA THR ALA SEQRES 21 B 404 ILE PHE PHE LEU PRO ASP GLU GLY LYS LEU GLN HIS LEU SEQRES 22 B 404 GLU ASN GLU LEU THR HIS ASP ILE ILE THR LYS PHE LEU SEQRES 23 B 404 GLU ASN GLU ASP ARG ARG SER ALA SER LEU HIS LEU PRO SEQRES 24 B 404 LYS LEU SER ILE THR GLY THR TYR ASP LEU LYS SER VAL SEQRES 25 B 404 LEU GLY GLN LEU GLY ILE THR LYS VAL PHE SER ASN GLY SEQRES 26 B 404 ALA ASP LEU SER GLY VAL THR GLU GLU ALA PRO LEU LYS SEQRES 27 B 404 LEU SER LYS ALA VAL HIS LYS ALA VAL LEU THR ILE ASP SEQRES 28 B 404 GLU LYS GLY THR GLU ALA ALA GLY ALA MET PHE LEU GLU SEQRES 29 B 404 ALA ILE PRO MET SER ILE PRO PRO GLU VAL LYS PHE ASN SEQRES 30 B 404 LYS PRO PHE VAL PHE LEU MET ILE GLU GLN ASN THR LYS SEQRES 31 B 404 SER PRO LEU PHE MET GLY LYS VAL VAL ASN PRO THR GLN SEQRES 32 B 404 LYS SEQRES 1 H 222 ASP VAL GLN LEU LYS GLN SER GLY SER SER LEU VAL GLN SEQRES 2 H 222 PRO SER GLN SER LEU SER VAL THR CYS THR VAL SER GLY SEQRES 3 H 222 PHE SER LEU THR SER TYR GLY VAL HIS TRP VAL ARG GLN SEQRES 4 H 222 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP SEQRES 5 H 222 SER GLY GLY GLY THR ASP TYR ASN ALA ALA PHE ILE SER SEQRES 6 H 222 ARG LEU SER ILE THR LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 H 222 PHE PHE LYS MET ASN SER LEU GLN ALA ARG ASP THR ALA SEQRES 8 H 222 ILE TYR TYR CYS ALA ARG ASP PHE TYR GLY ASN TYR GLY SEQRES 9 H 222 ARG TYR THR MET ASN TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 H 222 THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR SEQRES 11 H 222 PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN ASN SER SEQRES 12 H 222 MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO SEQRES 13 H 222 GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SEQRES 14 H 222 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP SEQRES 15 H 222 LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SER SEQRES 16 H 222 THR TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS SEQRES 17 H 222 PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 18 H 222 ARG SEQRES 1 L 212 ASP ILE GLN VAL THR GLN THR PRO SER SER LEU SER ALA SEQRES 2 L 212 SER LEU GLY GLY LYS VAL THR ILE THR CYS LYS THR SER SEQRES 3 L 212 GLN ASP ILE ASN LYS PHE ILE ALA TRP TYR GLN HIS LYS SEQRES 4 L 212 PRO GLY LYS GLY PRO ARG LEU LEU ILE HIS TYR THR SER SEQRES 5 L 212 THR LEU GLN PRO GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY ARG ASP TYR SER PHE SER ILE SER ASN LEU SEQRES 7 L 212 GLU PRO GLU ASP ILE ALA THR TYR TYR CYS LEU GLN TYR SEQRES 8 L 212 ASP ASN LEU TYR THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 9 L 212 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 L 212 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 L 212 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 L 212 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 L 212 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 L 212 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 L 212 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 L 212 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 L 212 ASN ARG ASN GLU HET EDO A 401 4 HET EDO A 402 4 HET EDO H 301 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 5 EDO 3(C2 H6 O2) FORMUL 8 HOH *610(H2 O) HELIX 1 AA1 ILE A 26 GLN A 44 1 19 HELIX 2 AA2 SER A 53 LEU A 66 1 14 HELIX 3 AA3 LYS A 69 LEU A 80 1 12 HELIX 4 AA4 PRO A 88 ASN A 104 1 17 HELIX 5 AA5 VAL A 127 TYR A 138 1 12 HELIX 6 AA6 ASP A 149 THR A 165 1 17 HELIX 7 AA7 GLU A 199 THR A 203 5 5 HELIX 8 AA8 LYS A 259 LEU A 267 1 9 HELIX 9 AA9 THR A 268 ASN A 278 1 11 HELIX 10 AB1 LEU A 299 LEU A 306 1 8 HELIX 11 AB2 THR A 309 SER A 313 5 5 HELIX 12 AB3 ALA H 61 ILE H 64 5 4 HELIX 13 AB4 GLN H 83 THR H 87 5 5 HELIX 14 AB5 SER H 155 SER H 157 5 3 HELIX 15 AB6 PRO H 199 SER H 202 5 4 HELIX 16 AB7 GLU L 79 ILE L 83 5 5 HELIX 17 AB8 SER L 120 THR L 125 1 6 HELIX 18 AB9 LYS L 182 GLU L 186 1 5 SHEET 1 AA1 7 ILE A 50 PHE A 52 0 SHEET 2 AA1 7 PRO B 382 VAL B 388 -1 O MET B 385 N PHE A 52 SHEET 3 AA1 7 PHE B 370 GLU B 376 -1 N PHE B 372 O GLY B 386 SHEET 4 AA1 7 ALA A 248 PRO A 255 -1 N PHE A 253 O VAL B 371 SHEET 5 AA1 7 SER A 237 LYS A 243 -1 N MET A 242 O ALA A 250 SHEET 6 AA1 7 THR A 215 CYS A 232 -1 N GLN A 230 O VAL A 239 SHEET 7 AA1 7 GLU A 204 HIS A 209 -1 N GLU A 204 O MET A 220 SHEET 1 AA2 8 ILE A 50 PHE A 52 0 SHEET 2 AA2 8 PRO B 382 VAL B 388 -1 O MET B 385 N PHE A 52 SHEET 3 AA2 8 PHE B 370 GLU B 376 -1 N PHE B 372 O GLY B 386 SHEET 4 AA2 8 ALA A 248 PRO A 255 -1 N PHE A 253 O VAL B 371 SHEET 5 AA2 8 SER A 237 LYS A 243 -1 N MET A 242 O ALA A 250 SHEET 6 AA2 8 THR A 215 CYS A 232 -1 N GLN A 230 O VAL A 239 SHEET 7 AA2 8 ARG A 282 PRO A 289 -1 O LEU A 286 N ARG A 223 SHEET 8 AA2 8 GLU B 363 LYS B 365 1 O VAL B 364 N SER A 285 SHEET 1 AA3 6 GLU A 141 VAL A 145 0 SHEET 2 AA3 6 GLN A 111 SER A 121 1 N LEU A 120 O PHE A 143 SHEET 3 AA3 6 PHE A 182 LYS A 193 -1 O VAL A 185 N GLY A 117 SHEET 4 AA3 6 GLY A 344 GLU A 354 -1 O LEU A 353 N LEU A 184 SHEET 5 AA3 6 LYS A 331 ILE A 340 -1 N VAL A 333 O PHE A 352 SHEET 6 AA3 6 LEU A 291 ASP A 298 -1 N TYR A 297 O HIS A 334 SHEET 1 AA4 4 GLN H 3 GLN H 6 0 SHEET 2 AA4 4 LEU H 18 SER H 25 -1 O THR H 23 N LYS H 5 SHEET 3 AA4 4 GLN H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA4 4 LEU H 67 ASP H 72 -1 N THR H 70 O PHE H 79 SHEET 1 AA5 6 SER H 10 VAL H 12 0 SHEET 2 AA5 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA5 6 ALA H 88 TYR H 97 -1 N TYR H 90 O THR H 107 SHEET 4 AA5 6 VAL H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA5 6 LEU H 45 ILE H 51 -1 O LEU H 48 N TRP H 36 SHEET 6 AA5 6 THR H 57 TYR H 59 -1 O ASP H 58 N VAL H 50 SHEET 1 AA6 4 SER H 10 VAL H 12 0 SHEET 2 AA6 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA6 4 ALA H 88 TYR H 97 -1 N TYR H 90 O THR H 107 SHEET 4 AA6 4 TYR H 100C ASN H 101 -1 O ASN H 101 N ARG H 94 SHEET 1 AA7 4 SER H 120 LEU H 124 0 SHEET 2 AA7 4 MET H 134 TYR H 144 -1 O LEU H 140 N TYR H 122 SHEET 3 AA7 4 LEU H 173 PRO H 183 -1 O LEU H 176 N VAL H 141 SHEET 4 AA7 4 VAL H 162 THR H 164 -1 N HIS H 163 O SER H 179 SHEET 1 AA8 4 SER H 120 LEU H 124 0 SHEET 2 AA8 4 MET H 134 TYR H 144 -1 O LEU H 140 N TYR H 122 SHEET 3 AA8 4 LEU H 173 PRO H 183 -1 O LEU H 176 N VAL H 141 SHEET 4 AA8 4 VAL H 168 GLN H 170 -1 N GLN H 170 O LEU H 173 SHEET 1 AA9 3 THR H 150 TRP H 153 0 SHEET 2 AA9 3 THR H 193 HIS H 198 -1 O ASN H 195 N THR H 152 SHEET 3 AA9 3 THR H 203 LYS H 208 -1 O VAL H 205 N VAL H 196 SHEET 1 AB1 4 VAL L 4 THR L 7 0 SHEET 2 AB1 4 VAL L 19 THR L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB1 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AB1 4 PHE L 62 SER L 67 -1 N SER L 65 O SER L 72 SHEET 1 AB2 6 SER L 10 ALA L 13 0 SHEET 2 AB2 6 THR L 101 ILE L 105 1 O GLU L 104 N ALA L 13 SHEET 3 AB2 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 101 SHEET 4 AB2 6 ILE L 33 HIS L 38 -1 N HIS L 38 O THR L 85 SHEET 5 AB2 6 ARG L 45 HIS L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB2 6 THR L 53 LEU L 54 -1 O THR L 53 N HIS L 49 SHEET 1 AB3 4 SER L 10 ALA L 13 0 SHEET 2 AB3 4 THR L 101 ILE L 105 1 O GLU L 104 N ALA L 13 SHEET 3 AB3 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 101 SHEET 4 AB3 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 90 SHEET 1 AB4 4 THR L 113 PHE L 117 0 SHEET 2 AB4 4 GLY L 128 PHE L 138 -1 O PHE L 134 N SER L 115 SHEET 3 AB4 4 TYR L 172 THR L 181 -1 O LEU L 180 N ALA L 129 SHEET 4 AB4 4 VAL L 158 TRP L 162 -1 N LEU L 159 O THR L 177 SHEET 1 AB5 4 SER L 152 ARG L 154 0 SHEET 2 AB5 4 ASN L 144 ILE L 149 -1 N ILE L 149 O SER L 152 SHEET 3 AB5 4 SER L 190 THR L 196 -1 O GLU L 194 N LYS L 146 SHEET 4 AB5 4 ILE L 204 ASN L 209 -1 O ILE L 204 N ALA L 195 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.12 SSBOND 2 CYS H 139 CYS H 194 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 4 CYS L 133 CYS L 193 1555 1555 2.05 CISPEP 1 PHE H 145 PRO H 146 0 -4.64 CISPEP 2 GLU H 147 PRO H 148 0 -1.82 CISPEP 3 TRP H 187 PRO H 188 0 4.70 CISPEP 4 THR L 7 PRO L 8 0 -3.73 CISPEP 5 TYR L 139 PRO L 140 0 3.26 CRYST1 140.946 75.554 87.146 90.00 90.00 90.00 P 21 21 2 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 0.007095 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013236 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011475 0.00000