HEADER IMMUNE SYSTEM 26-SEP-24 9DS3 TITLE CRYSTAL STRUCTURE OF APO-241_2F04 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 241_2F04, HEAVY CHAIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 241_2F04, LIGHT CHAIN; COMPND 7 CHAIN: I, C; COMPND 8 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 KEYWDS ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.H.LIN,I.A.WILSON REVDAT 1 01-OCT-25 9DS3 0 JRNL AUTH T.H.LIN,N.MOORE,I.A.WILSON,A.H.ELLEBEDY,S.H.KLEINSTEIN, JRNL AUTH 2 A.B.WARD,J.S.TURNER,F.KRAMMER,P.M.PRESTI,S.A.TEEFEY, JRNL AUTH 3 W.D.MIDDLETON,T.SUESSEN,K.HOEHN,A.J.SCHMITZ,J.Q.ZHOU, JRNL AUTH 4 B.M.MOHAMMED,S.K.MSLLSDI,M.WNAG,M.MCMAHON,J.HAN,W.KIM, JRNL AUTH 5 H.MENG,K.M.MCINTIRE JRNL TITL CRYSTAL STRUCTURE OF 05.GC.W13.02 FAB IN COMPLEX WITH H1 HA JRNL TITL 2 FROM A/CALIFORNIA/04/2009(H1N1) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.67 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.5 REMARK 3 NUMBER OF REFLECTIONS : 102180 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.209 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 5067 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 37.6700 - 5.9000 0.99 3597 180 0.1915 0.2010 REMARK 3 2 5.9000 - 4.6900 1.00 3577 180 0.1571 0.1738 REMARK 3 3 4.6900 - 4.0900 1.00 3553 197 0.1462 0.1615 REMARK 3 4 4.0900 - 3.7200 1.00 3543 184 0.1660 0.1884 REMARK 3 5 3.7200 - 3.4500 1.00 3513 183 0.1874 0.2162 REMARK 3 6 3.4500 - 3.2500 1.00 3556 186 0.1809 0.2271 REMARK 3 7 3.2500 - 3.0900 1.00 3511 186 0.1979 0.2207 REMARK 3 8 3.0900 - 2.9500 0.99 3521 159 0.2071 0.2498 REMARK 3 9 2.9500 - 2.8400 0.99 3502 192 0.2082 0.2255 REMARK 3 10 2.8400 - 2.7400 0.99 3481 165 0.2018 0.2246 REMARK 3 11 2.7400 - 2.6600 0.98 3518 175 0.2060 0.2471 REMARK 3 12 2.6600 - 2.5800 0.98 3467 201 0.2118 0.2456 REMARK 3 13 2.5800 - 2.5100 0.98 3469 179 0.2236 0.2561 REMARK 3 14 2.5100 - 2.4500 0.97 3423 178 0.2220 0.2496 REMARK 3 15 2.4500 - 2.4000 0.97 3430 173 0.2160 0.3022 REMARK 3 16 2.4000 - 2.3400 0.97 3432 170 0.2282 0.2469 REMARK 3 17 2.3400 - 2.3000 0.97 3422 211 0.2260 0.2752 REMARK 3 18 2.3000 - 2.2500 0.95 3342 190 0.2740 0.3345 REMARK 3 19 2.2500 - 2.2100 0.97 3418 162 0.3476 0.3687 REMARK 3 20 2.2100 - 2.1800 0.94 3326 168 0.2674 0.2778 REMARK 3 21 2.1800 - 2.1400 0.96 3362 174 0.2634 0.2926 REMARK 3 22 2.1400 - 2.1100 0.95 3414 172 0.2588 0.2822 REMARK 3 23 2.1100 - 2.0800 0.94 3280 194 0.2650 0.2877 REMARK 3 24 2.0800 - 2.0500 0.92 3196 156 0.2883 0.3137 REMARK 3 25 2.0500 - 2.0200 0.88 3145 181 0.2954 0.3319 REMARK 3 26 2.0200 - 1.9900 0.79 2777 149 0.3128 0.3053 REMARK 3 27 1.9900 - 1.9700 0.70 2442 111 0.3208 0.3478 REMARK 3 28 1.9700 - 1.9500 0.62 2223 104 0.3388 0.3979 REMARK 3 29 1.9500 - 1.9200 0.55 1900 110 0.3807 0.3926 REMARK 3 30 1.9200 - 1.9000 0.50 1773 97 0.4038 0.4634 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) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.240 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 : 0.006 6844 REMARK 3 ANGLE : 0.884 9306 REMARK 3 CHIRALITY : 0.056 1044 REMARK 3 PLANARITY : 0.007 1192 REMARK 3 DIHEDRAL : 6.255 942 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 9DS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288701. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-SEP-22 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 : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102332 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 37.670 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : 0.17000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.90000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, PH 6.2, 20% REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 75.97500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.98650 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 75.97500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 58.98650 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3650 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 CYS I 215 REMARK 465 CYS C 215 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH B 457 O HOH B 510 1.80 REMARK 500 O HOH I 393 O HOH I 445 1.81 REMARK 500 O HOH C 363 O HOH C 460 1.84 REMARK 500 O HOH I 415 O HOH I 444 1.85 REMARK 500 O HOH B 448 O HOH C 382 1.85 REMARK 500 O HOH C 422 O HOH C 434 1.89 REMARK 500 O HOH I 434 O HOH C 438 1.93 REMARK 500 OD2 ASP B 62 O HOH B 301 1.94 REMARK 500 O HOH C 336 O HOH C 436 1.95 REMARK 500 O HOH C 429 O HOH C 442 1.98 REMARK 500 O HOH I 401 O HOH I 443 2.00 REMARK 500 O HOH B 438 O HOH B 441 2.01 REMARK 500 O HOH I 423 O HOH I 432 2.03 REMARK 500 OG SER C 63 O HOH C 301 2.04 REMARK 500 O HOH C 423 O HOH C 436 2.07 REMARK 500 O HOH B 310 O HOH B 426 2.08 REMARK 500 O HOH B 506 O HOH B 514 2.08 REMARK 500 O HOH B 383 O HOH B 392 2.09 REMARK 500 O HOH A 442 O HOH A 479 2.12 REMARK 500 O HOH B 464 O HOH B 468 2.13 REMARK 500 O HOH B 313 O HOH B 467 2.13 REMARK 500 O HOH B 306 O HOH B 470 2.15 REMARK 500 O HOH C 438 O HOH C 461 2.15 REMARK 500 NE ARG A 19 O HOH A 301 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 471 O HOH C 432 4545 1.96 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 ALA A 92 164.91 177.82 REMARK 500 SER A 102 -63.59 -92.77 REMARK 500 ASP A 154 65.96 61.13 REMARK 500 SER I 30 -133.07 52.74 REMARK 500 ALA I 51 -14.82 73.35 REMARK 500 ALA I 84 -178.18 -174.71 REMARK 500 ASN I 139 62.56 60.98 REMARK 500 ALA B 92 167.04 179.52 REMARK 500 ASP B 154 63.07 64.44 REMARK 500 SER C 30 -131.31 52.68 REMARK 500 ALA C 51 -16.41 71.28 REMARK 500 SER C 52 -2.43 -143.79 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 I 457 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH I 458 DISTANCE = 6.28 ANGSTROMS REMARK 525 HOH I 459 DISTANCE = 6.34 ANGSTROMS REMARK 525 HOH I 460 DISTANCE = 9.09 ANGSTROMS REMARK 525 HOH I 461 DISTANCE = 9.31 ANGSTROMS REMARK 525 HOH B 513 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH B 514 DISTANCE = 6.23 ANGSTROMS DBREF 9DS3 A 1 226 PDB 9DS3 9DS3 1 226 DBREF 9DS3 I 1 215 PDB 9DS3 9DS3 1 215 DBREF 9DS3 B 1 226 PDB 9DS3 9DS3 1 226 DBREF 9DS3 C 1 215 PDB 9DS3 9DS3 1 215 SEQRES 1 A 226 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 226 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 A 226 PHE THR PHE SER LYS TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 A 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 A 226 GLY SER GLY ILE SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 226 GLY ARG PHE THR ILE SER ARG ASP THR SER LYS ASN MET SEQRES 7 A 226 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 226 ALA ILE TYR TYR CYS ALA LYS ASP ALA ILE SER GLY GLN SEQRES 9 A 226 ILE TRP LEU GLN GLY THR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 A 226 THR LEU VAL THR VAL PHE ASN GLN ILE LYS GLY PRO SER SEQRES 11 A 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 A 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 A 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 A 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 A 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 A 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 A 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 A 226 GLU PRO LYS SER CYS SEQRES 1 I 215 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 I 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 I 215 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 I 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 I 215 THR ARG ALA THR GLY ILE PRO PRO ARG PHE SER GLY SER SEQRES 6 I 215 GLY SER GLY THR GLU PHE SER LEU THR ILE SER SER LEU SEQRES 7 I 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 I 215 ASN ASN TRP PRO PRO ILE THR PHE GLY GLN GLY THR ARG SEQRES 9 I 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 I 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 I 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 I 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 I 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 I 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 I 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 I 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 I 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 226 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 226 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 B 226 PHE THR PHE SER LYS TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 B 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 B 226 GLY SER GLY ILE SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 B 226 GLY ARG PHE THR ILE SER ARG ASP THR SER LYS ASN MET SEQRES 7 B 226 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 226 ALA ILE TYR TYR CYS ALA LYS ASP ALA ILE SER GLY GLN SEQRES 9 B 226 ILE TRP LEU GLN GLY THR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 B 226 THR LEU VAL THR VAL PHE ASN GLN ILE LYS GLY PRO SER SEQRES 11 B 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 B 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 B 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 B 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 B 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 B 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 B 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 B 226 GLU PRO LYS SER CYS SEQRES 1 C 215 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 C 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 C 215 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 C 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 C 215 THR ARG ALA THR GLY ILE PRO PRO ARG PHE SER GLY SER SEQRES 6 C 215 GLY SER GLY THR GLU PHE SER LEU THR ILE SER SER LEU SEQRES 7 C 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 C 215 ASN ASN TRP PRO PRO ILE THR PHE GLY GLN GLY THR ARG SEQRES 9 C 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 C 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 C 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 C 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 C 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 C 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 C 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 C 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 C 215 SER PHE ASN ARG GLY GLU CYS FORMUL 5 HOH *736(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 THR A 74 LYS A 76 5 3 HELIX 3 AA3 ARG A 87 THR A 91 5 5 HELIX 4 AA4 GLN A 104 GLN A 108 5 5 HELIX 5 AA5 SER A 166 ALA A 168 5 3 HELIX 6 AA6 SER A 197 LEU A 199 5 3 HELIX 7 AA7 LYS A 211 ASN A 214 5 4 HELIX 8 AA8 GLN I 79 PHE I 83 5 5 HELIX 9 AA9 SER I 122 SER I 128 1 7 HELIX 10 AB1 LYS I 184 GLU I 188 1 5 HELIX 11 AB2 THR B 28 TYR B 32 5 5 HELIX 12 AB3 ASP B 62 LYS B 65 5 4 HELIX 13 AB4 ARG B 87 THR B 91 5 5 HELIX 14 AB5 GLN B 104 GLN B 108 5 5 HELIX 15 AB6 SER B 166 ALA B 168 5 3 HELIX 16 AB7 SER B 197 GLY B 200 5 4 HELIX 17 AB8 LYS B 211 ASN B 214 5 4 HELIX 18 AB9 GLN C 79 PHE C 83 5 5 HELIX 19 AC1 SER C 122 SER C 128 1 7 HELIX 20 AC2 LYS C 184 GLU C 188 1 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N LEU A 5 SHEET 3 AA1 4 MET A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 118 VAL A 122 1 O THR A 121 N VAL A 12 SHEET 3 AA2 6 ALA A 92 ASP A 99 -1 N TYR A 94 O THR A 118 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O TYR A 59 N HIS A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 118 VAL A 122 1 O THR A 121 N VAL A 12 SHEET 3 AA3 4 ALA A 92 ASP A 99 -1 N TYR A 94 O THR A 118 SHEET 4 AA3 4 PHE A 111 TRP A 114 -1 O TYR A 113 N LYS A 98 SHEET 1 AA4 4 SER A 130 LEU A 134 0 SHEET 2 AA4 4 THR A 145 TYR A 155 -1 O LEU A 151 N PHE A 132 SHEET 3 AA4 4 TYR A 186 PRO A 195 -1 O VAL A 194 N ALA A 146 SHEET 4 AA4 4 VAL A 173 THR A 175 -1 N HIS A 174 O VAL A 191 SHEET 1 AA5 4 SER A 130 LEU A 134 0 SHEET 2 AA5 4 THR A 145 TYR A 155 -1 O LEU A 151 N PHE A 132 SHEET 3 AA5 4 TYR A 186 PRO A 195 -1 O VAL A 194 N ALA A 146 SHEET 4 AA5 4 VAL A 179 LEU A 180 -1 N VAL A 179 O SER A 187 SHEET 1 AA6 3 THR A 161 TRP A 164 0 SHEET 2 AA6 3 ILE A 205 HIS A 210 -1 O ASN A 207 N SER A 163 SHEET 3 AA6 3 THR A 215 LYS A 220 -1 O VAL A 217 N VAL A 208 SHEET 1 AA7 4 MET I 4 THR I 5 0 SHEET 2 AA7 4 ALA I 19 ALA I 25 -1 O ARG I 24 N THR I 5 SHEET 3 AA7 4 GLU I 70 ILE I 75 -1 O LEU I 73 N LEU I 21 SHEET 4 AA7 4 PHE I 62 SER I 67 -1 N SER I 63 O THR I 74 SHEET 1 AA8 6 THR I 10 VAL I 13 0 SHEET 2 AA8 6 THR I 103 ILE I 107 1 O ARG I 104 N LEU I 11 SHEET 3 AA8 6 VAL I 85 GLN I 90 -1 N TYR I 86 O THR I 103 SHEET 4 AA8 6 LEU I 33 GLN I 38 -1 N ALA I 34 O GLN I 89 SHEET 5 AA8 6 ARG I 45 TYR I 49 -1 O LEU I 47 N TRP I 35 SHEET 6 AA8 6 THR I 53 ARG I 54 -1 O THR I 53 N TYR I 49 SHEET 1 AA9 4 THR I 10 VAL I 13 0 SHEET 2 AA9 4 THR I 103 ILE I 107 1 O ARG I 104 N LEU I 11 SHEET 3 AA9 4 VAL I 85 GLN I 90 -1 N TYR I 86 O THR I 103 SHEET 4 AA9 4 THR I 98 PHE I 99 -1 O THR I 98 N GLN I 90 SHEET 1 AB1 4 SER I 115 PHE I 119 0 SHEET 2 AB1 4 THR I 130 PHE I 140 -1 O LEU I 136 N PHE I 117 SHEET 3 AB1 4 TYR I 174 SER I 183 -1 O LEU I 182 N ALA I 131 SHEET 4 AB1 4 SER I 160 VAL I 164 -1 N GLN I 161 O THR I 179 SHEET 1 AB2 4 ALA I 154 LEU I 155 0 SHEET 2 AB2 4 LYS I 146 VAL I 151 -1 N VAL I 151 O ALA I 154 SHEET 3 AB2 4 VAL I 192 THR I 198 -1 O GLU I 196 N GLN I 148 SHEET 4 AB2 4 VAL I 206 ASN I 211 -1 O VAL I 206 N VAL I 197 SHEET 1 AB3 4 GLN B 3 SER B 7 0 SHEET 2 AB3 4 LEU B 18 SER B 25 -1 O ALA B 23 N LEU B 5 SHEET 3 AB3 4 MET B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AB3 4 PHE B 68 ASP B 73 -1 N SER B 71 O TYR B 80 SHEET 1 AB4 6 LEU B 11 VAL B 12 0 SHEET 2 AB4 6 THR B 118 VAL B 122 1 O THR B 121 N VAL B 12 SHEET 3 AB4 6 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AB4 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AB4 6 LEU B 45 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AB4 6 THR B 58 TYR B 60 -1 O TYR B 59 N HIS B 50 SHEET 1 AB5 4 LEU B 11 VAL B 12 0 SHEET 2 AB5 4 THR B 118 VAL B 122 1 O THR B 121 N VAL B 12 SHEET 3 AB5 4 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AB5 4 PHE B 111 TRP B 114 -1 O TYR B 113 N LYS B 98 SHEET 1 AB6 4 SER B 130 LEU B 134 0 SHEET 2 AB6 4 THR B 145 TYR B 155 -1 O GLY B 149 N LEU B 134 SHEET 3 AB6 4 TYR B 186 PRO B 195 -1 O VAL B 194 N ALA B 146 SHEET 4 AB6 4 VAL B 173 THR B 175 -1 N HIS B 174 O VAL B 191 SHEET 1 AB7 4 SER B 130 LEU B 134 0 SHEET 2 AB7 4 THR B 145 TYR B 155 -1 O GLY B 149 N LEU B 134 SHEET 3 AB7 4 TYR B 186 PRO B 195 -1 O VAL B 194 N ALA B 146 SHEET 4 AB7 4 VAL B 179 LEU B 180 -1 N VAL B 179 O SER B 187 SHEET 1 AB8 3 THR B 161 TRP B 164 0 SHEET 2 AB8 3 TYR B 204 HIS B 210 -1 O ASN B 207 N SER B 163 SHEET 3 AB8 3 THR B 215 VAL B 221 -1 O VAL B 217 N VAL B 208 SHEET 1 AB9 4 MET C 4 GLN C 6 0 SHEET 2 AB9 4 ALA C 19 ALA C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AB9 4 GLU C 70 ILE C 75 -1 O LEU C 73 N LEU C 21 SHEET 4 AB9 4 PHE C 62 SER C 67 -1 N SER C 63 O THR C 74 SHEET 1 AC1 6 THR C 10 VAL C 13 0 SHEET 2 AC1 6 THR C 103 ILE C 107 1 O ARG C 104 N LEU C 11 SHEET 3 AC1 6 VAL C 85 GLN C 90 -1 N TYR C 86 O THR C 103 SHEET 4 AC1 6 LEU C 33 GLN C 38 -1 N TYR C 36 O TYR C 87 SHEET 5 AC1 6 ARG C 45 TYR C 49 -1 O LEU C 47 N TRP C 35 SHEET 6 AC1 6 THR C 53 ARG C 54 -1 O THR C 53 N TYR C 49 SHEET 1 AC2 4 THR C 10 VAL C 13 0 SHEET 2 AC2 4 THR C 103 ILE C 107 1 O ARG C 104 N LEU C 11 SHEET 3 AC2 4 VAL C 85 GLN C 90 -1 N TYR C 86 O THR C 103 SHEET 4 AC2 4 THR C 98 PHE C 99 -1 O THR C 98 N GLN C 90 SHEET 1 AC3 4 SER C 115 PHE C 119 0 SHEET 2 AC3 4 THR C 130 PHE C 140 -1 O LEU C 136 N PHE C 117 SHEET 3 AC3 4 TYR C 174 SER C 183 -1 O LEU C 180 N VAL C 133 SHEET 4 AC3 4 SER C 160 VAL C 164 -1 N GLN C 161 O THR C 179 SHEET 1 AC4 4 ALA C 154 LEU C 155 0 SHEET 2 AC4 4 LYS C 146 VAL C 151 -1 N VAL C 151 O ALA C 154 SHEET 3 AC4 4 VAL C 192 THR C 198 -1 O GLU C 196 N GLN C 148 SHEET 4 AC4 4 VAL C 206 ASN C 211 -1 O LYS C 208 N CYS C 195 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.05 SSBOND 2 CYS A 150 CYS A 206 1555 1555 2.03 SSBOND 3 CYS I 23 CYS I 88 1555 1555 2.08 SSBOND 4 CYS I 135 CYS I 195 1555 1555 2.03 SSBOND 5 CYS B 22 CYS B 96 1555 1555 2.06 SSBOND 6 CYS B 150 CYS B 206 1555 1555 2.04 SSBOND 7 CYS C 23 CYS C 88 1555 1555 2.08 SSBOND 8 CYS C 135 CYS C 195 1555 1555 2.02 CISPEP 1 PHE A 156 PRO A 157 0 -6.53 CISPEP 2 GLU A 158 PRO A 159 0 1.46 CISPEP 3 SER I 7 PRO I 8 0 9.84 CISPEP 4 TRP I 94 PRO I 95 0 4.89 CISPEP 5 PRO I 95 PRO I 96 0 -2.88 CISPEP 6 TYR I 141 PRO I 142 0 1.92 CISPEP 7 PHE B 156 PRO B 157 0 -1.76 CISPEP 8 GLU B 158 PRO B 159 0 1.32 CISPEP 9 SER C 7 PRO C 8 0 9.35 CISPEP 10 TRP C 94 PRO C 95 0 3.34 CISPEP 11 PRO C 95 PRO C 96 0 -6.39 CISPEP 12 TYR C 141 PRO C 142 0 3.03 CRYST1 151.950 117.973 93.428 90.00 120.10 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 0.006581 0.000000 0.003815 0.00000 SCALE2 0.000000 0.008477 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012372 0.00000