HEADER IMMUNE SYSTEM 10-FEB-25 9LUX TITLE SINGLE-CHAIN FV ANTIBODY OF G2 FUSED WITH ANTIGEN PEPTIDE FROM CHICKEN TITLE 2 PRION PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR PRION PROTEIN HOMOLOG,SINGLE-CHAIN FV ANTIBODY OF G2 COMPND 3 FUSED WITH ANTIGEN PEPTIDE FROM CHICKEN PRION PROTEIN; COMPND 4 CHAIN: A, B, C, D, E, F; COMPND 5 SYNONYM: 65-21 PROTEIN,ACETYLCHOLINE RECEPTOR-INDUCING ACTIVITY,ARIA, COMPND 6 PR-LP; COMPND 7 ENGINEERED: YES; COMPND 8 OTHER_DETAILS: THE FUSION PROTEIN COMPOSED OF AN EXPRESSION TAG COMPND 9 (RESIDUES 1-2), A FRAGMENT FROM CHICKEN PRION PROTEIN (RESIDUES 3- COMPND 10 20), A LINKER (RESIDUES 21-28), THE LIGHT CHAIN (RESIDUES 29-138), A COMPND 11 SECOND LINKER (RESIDUES 139-153), AND THE HEAVY CHAIN (RESIDUES 154- COMPND 12 271). SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS, MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031, 10090; SOURCE 5 GENE: PRNP, PRN-P; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIGEN BINDING, AFFINITY MATURATION, SOMATIC HYPERMUTATION, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.HANAZONO,S.YABUNO,T.HAYASHI,N.NUMOTO,N.ITO,M.ODA REVDAT 1 11-JUN-25 9LUX 0 JRNL AUTH Y.HANAZONO,S.YABUNO,T.HAYASHI,N.NUMOTO,Y.O.KAMATARI,N.ITO, JRNL AUTH 2 M.ODA JRNL TITL ANTIGEN RECOGNITION MECHANISM OF G2 ANTIBODY POSSESSING JRNL TITL 2 MULTI-SPECIFICITY REVEALED BY CRYSTAL STRUCTURES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.85 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 3 NUMBER OF REFLECTIONS : 183558 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.196 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 9155 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 49.3200 - 5.7500 0.99 5936 293 0.1797 0.2014 REMARK 3 2 5.7500 - 4.5600 0.92 5487 292 0.1514 0.1598 REMARK 3 3 4.5600 - 3.9900 0.96 5787 305 0.1444 0.1703 REMARK 3 4 3.9900 - 3.6200 0.98 5798 317 0.1710 0.2092 REMARK 3 5 3.6200 - 3.3600 0.98 5856 311 0.1752 0.2075 REMARK 3 6 3.3600 - 3.1600 0.98 5875 315 0.1976 0.2245 REMARK 3 7 3.1600 - 3.0000 0.99 5884 300 0.1979 0.2202 REMARK 3 8 3.0000 - 2.8700 0.99 5865 313 0.2039 0.2272 REMARK 3 9 2.8700 - 2.7600 0.99 5908 307 0.2143 0.2534 REMARK 3 10 2.7600 - 2.6700 0.99 5895 324 0.2242 0.2620 REMARK 3 11 2.6700 - 2.5800 0.95 5709 272 0.2208 0.2793 REMARK 3 12 2.5800 - 2.5100 0.90 5288 295 0.2113 0.2625 REMARK 3 13 2.5100 - 2.4400 0.97 5790 270 0.2095 0.2744 REMARK 3 14 2.4400 - 2.3900 0.97 5780 318 0.2070 0.2689 REMARK 3 15 2.3900 - 2.3300 0.98 5760 318 0.2142 0.2687 REMARK 3 16 2.3300 - 2.2800 0.97 5834 304 0.2175 0.2621 REMARK 3 17 2.2800 - 2.2400 0.98 5802 328 0.2173 0.2522 REMARK 3 18 2.2400 - 2.1900 0.98 5898 288 0.2137 0.2494 REMARK 3 19 2.1900 - 2.1500 0.98 5785 292 0.2147 0.2753 REMARK 3 20 2.1500 - 2.1200 0.98 5826 329 0.2301 0.2568 REMARK 3 21 2.1200 - 2.0800 0.98 5997 280 0.2313 0.2637 REMARK 3 22 2.0800 - 2.0500 0.98 5780 310 0.2326 0.2747 REMARK 3 23 2.0500 - 2.0200 0.98 5864 311 0.2413 0.2734 REMARK 3 24 2.0200 - 1.9900 0.98 5895 322 0.2427 0.2714 REMARK 3 25 1.9900 - 1.9700 0.98 5809 333 0.2541 0.2834 REMARK 3 26 1.9700 - 1.9400 0.98 5942 286 0.2638 0.3167 REMARK 3 27 1.9400 - 1.9200 0.98 5806 301 0.2771 0.2760 REMARK 3 28 1.9200 - 1.8900 0.98 5906 308 0.2932 0.3280 REMARK 3 29 1.8900 - 1.8700 0.98 5870 326 0.2993 0.3499 REMARK 3 30 1.8700 - 1.8500 0.97 5771 287 0.3086 0.3323 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) : 0.247 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.737 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.16 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 : 0.009 11974 REMARK 3 ANGLE : 1.014 16233 REMARK 3 CHIRALITY : 0.060 1766 REMARK 3 PLANARITY : 0.007 2091 REMARK 3 DIHEDRAL : 14.009 4297 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 9LUX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300056397. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-AUG-21 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 : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 183582 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.09400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 3.20 REMARK 200 R MERGE FOR SHELL (I) : 0.78600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 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: 6PGX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M AMMONIUM SULPHATE, 0.1 M SODIUM REMARK 280 CITRATE TRIBASIC DIHYDRATE PH 5.6, 1.0 M LITHIUM SULFATE REMARK 280 MONOHYDRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F 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 MET A 1 REMARK 465 GLY A 139 REMARK 465 GLY A 140 REMARK 465 GLY A 141 REMARK 465 GLY A 142 REMARK 465 SER A 143 REMARK 465 GLY A 144 REMARK 465 GLY A 145 REMARK 465 GLY A 146 REMARK 465 GLY A 147 REMARK 465 SER A 148 REMARK 465 GLY A 149 REMARK 465 GLY A 150 REMARK 465 GLY A 151 REMARK 465 GLY A 152 REMARK 465 SER A 153 REMARK 465 MET B 1 REMARK 465 GLY B 139 REMARK 465 GLY B 140 REMARK 465 GLY B 141 REMARK 465 GLY B 142 REMARK 465 SER B 143 REMARK 465 GLY B 144 REMARK 465 GLY B 145 REMARK 465 GLY B 146 REMARK 465 GLY B 147 REMARK 465 SER B 148 REMARK 465 GLY B 149 REMARK 465 GLY B 150 REMARK 465 GLY B 151 REMARK 465 GLY B 152 REMARK 465 SER B 153 REMARK 465 MET C 1 REMARK 465 GLY C 139 REMARK 465 GLY C 140 REMARK 465 GLY C 141 REMARK 465 GLY C 142 REMARK 465 SER C 143 REMARK 465 GLY C 144 REMARK 465 GLY C 145 REMARK 465 GLY C 146 REMARK 465 GLY C 147 REMARK 465 SER C 148 REMARK 465 GLY C 149 REMARK 465 GLY C 150 REMARK 465 GLY C 151 REMARK 465 GLY C 152 REMARK 465 SER C 153 REMARK 465 GLU C 154 REMARK 465 VAL C 155 REMARK 465 MET C 156 REMARK 465 MET D 1 REMARK 465 GLY D 139 REMARK 465 GLY D 140 REMARK 465 GLY D 141 REMARK 465 GLY D 142 REMARK 465 SER D 143 REMARK 465 GLY D 144 REMARK 465 GLY D 145 REMARK 465 GLY D 146 REMARK 465 GLY D 147 REMARK 465 SER D 148 REMARK 465 GLY D 149 REMARK 465 GLY D 150 REMARK 465 GLY D 151 REMARK 465 GLY D 152 REMARK 465 SER D 153 REMARK 465 GLU D 154 REMARK 465 VAL D 155 REMARK 465 MET D 156 REMARK 465 MET E 1 REMARK 465 GLY E 139 REMARK 465 GLY E 140 REMARK 465 GLY E 141 REMARK 465 GLY E 142 REMARK 465 SER E 143 REMARK 465 GLY E 144 REMARK 465 GLY E 145 REMARK 465 GLY E 146 REMARK 465 GLY E 147 REMARK 465 SER E 148 REMARK 465 GLY E 149 REMARK 465 GLY E 150 REMARK 465 GLY E 151 REMARK 465 GLY E 152 REMARK 465 SER E 153 REMARK 465 GLU E 154 REMARK 465 MET F 1 REMARK 465 GLY F 139 REMARK 465 GLY F 140 REMARK 465 GLY F 141 REMARK 465 GLY F 142 REMARK 465 SER F 143 REMARK 465 GLY F 144 REMARK 465 GLY F 145 REMARK 465 GLY F 146 REMARK 465 GLY F 147 REMARK 465 SER F 148 REMARK 465 GLY F 149 REMARK 465 GLY F 150 REMARK 465 GLY F 151 REMARK 465 GLY F 152 REMARK 465 SER F 153 REMARK 465 GLU F 154 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 83 -40.51 69.95 REMARK 500 ASP A 126 -142.91 45.21 REMARK 500 ALA A 202 148.27 -170.38 REMARK 500 ASP B 60 86.55 -66.25 REMARK 500 ALA B 83 -37.28 70.94 REMARK 500 ALA B 116 -179.75 -174.33 REMARK 500 ASP B 126 -143.86 50.64 REMARK 500 ALA B 202 149.88 -171.58 REMARK 500 ALA C 83 -49.12 75.14 REMARK 500 ASP C 126 -141.73 47.40 REMARK 500 ALA C 202 147.34 -171.27 REMARK 500 LYS D 18 92.77 -68.87 REMARK 500 ASP D 60 -119.66 47.90 REMARK 500 ALA D 83 -40.90 74.34 REMARK 500 ALA D 116 173.22 177.93 REMARK 500 ASP D 126 -144.01 48.30 REMARK 500 ALA D 202 145.70 -171.94 REMARK 500 ALA E 83 -44.51 73.69 REMARK 500 SER E 84 -0.02 -143.34 REMARK 500 ALA E 116 172.86 177.13 REMARK 500 ASP E 126 -142.34 53.54 REMARK 500 ALA E 202 144.11 -175.07 REMARK 500 SER E 270 -163.96 -73.57 REMARK 500 ASP F 60 93.04 -63.72 REMARK 500 ALA F 83 -40.56 73.07 REMARK 500 SER F 84 -0.01 -141.87 REMARK 500 ASP F 126 -142.58 48.10 REMARK 500 ALA F 202 141.56 179.57 REMARK 500 SER F 270 -156.38 -76.64 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 D 571 DISTANCE = 6.62 ANGSTROMS DBREF 9LUX A 3 20 UNP P27177 PRIO_CHICK 212 229 DBREF 9LUX A 21 271 PDB 9LUX 9LUX 21 271 DBREF 9LUX B 3 20 UNP P27177 PRIO_CHICK 212 229 DBREF 9LUX B 21 271 PDB 9LUX 9LUX 21 271 DBREF 9LUX C 3 20 UNP P27177 PRIO_CHICK 212 229 DBREF 9LUX C 21 271 PDB 9LUX 9LUX 21 271 DBREF 9LUX D 3 20 UNP P27177 PRIO_CHICK 212 229 DBREF 9LUX D 21 271 PDB 9LUX 9LUX 21 271 DBREF 9LUX E 3 20 UNP P27177 PRIO_CHICK 212 229 DBREF 9LUX E 21 271 PDB 9LUX 9LUX 21 271 DBREF 9LUX F 3 20 UNP P27177 PRIO_CHICK 212 229 DBREF 9LUX F 21 271 PDB 9LUX 9LUX 21 271 SEQADV 9LUX MET A 1 UNP P27177 INITIATING METHIONINE SEQADV 9LUX GLY A 2 UNP P27177 EXPRESSION TAG SEQADV 9LUX MET B 1 UNP P27177 INITIATING METHIONINE SEQADV 9LUX GLY B 2 UNP P27177 EXPRESSION TAG SEQADV 9LUX MET C 1 UNP P27177 INITIATING METHIONINE SEQADV 9LUX GLY C 2 UNP P27177 EXPRESSION TAG SEQADV 9LUX MET D 1 UNP P27177 INITIATING METHIONINE SEQADV 9LUX GLY D 2 UNP P27177 EXPRESSION TAG SEQADV 9LUX MET E 1 UNP P27177 INITIATING METHIONINE SEQADV 9LUX GLY E 2 UNP P27177 EXPRESSION TAG SEQADV 9LUX MET F 1 UNP P27177 INITIATING METHIONINE SEQADV 9LUX GLY F 2 UNP P27177 EXPRESSION TAG SEQRES 1 A 271 MET GLY GLU ALA VAL ALA ALA ALA ASN GLN THR GLU VAL SEQRES 2 A 271 GLU MET GLU ASN LYS VAL VAL LEU GLU VAL LEU PHE GLN SEQRES 3 A 271 GLY PRO ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SEQRES 4 A 271 ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS SEQRES 5 A 271 ALA SER GLN THR LEU ASP TYR ASP GLY GLY THR TYR MET SEQRES 6 A 271 ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 7 A 271 LEU ILE PHE ALA ALA SER ASN LEU GLU SER GLY ILE PRO SEQRES 8 A 271 ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 9 A 271 LEU ASN ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR SEQRES 10 A 271 TYR TYR CYS GLN GLN SER ARG GLU ASP LEU THR PHE GLY SEQRES 11 A 271 ALA GLY THR LYS LEU ASP LEU LYS GLY GLY GLY GLY SER SEQRES 12 A 271 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL MET SEQRES 13 A 271 LEU VAL GLU SER GLY GLY VAL LEU VAL LYS PRO GLY GLY SEQRES 14 A 271 SER LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SEQRES 15 A 271 SER ARG TYR ALA MET SER TRP VAL ARG GLN THR PRO GLU SEQRES 16 A 271 LYS ARG LEU GLU TRP VAL ALA SER ILE SER SER GLY GLY SEQRES 17 A 271 SER TYR THR PHE TYR PRO ASP SER VAL LYS GLY ARG PHE SEQRES 18 A 271 THR ILE SER ARG ASN ASN ALA LYS ASN PHE LEU TYR LEU SEQRES 19 A 271 LYS MET SER SER LEU ARG SER GLU ASP THR ALA MET TYR SEQRES 20 A 271 TYR CYS ALA ARG SER GLY ASN ASP TYR ALA VAL ASP TYR SEQRES 21 A 271 TRP GLY GLN GLY THR SER VAL THR VAL SER SER SEQRES 1 B 271 MET GLY GLU ALA VAL ALA ALA ALA ASN GLN THR GLU VAL SEQRES 2 B 271 GLU MET GLU ASN LYS VAL VAL LEU GLU VAL LEU PHE GLN SEQRES 3 B 271 GLY PRO ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SEQRES 4 B 271 ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS SEQRES 5 B 271 ALA SER GLN THR LEU ASP TYR ASP GLY GLY THR TYR MET SEQRES 6 B 271 ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 7 B 271 LEU ILE PHE ALA ALA SER ASN LEU GLU SER GLY ILE PRO SEQRES 8 B 271 ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 9 B 271 LEU ASN ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR SEQRES 10 B 271 TYR TYR CYS GLN GLN SER ARG GLU ASP LEU THR PHE GLY SEQRES 11 B 271 ALA GLY THR LYS LEU ASP LEU LYS GLY GLY GLY GLY SER SEQRES 12 B 271 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL MET SEQRES 13 B 271 LEU VAL GLU SER GLY GLY VAL LEU VAL LYS PRO GLY GLY SEQRES 14 B 271 SER LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SEQRES 15 B 271 SER ARG TYR ALA MET SER TRP VAL ARG GLN THR PRO GLU SEQRES 16 B 271 LYS ARG LEU GLU TRP VAL ALA SER ILE SER SER GLY GLY SEQRES 17 B 271 SER TYR THR PHE TYR PRO ASP SER VAL LYS GLY ARG PHE SEQRES 18 B 271 THR ILE SER ARG ASN ASN ALA LYS ASN PHE LEU TYR LEU SEQRES 19 B 271 LYS MET SER SER LEU ARG SER GLU ASP THR ALA MET TYR SEQRES 20 B 271 TYR CYS ALA ARG SER GLY ASN ASP TYR ALA VAL ASP TYR SEQRES 21 B 271 TRP GLY GLN GLY THR SER VAL THR VAL SER SER SEQRES 1 C 271 MET GLY GLU ALA VAL ALA ALA ALA ASN GLN THR GLU VAL SEQRES 2 C 271 GLU MET GLU ASN LYS VAL VAL LEU GLU VAL LEU PHE GLN SEQRES 3 C 271 GLY PRO ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SEQRES 4 C 271 ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS SEQRES 5 C 271 ALA SER GLN THR LEU ASP TYR ASP GLY GLY THR TYR MET SEQRES 6 C 271 ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 7 C 271 LEU ILE PHE ALA ALA SER ASN LEU GLU SER GLY ILE PRO SEQRES 8 C 271 ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 9 C 271 LEU ASN ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR SEQRES 10 C 271 TYR TYR CYS GLN GLN SER ARG GLU ASP LEU THR PHE GLY SEQRES 11 C 271 ALA GLY THR LYS LEU ASP LEU LYS GLY GLY GLY GLY SER SEQRES 12 C 271 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL MET SEQRES 13 C 271 LEU VAL GLU SER GLY GLY VAL LEU VAL LYS PRO GLY GLY SEQRES 14 C 271 SER LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SEQRES 15 C 271 SER ARG TYR ALA MET SER TRP VAL ARG GLN THR PRO GLU SEQRES 16 C 271 LYS ARG LEU GLU TRP VAL ALA SER ILE SER SER GLY GLY SEQRES 17 C 271 SER TYR THR PHE TYR PRO ASP SER VAL LYS GLY ARG PHE SEQRES 18 C 271 THR ILE SER ARG ASN ASN ALA LYS ASN PHE LEU TYR LEU SEQRES 19 C 271 LYS MET SER SER LEU ARG SER GLU ASP THR ALA MET TYR SEQRES 20 C 271 TYR CYS ALA ARG SER GLY ASN ASP TYR ALA VAL ASP TYR SEQRES 21 C 271 TRP GLY GLN GLY THR SER VAL THR VAL SER SER SEQRES 1 D 271 MET GLY GLU ALA VAL ALA ALA ALA ASN GLN THR GLU VAL SEQRES 2 D 271 GLU MET GLU ASN LYS VAL VAL LEU GLU VAL LEU PHE GLN SEQRES 3 D 271 GLY PRO ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SEQRES 4 D 271 ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS SEQRES 5 D 271 ALA SER GLN THR LEU ASP TYR ASP GLY GLY THR TYR MET SEQRES 6 D 271 ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 7 D 271 LEU ILE PHE ALA ALA SER ASN LEU GLU SER GLY ILE PRO SEQRES 8 D 271 ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 9 D 271 LEU ASN ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR SEQRES 10 D 271 TYR TYR CYS GLN GLN SER ARG GLU ASP LEU THR PHE GLY SEQRES 11 D 271 ALA GLY THR LYS LEU ASP LEU LYS GLY GLY GLY GLY SER SEQRES 12 D 271 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL MET SEQRES 13 D 271 LEU VAL GLU SER GLY GLY VAL LEU VAL LYS PRO GLY GLY SEQRES 14 D 271 SER LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SEQRES 15 D 271 SER ARG TYR ALA MET SER TRP VAL ARG GLN THR PRO GLU SEQRES 16 D 271 LYS ARG LEU GLU TRP VAL ALA SER ILE SER SER GLY GLY SEQRES 17 D 271 SER TYR THR PHE TYR PRO ASP SER VAL LYS GLY ARG PHE SEQRES 18 D 271 THR ILE SER ARG ASN ASN ALA LYS ASN PHE LEU TYR LEU SEQRES 19 D 271 LYS MET SER SER LEU ARG SER GLU ASP THR ALA MET TYR SEQRES 20 D 271 TYR CYS ALA ARG SER GLY ASN ASP TYR ALA VAL ASP TYR SEQRES 21 D 271 TRP GLY GLN GLY THR SER VAL THR VAL SER SER SEQRES 1 E 271 MET GLY GLU ALA VAL ALA ALA ALA ASN GLN THR GLU VAL SEQRES 2 E 271 GLU MET GLU ASN LYS VAL VAL LEU GLU VAL LEU PHE GLN SEQRES 3 E 271 GLY PRO ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SEQRES 4 E 271 ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS SEQRES 5 E 271 ALA SER GLN THR LEU ASP TYR ASP GLY GLY THR TYR MET SEQRES 6 E 271 ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 7 E 271 LEU ILE PHE ALA ALA SER ASN LEU GLU SER GLY ILE PRO SEQRES 8 E 271 ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 9 E 271 LEU ASN ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR SEQRES 10 E 271 TYR TYR CYS GLN GLN SER ARG GLU ASP LEU THR PHE GLY SEQRES 11 E 271 ALA GLY THR LYS LEU ASP LEU LYS GLY GLY GLY GLY SER SEQRES 12 E 271 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL MET SEQRES 13 E 271 LEU VAL GLU SER GLY GLY VAL LEU VAL LYS PRO GLY GLY SEQRES 14 E 271 SER LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SEQRES 15 E 271 SER ARG TYR ALA MET SER TRP VAL ARG GLN THR PRO GLU SEQRES 16 E 271 LYS ARG LEU GLU TRP VAL ALA SER ILE SER SER GLY GLY SEQRES 17 E 271 SER TYR THR PHE TYR PRO ASP SER VAL LYS GLY ARG PHE SEQRES 18 E 271 THR ILE SER ARG ASN ASN ALA LYS ASN PHE LEU TYR LEU SEQRES 19 E 271 LYS MET SER SER LEU ARG SER GLU ASP THR ALA MET TYR SEQRES 20 E 271 TYR CYS ALA ARG SER GLY ASN ASP TYR ALA VAL ASP TYR SEQRES 21 E 271 TRP GLY GLN GLY THR SER VAL THR VAL SER SER SEQRES 1 F 271 MET GLY GLU ALA VAL ALA ALA ALA ASN GLN THR GLU VAL SEQRES 2 F 271 GLU MET GLU ASN LYS VAL VAL LEU GLU VAL LEU PHE GLN SEQRES 3 F 271 GLY PRO ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SEQRES 4 F 271 ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS SEQRES 5 F 271 ALA SER GLN THR LEU ASP TYR ASP GLY GLY THR TYR MET SEQRES 6 F 271 ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 7 F 271 LEU ILE PHE ALA ALA SER ASN LEU GLU SER GLY ILE PRO SEQRES 8 F 271 ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 9 F 271 LEU ASN ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR SEQRES 10 F 271 TYR TYR CYS GLN GLN SER ARG GLU ASP LEU THR PHE GLY SEQRES 11 F 271 ALA GLY THR LYS LEU ASP LEU LYS GLY GLY GLY GLY SER SEQRES 12 F 271 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL MET SEQRES 13 F 271 LEU VAL GLU SER GLY GLY VAL LEU VAL LYS PRO GLY GLY SEQRES 14 F 271 SER LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SEQRES 15 F 271 SER ARG TYR ALA MET SER TRP VAL ARG GLN THR PRO GLU SEQRES 16 F 271 LYS ARG LEU GLU TRP VAL ALA SER ILE SER SER GLY GLY SEQRES 17 F 271 SER TYR THR PHE TYR PRO ASP SER VAL LYS GLY ARG PHE SEQRES 18 F 271 THR ILE SER ARG ASN ASN ALA LYS ASN PHE LEU TYR LEU SEQRES 19 F 271 LYS MET SER SER LEU ARG SER GLU ASP THR ALA MET TYR SEQRES 20 F 271 TYR CYS ALA ARG SER GLY ASN ASP TYR ALA VAL ASP TYR SEQRES 21 F 271 TRP GLY GLN GLY THR SER VAL THR VAL SER SER HET SO4 A 301 5 HET SO4 A 302 5 HET SO4 A 303 5 HET SO4 A 304 5 HET GOL A 305 6 HET SO4 B 301 5 HET SO4 B 302 5 HET GOL B 303 6 HET SO4 C 301 5 HET SO4 C 302 5 HET SO4 C 303 5 HET SO4 C 304 5 HET GOL C 305 6 HET GOL C 306 6 HET SO4 D 301 5 HET SO4 D 302 5 HET SO4 D 303 5 HET SO4 E 301 5 HET SO4 F 301 5 HETNAM SO4 SULFATE ION HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 SO4 15(O4 S 2-) FORMUL 11 GOL 4(C3 H8 O3) FORMUL 26 HOH *982(H2 O) HELIX 1 AA1 ALA A 7 GLU A 14 5 8 HELIX 2 AA2 GLU A 111 ALA A 115 5 5 HELIX 3 AA3 THR A 181 TYR A 185 5 5 HELIX 4 AA4 PRO A 214 LYS A 218 5 5 HELIX 5 AA5 ARG A 240 THR A 244 5 5 HELIX 6 AA6 ASN A 254 TYR A 256 5 3 HELIX 7 AA7 ALA B 7 GLU B 14 5 8 HELIX 8 AA8 GLU B 111 ALA B 115 5 5 HELIX 9 AA9 THR B 181 TYR B 185 5 5 HELIX 10 AB1 PRO B 214 LYS B 218 5 5 HELIX 11 AB2 ARG B 240 THR B 244 5 5 HELIX 12 AB3 ASN B 254 TYR B 256 5 3 HELIX 13 AB4 ALA C 7 GLU C 14 5 8 HELIX 14 AB5 GLU C 111 ALA C 115 5 5 HELIX 15 AB6 THR C 181 TYR C 185 5 5 HELIX 16 AB7 PRO C 214 LYS C 218 5 5 HELIX 17 AB8 ARG C 240 THR C 244 5 5 HELIX 18 AB9 ASN C 254 TYR C 256 5 3 HELIX 19 AC1 ALA D 7 GLU D 14 5 8 HELIX 20 AC2 GLU D 111 ALA D 115 5 5 HELIX 21 AC3 THR D 181 TYR D 185 5 5 HELIX 22 AC4 PRO D 214 LYS D 218 5 5 HELIX 23 AC5 ARG D 240 THR D 244 5 5 HELIX 24 AC6 ASN D 254 TYR D 256 5 3 HELIX 25 AC7 ALA E 7 GLU E 14 5 8 HELIX 26 AC8 GLU E 111 ALA E 115 5 5 HELIX 27 AC9 THR E 181 TYR E 185 5 5 HELIX 28 AD1 PRO E 214 LYS E 218 5 5 HELIX 29 AD2 ARG E 240 THR E 244 5 5 HELIX 30 AD3 ASN E 254 TYR E 256 5 3 HELIX 31 AD4 ALA F 7 GLU F 14 5 8 HELIX 32 AD5 GLU F 111 ALA F 115 5 5 HELIX 33 AD6 THR F 181 TYR F 185 5 5 HELIX 34 AD7 PRO F 214 LYS F 218 5 5 HELIX 35 AD8 ARG F 240 THR F 244 5 5 HELIX 36 AD9 ASN F 254 TYR F 256 5 3 SHEET 1 AA1 6 LEU A 21 VAL A 23 0 SHEET 2 AA1 6 TYR A 210 PHE A 212 1 O THR A 211 N VAL A 23 SHEET 3 AA1 6 LEU A 198 ILE A 204 -1 N SER A 203 O PHE A 212 SHEET 4 AA1 6 MET A 187 GLN A 192 -1 N ARG A 191 O GLU A 199 SHEET 5 AA1 6 ALA A 245 SER A 252 -1 O TYR A 248 N VAL A 190 SHEET 6 AA1 6 VAL A 258 TRP A 261 -1 O TYR A 260 N ARG A 251 SHEET 1 AA210 LEU A 21 VAL A 23 0 SHEET 2 AA210 TYR A 210 PHE A 212 1 O THR A 211 N VAL A 23 SHEET 3 AA210 LEU A 198 ILE A 204 -1 N SER A 203 O PHE A 212 SHEET 4 AA210 MET A 187 GLN A 192 -1 N ARG A 191 O GLU A 199 SHEET 5 AA210 ALA A 245 SER A 252 -1 O TYR A 248 N VAL A 190 SHEET 6 AA210 THR A 265 VAL A 269 -1 O THR A 265 N TYR A 247 SHEET 7 AA210 MET A 156 VAL A 165 1 N GLY A 161 O SER A 266 SHEET 8 AA210 LEU E 171 SER E 178 -1 O SER E 174 N SER A 160 SHEET 9 AA210 PHE E 231 MET E 236 -1 O LEU E 234 N LEU E 173 SHEET 10 AA210 PHE E 221 ASN E 226 -1 N THR E 222 O LYS E 235 SHEET 1 AA3 4 LEU A 32 SER A 35 0 SHEET 2 AA3 4 ALA A 47 ALA A 53 -1 O SER A 50 N SER A 35 SHEET 3 AA3 4 ASP A 102 ILE A 107 -1 O LEU A 105 N ILE A 49 SHEET 4 AA3 4 PHE A 94 SER A 99 -1 N SER A 95 O ASN A 106 SHEET 1 AA412 ASN A 85 LEU A 86 0 SHEET 2 AA412 LYS A 77 PHE A 81 -1 N PHE A 81 O ASN A 85 SHEET 3 AA412 MET A 65 GLN A 70 -1 N TRP A 67 O LEU A 79 SHEET 4 AA412 ALA A 116 GLN A 122 -1 O GLN A 121 N ASN A 66 SHEET 5 AA412 THR A 133 LEU A 137 -1 O LEU A 135 N ALA A 116 SHEET 6 AA412 SER A 38 VAL A 41 1 N LEU A 39 O ASP A 136 SHEET 7 AA412 SER C 38 VAL C 41 -1 O SER C 38 N ALA A 40 SHEET 8 AA412 THR C 133 LEU C 137 1 O ASP C 136 N LEU C 39 SHEET 9 AA412 ALA C 116 GLN C 122 -1 N ALA C 116 O LEU C 135 SHEET 10 AA412 MET C 65 GLN C 70 -1 N GLN C 70 O THR C 117 SHEET 11 AA412 LYS C 77 PHE C 81 -1 O LEU C 79 N TRP C 67 SHEET 12 AA412 ASN C 85 LEU C 86 -1 O ASN C 85 N PHE C 81 SHEET 1 AA5 8 THR A 128 PHE A 129 0 SHEET 2 AA5 8 ALA A 116 GLN A 122 -1 N GLN A 122 O THR A 128 SHEET 3 AA5 8 THR A 133 LEU A 137 -1 O LEU A 135 N ALA A 116 SHEET 4 AA5 8 SER A 38 VAL A 41 1 N LEU A 39 O ASP A 136 SHEET 5 AA5 8 SER C 38 VAL C 41 -1 O SER C 38 N ALA A 40 SHEET 6 AA5 8 THR C 133 LEU C 137 1 O ASP C 136 N LEU C 39 SHEET 7 AA5 8 ALA C 116 GLN C 122 -1 N ALA C 116 O LEU C 135 SHEET 8 AA5 8 THR C 128 PHE C 129 -1 O THR C 128 N GLN C 122 SHEET 1 AA6 4 PHE A 221 ASN A 226 0 SHEET 2 AA6 4 PHE A 231 MET A 236 -1 O LYS A 235 N THR A 222 SHEET 3 AA6 4 LEU A 171 SER A 178 -1 N LEU A 171 O MET A 236 SHEET 4 AA6 4 LEU E 157 SER E 160 -1 O GLU E 159 N SER A 176 SHEET 1 AA7 6 LEU B 21 VAL B 23 0 SHEET 2 AA7 6 TYR B 210 PHE B 212 1 O THR B 211 N VAL B 23 SHEET 3 AA7 6 LEU B 198 ILE B 204 -1 N SER B 203 O PHE B 212 SHEET 4 AA7 6 MET B 187 GLN B 192 -1 N ARG B 191 O GLU B 199 SHEET 5 AA7 6 ALA B 245 SER B 252 -1 O TYR B 248 N VAL B 190 SHEET 6 AA7 6 VAL B 258 TRP B 261 -1 O TYR B 260 N ARG B 251 SHEET 1 AA810 LEU B 21 VAL B 23 0 SHEET 2 AA810 TYR B 210 PHE B 212 1 O THR B 211 N VAL B 23 SHEET 3 AA810 LEU B 198 ILE B 204 -1 N SER B 203 O PHE B 212 SHEET 4 AA810 MET B 187 GLN B 192 -1 N ARG B 191 O GLU B 199 SHEET 5 AA810 ALA B 245 SER B 252 -1 O TYR B 248 N VAL B 190 SHEET 6 AA810 THR B 265 VAL B 269 -1 O VAL B 267 N ALA B 245 SHEET 7 AA810 MET B 156 VAL B 165 1 N VAL B 165 O THR B 268 SHEET 8 AA810 LEU F 171 SER F 178 -1 O SER F 176 N VAL B 158 SHEET 9 AA810 PHE F 231 MET F 236 -1 O MET F 236 N LEU F 171 SHEET 10 AA810 PHE F 221 ASN F 226 -1 N SER F 224 O TYR F 233 SHEET 1 AA9 4 LEU B 32 SER B 35 0 SHEET 2 AA9 4 ALA B 47 ALA B 53 -1 O SER B 50 N SER B 35 SHEET 3 AA9 4 ASP B 102 ILE B 107 -1 O LEU B 105 N ILE B 49 SHEET 4 AA9 4 PHE B 94 SER B 99 -1 N SER B 95 O ASN B 106 SHEET 1 AB112 ASN B 85 LEU B 86 0 SHEET 2 AB112 LYS B 77 PHE B 81 -1 N PHE B 81 O ASN B 85 SHEET 3 AB112 MET B 65 GLN B 70 -1 N TRP B 67 O LEU B 79 SHEET 4 AB112 ALA B 116 GLN B 122 -1 O GLN B 121 N ASN B 66 SHEET 5 AB112 THR B 133 LEU B 137 -1 O LEU B 135 N ALA B 116 SHEET 6 AB112 SER B 38 VAL B 41 1 N LEU B 39 O ASP B 136 SHEET 7 AB112 SER D 38 VAL D 41 -1 O ALA D 40 N SER B 38 SHEET 8 AB112 THR D 133 LEU D 137 1 O ASP D 136 N LEU D 39 SHEET 9 AB112 ALA D 116 GLN D 122 -1 N ALA D 116 O LEU D 135 SHEET 10 AB112 MET D 65 GLN D 70 -1 N ASN D 66 O GLN D 121 SHEET 11 AB112 LYS D 77 PHE D 81 -1 O LEU D 79 N TRP D 67 SHEET 12 AB112 ASN D 85 LEU D 86 -1 O ASN D 85 N PHE D 81 SHEET 1 AB2 8 THR B 128 PHE B 129 0 SHEET 2 AB2 8 ALA B 116 GLN B 122 -1 N GLN B 122 O THR B 128 SHEET 3 AB2 8 THR B 133 LEU B 137 -1 O LEU B 135 N ALA B 116 SHEET 4 AB2 8 SER B 38 VAL B 41 1 N LEU B 39 O ASP B 136 SHEET 5 AB2 8 SER D 38 VAL D 41 -1 O ALA D 40 N SER B 38 SHEET 6 AB2 8 THR D 133 LEU D 137 1 O ASP D 136 N LEU D 39 SHEET 7 AB2 8 ALA D 116 GLN D 122 -1 N ALA D 116 O LEU D 135 SHEET 8 AB2 8 THR D 128 PHE D 129 -1 O THR D 128 N GLN D 122 SHEET 1 AB3 2 ASP B 58 TYR B 59 0 SHEET 2 AB3 2 GLY B 62 THR B 63 -1 O GLY B 62 N TYR B 59 SHEET 1 AB4 4 PHE B 221 ASN B 226 0 SHEET 2 AB4 4 PHE B 231 MET B 236 -1 O TYR B 233 N SER B 224 SHEET 3 AB4 4 LEU B 171 SER B 178 -1 N LEU B 171 O MET B 236 SHEET 4 AB4 4 LEU F 157 SER F 160 -1 O GLU F 159 N SER B 176 SHEET 1 AB5 7 LEU C 21 VAL C 23 0 SHEET 2 AB5 7 TYR C 210 PHE C 212 1 O THR C 211 N VAL C 23 SHEET 3 AB5 7 LEU C 198 ILE C 204 -1 N SER C 203 O PHE C 212 SHEET 4 AB5 7 MET C 187 GLN C 192 -1 N ARG C 191 O GLU C 199 SHEET 5 AB5 7 ALA C 245 SER C 252 -1 O TYR C 248 N VAL C 190 SHEET 6 AB5 7 THR C 265 VAL C 269 -1 O THR C 265 N TYR C 247 SHEET 7 AB5 7 VAL C 163 VAL C 165 1 N VAL C 163 O SER C 266 SHEET 1 AB6 6 LEU C 21 VAL C 23 0 SHEET 2 AB6 6 TYR C 210 PHE C 212 1 O THR C 211 N VAL C 23 SHEET 3 AB6 6 LEU C 198 ILE C 204 -1 N SER C 203 O PHE C 212 SHEET 4 AB6 6 MET C 187 GLN C 192 -1 N ARG C 191 O GLU C 199 SHEET 5 AB6 6 ALA C 245 SER C 252 -1 O TYR C 248 N VAL C 190 SHEET 6 AB6 6 VAL C 258 TRP C 261 -1 O TYR C 260 N ARG C 251 SHEET 1 AB7 4 LEU C 32 SER C 35 0 SHEET 2 AB7 4 ALA C 47 ALA C 53 -1 O LYS C 52 N THR C 33 SHEET 3 AB7 4 ASP C 102 ILE C 107 -1 O LEU C 105 N ILE C 49 SHEET 4 AB7 4 PHE C 94 SER C 99 -1 N SER C 95 O ASN C 106 SHEET 1 AB8 2 ASP C 58 TYR C 59 0 SHEET 2 AB8 2 GLY C 62 THR C 63 -1 O GLY C 62 N TYR C 59 SHEET 1 AB9 3 LEU C 171 SER C 176 0 SHEET 2 AB9 3 PHE C 231 MET C 236 -1 O MET C 236 N LEU C 171 SHEET 3 AB9 3 PHE C 221 ASN C 226 -1 N THR C 222 O LYS C 235 SHEET 1 AC1 7 LEU D 21 VAL D 23 0 SHEET 2 AC1 7 TYR D 210 PHE D 212 1 O THR D 211 N VAL D 23 SHEET 3 AC1 7 LEU D 198 ILE D 204 -1 N SER D 203 O PHE D 212 SHEET 4 AC1 7 MET D 187 GLN D 192 -1 N ARG D 191 O GLU D 199 SHEET 5 AC1 7 ALA D 245 SER D 252 -1 O TYR D 248 N VAL D 190 SHEET 6 AC1 7 THR D 265 VAL D 269 -1 O VAL D 267 N ALA D 245 SHEET 7 AC1 7 VAL D 163 VAL D 165 1 N VAL D 165 O THR D 268 SHEET 1 AC2 6 LEU D 21 VAL D 23 0 SHEET 2 AC2 6 TYR D 210 PHE D 212 1 O THR D 211 N VAL D 23 SHEET 3 AC2 6 LEU D 198 ILE D 204 -1 N SER D 203 O PHE D 212 SHEET 4 AC2 6 MET D 187 GLN D 192 -1 N ARG D 191 O GLU D 199 SHEET 5 AC2 6 ALA D 245 SER D 252 -1 O TYR D 248 N VAL D 190 SHEET 6 AC2 6 VAL D 258 TRP D 261 -1 O TYR D 260 N ARG D 251 SHEET 1 AC3 4 LEU D 32 SER D 35 0 SHEET 2 AC3 4 ALA D 47 ALA D 53 -1 O SER D 50 N SER D 35 SHEET 3 AC3 4 ASP D 102 ILE D 107 -1 O LEU D 105 N ILE D 49 SHEET 4 AC3 4 PHE D 94 SER D 99 -1 N SER D 95 O ASN D 106 SHEET 1 AC4 3 LEU D 171 SER D 176 0 SHEET 2 AC4 3 PHE D 231 MET D 236 -1 O MET D 236 N LEU D 171 SHEET 3 AC4 3 PHE D 221 ASN D 226 -1 N SER D 224 O TYR D 233 SHEET 1 AC5 7 LEU E 21 VAL E 23 0 SHEET 2 AC5 7 TYR E 210 PHE E 212 1 O THR E 211 N VAL E 23 SHEET 3 AC5 7 LEU E 198 ILE E 204 -1 N SER E 203 O PHE E 212 SHEET 4 AC5 7 MET E 187 GLN E 192 -1 N ARG E 191 O GLU E 199 SHEET 5 AC5 7 ALA E 245 SER E 252 -1 O TYR E 248 N VAL E 190 SHEET 6 AC5 7 THR E 265 VAL E 269 -1 O THR E 265 N TYR E 247 SHEET 7 AC5 7 VAL E 163 VAL E 165 1 N VAL E 165 O THR E 268 SHEET 1 AC6 6 LEU E 21 VAL E 23 0 SHEET 2 AC6 6 TYR E 210 PHE E 212 1 O THR E 211 N VAL E 23 SHEET 3 AC6 6 LEU E 198 ILE E 204 -1 N SER E 203 O PHE E 212 SHEET 4 AC6 6 MET E 187 GLN E 192 -1 N ARG E 191 O GLU E 199 SHEET 5 AC6 6 ALA E 245 SER E 252 -1 O TYR E 248 N VAL E 190 SHEET 6 AC6 6 VAL E 258 TRP E 261 -1 O TYR E 260 N ARG E 251 SHEET 1 AC7 4 LEU E 32 SER E 35 0 SHEET 2 AC7 4 ALA E 47 ALA E 53 -1 O SER E 50 N SER E 35 SHEET 3 AC7 4 ASP E 102 ILE E 107 -1 O LEU E 105 N ILE E 49 SHEET 4 AC7 4 PHE E 94 SER E 99 -1 N SER E 95 O ASN E 106 SHEET 1 AC8 6 SER E 38 VAL E 41 0 SHEET 2 AC8 6 THR E 133 LEU E 137 1 O ASP E 136 N LEU E 39 SHEET 3 AC8 6 ALA E 116 GLN E 122 -1 N ALA E 116 O LEU E 135 SHEET 4 AC8 6 MET E 65 GLN E 70 -1 N ASN E 66 O GLN E 121 SHEET 5 AC8 6 LYS E 77 PHE E 81 -1 O LEU E 79 N TRP E 67 SHEET 6 AC8 6 ASN E 85 LEU E 86 -1 O ASN E 85 N PHE E 81 SHEET 1 AC9 4 SER E 38 VAL E 41 0 SHEET 2 AC9 4 THR E 133 LEU E 137 1 O ASP E 136 N LEU E 39 SHEET 3 AC9 4 ALA E 116 GLN E 122 -1 N ALA E 116 O LEU E 135 SHEET 4 AC9 4 THR E 128 PHE E 129 -1 O THR E 128 N GLN E 122 SHEET 1 AD1 2 ASP E 58 TYR E 59 0 SHEET 2 AD1 2 GLY E 62 THR E 63 -1 O GLY E 62 N TYR E 59 SHEET 1 AD2 7 LEU F 21 LEU F 24 0 SHEET 2 AD2 7 TYR F 210 TYR F 213 1 O THR F 211 N VAL F 23 SHEET 3 AD2 7 LEU F 198 ILE F 204 -1 N SER F 203 O PHE F 212 SHEET 4 AD2 7 MET F 187 GLN F 192 -1 N ARG F 191 O GLU F 199 SHEET 5 AD2 7 ALA F 245 SER F 252 -1 O TYR F 248 N VAL F 190 SHEET 6 AD2 7 THR F 265 VAL F 269 -1 O THR F 265 N TYR F 247 SHEET 7 AD2 7 VAL F 163 VAL F 165 1 N VAL F 165 O THR F 268 SHEET 1 AD3 6 LEU F 21 LEU F 24 0 SHEET 2 AD3 6 TYR F 210 TYR F 213 1 O THR F 211 N VAL F 23 SHEET 3 AD3 6 LEU F 198 ILE F 204 -1 N SER F 203 O PHE F 212 SHEET 4 AD3 6 MET F 187 GLN F 192 -1 N ARG F 191 O GLU F 199 SHEET 5 AD3 6 ALA F 245 SER F 252 -1 O TYR F 248 N VAL F 190 SHEET 6 AD3 6 VAL F 258 TRP F 261 -1 O TYR F 260 N ARG F 251 SHEET 1 AD4 4 LEU F 32 SER F 35 0 SHEET 2 AD4 4 ALA F 47 ALA F 53 -1 O LYS F 52 N THR F 33 SHEET 3 AD4 4 ASP F 102 ILE F 107 -1 O LEU F 105 N ILE F 49 SHEET 4 AD4 4 PHE F 94 SER F 99 -1 N SER F 95 O ASN F 106 SHEET 1 AD5 6 SER F 38 VAL F 41 0 SHEET 2 AD5 6 THR F 133 LEU F 137 1 O ASP F 136 N LEU F 39 SHEET 3 AD5 6 ALA F 116 GLN F 122 -1 N ALA F 116 O LEU F 135 SHEET 4 AD5 6 MET F 65 GLN F 70 -1 N GLN F 70 O THR F 117 SHEET 5 AD5 6 LYS F 77 PHE F 81 -1 O LEU F 79 N TRP F 67 SHEET 6 AD5 6 ASN F 85 LEU F 86 -1 O ASN F 85 N PHE F 81 SHEET 1 AD6 4 SER F 38 VAL F 41 0 SHEET 2 AD6 4 THR F 133 LEU F 137 1 O ASP F 136 N LEU F 39 SHEET 3 AD6 4 ALA F 116 GLN F 122 -1 N ALA F 116 O LEU F 135 SHEET 4 AD6 4 THR F 128 PHE F 129 -1 O THR F 128 N GLN F 122 SHEET 1 AD7 2 ASP F 58 TYR F 59 0 SHEET 2 AD7 2 GLY F 62 THR F 63 -1 O GLY F 62 N TYR F 59 SSBOND 1 CYS A 51 CYS A 120 1555 1555 2.15 SSBOND 2 CYS A 175 CYS A 249 1555 1555 2.04 SSBOND 3 CYS B 51 CYS B 120 1555 1555 2.10 SSBOND 4 CYS B 175 CYS B 249 1555 1555 2.06 SSBOND 5 CYS C 51 CYS C 120 1555 1555 2.12 SSBOND 6 CYS C 175 CYS C 249 1555 1555 2.07 SSBOND 7 CYS D 51 CYS D 120 1555 1555 2.14 SSBOND 8 CYS D 175 CYS D 249 1555 1555 2.05 SSBOND 9 CYS E 51 CYS E 120 1555 1555 2.09 SSBOND 10 CYS E 175 CYS E 249 1555 1555 2.07 SSBOND 11 CYS F 51 CYS F 120 1555 1555 2.08 SSBOND 12 CYS F 175 CYS F 249 1555 1555 2.06 CISPEP 1 SER A 35 PRO A 36 0 -6.03 CISPEP 2 HIS A 108 PRO A 109 0 -1.84 CISPEP 3 SER B 35 PRO B 36 0 -7.36 CISPEP 4 HIS B 108 PRO B 109 0 0.47 CISPEP 5 SER C 35 PRO C 36 0 -4.60 CISPEP 6 HIS C 108 PRO C 109 0 -8.20 CISPEP 7 SER D 35 PRO D 36 0 -2.19 CISPEP 8 HIS D 108 PRO D 109 0 -1.67 CISPEP 9 SER E 35 PRO E 36 0 -7.81 CISPEP 10 HIS E 108 PRO E 109 0 -2.97 CISPEP 11 SER F 35 PRO F 36 0 -4.19 CISPEP 12 HIS F 108 PRO F 109 0 0.41 CRYST1 86.360 86.720 86.580 105.13 107.91 100.88 P 1 6 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 0.011579 0.002226 0.004790 0.00000 SCALE2 0.000000 0.011742 0.004265 0.00000 SCALE3 0.000000 0.000000 0.012914 0.00000