HEADER IMMUNE SYSTEM 29-OCT-24 9KAT TITLE CRYSTAL STRUCTURE OF ANTI-SULFONYLUREA ANTIBODY SCFV APO FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-SULFONYLUREA ANTIBODY SCFV; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR X.T.YU,Y.G.GAO,H.T.LEI REVDAT 1 16-APR-25 9KAT 0 JRNL AUTH X.YU,T.ZHOU,K.PAN,M.H.FAN,X.YAN,X.A.HUANG,H.ZHANG,X.SHEN, JRNL AUTH 2 H.XIE,Y.G.GAO,H.LEI JRNL TITL STRUCTURE PROFILING OF BROAD-SPECIFICITY IMMUNOASSAYS: JRNL TITL 2 MULTITARGET RECOGNITION FOR SULFONYLUREA ADULTERATION IN JRNL TITL 3 FOOD. JRNL REF J.AGRIC.FOOD CHEM. 2025 JRNL REFN ESSN 1520-5118 JRNL PMID 40173361 JRNL DOI 10.1021/ACS.JAFC.5C00655 REMARK 2 REMARK 2 RESOLUTION. 1.51 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.18.2_3874: ???) 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) : 1.51 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.16 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 81033 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.200 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.214 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4053 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 29.1600 - 4.6300 1.00 2861 151 0.1992 0.2099 REMARK 3 2 4.6300 - 3.6800 1.00 2748 145 0.1645 0.1617 REMARK 3 3 3.6800 - 3.2200 1.00 2708 142 0.1824 0.1920 REMARK 3 4 3.2200 - 2.9200 1.00 2693 142 0.2031 0.2241 REMARK 3 5 2.9200 - 2.7100 1.00 2685 141 0.2066 0.2284 REMARK 3 6 2.7100 - 2.5500 1.00 2685 142 0.2050 0.2148 REMARK 3 7 2.5500 - 2.4300 1.00 2647 139 0.2093 0.1892 REMARK 3 8 2.4200 - 2.3200 1.00 2674 141 0.2065 0.2332 REMARK 3 9 2.3200 - 2.2300 1.00 2649 139 0.1993 0.2125 REMARK 3 10 2.2300 - 2.1500 1.00 2642 139 0.2033 0.2517 REMARK 3 11 2.1500 - 2.0900 1.00 2673 141 0.1975 0.1843 REMARK 3 12 2.0900 - 2.0300 1.00 2621 138 0.1983 0.2262 REMARK 3 13 2.0300 - 1.9700 1.00 2674 141 0.1967 0.2227 REMARK 3 14 1.9700 - 1.9200 1.00 2624 138 0.1988 0.2569 REMARK 3 15 1.9200 - 1.8800 1.00 2643 139 0.2035 0.2495 REMARK 3 16 1.8800 - 1.8400 1.00 2657 140 0.2019 0.2383 REMARK 3 17 1.8400 - 1.8000 1.00 2619 138 0.2164 0.2365 REMARK 3 18 1.8000 - 1.7700 1.00 2628 138 0.2090 0.2339 REMARK 3 19 1.7700 - 1.7400 1.00 2630 139 0.2118 0.2274 REMARK 3 20 1.7400 - 1.7100 1.00 2636 138 0.2195 0.2531 REMARK 3 21 1.7100 - 1.6800 1.00 2632 138 0.2325 0.2475 REMARK 3 22 1.6800 - 1.6600 1.00 2622 138 0.2460 0.2898 REMARK 3 23 1.6600 - 1.6300 1.00 2605 138 0.2524 0.2815 REMARK 3 24 1.6300 - 1.6100 1.00 2674 140 0.2506 0.2897 REMARK 3 25 1.6100 - 1.5900 1.00 2552 135 0.2734 0.2860 REMARK 3 26 1.5900 - 1.5700 1.00 2651 139 0.2747 0.2778 REMARK 3 27 1.5700 - 1.5500 1.00 2637 139 0.2957 0.3460 REMARK 3 28 1.5500 - 1.5300 1.00 2619 138 0.3103 0.3107 REMARK 3 29 1.5300 - 1.5100 0.98 2591 137 0.3541 0.3966 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) : 0.190 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.230 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 : 0.008 3449 REMARK 3 ANGLE : 1.372 4703 REMARK 3 CHIRALITY : 0.072 535 REMARK 3 PLANARITY : 0.008 597 REMARK 3 DIHEDRAL : 18.386 1195 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 9KAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 01-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300053144. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JUN-24 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.999 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 : 81110 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510 REMARK 200 RESOLUTION RANGE LOW (A) : 29.160 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.40 REMARK 200 R MERGE (I) : 0.06542 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.6700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.49 M SODIUM PHOSPHATE MONOBASIC REMARK 280 MONOHYDRATE, 0.91 M POTASSIUM PHOSPHATE DIBASIC, PH 6.8, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 37.53850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.80200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.82950 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.80200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.53850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.82950 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: 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 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 ARG A 2 REMARK 465 ALA A 3 REMARK 465 TRP A 4 REMARK 465 ILE A 5 REMARK 465 PHE A 6 REMARK 465 PHE A 7 REMARK 465 LEU A 8 REMARK 465 LEU A 9 REMARK 465 CYS A 10 REMARK 465 LEU A 11 REMARK 465 ALA A 12 REMARK 465 GLY A 13 REMARK 465 ARG A 14 REMARK 465 ALA A 15 REMARK 465 LEU A 16 REMARK 465 ALA A 17 REMARK 465 GLN A 18 REMARK 465 VAL A 19 REMARK 465 GLY A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 GLY A 132 REMARK 465 SER A 133 REMARK 465 GLY A 134 REMARK 465 GLY A 135 REMARK 465 GLY A 136 REMARK 465 GLY A 137 REMARK 465 SER A 138 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 MET B 1 REMARK 465 ARG B 2 REMARK 465 ALA B 3 REMARK 465 TRP B 4 REMARK 465 ILE B 5 REMARK 465 PHE B 6 REMARK 465 PHE B 7 REMARK 465 LEU B 8 REMARK 465 LEU B 9 REMARK 465 CYS B 10 REMARK 465 LEU B 11 REMARK 465 ALA B 12 REMARK 465 GLY B 13 REMARK 465 ARG B 14 REMARK 465 ALA B 15 REMARK 465 LEU B 16 REMARK 465 ALA B 17 REMARK 465 GLN B 18 REMARK 465 GLY B 129 REMARK 465 GLY B 130 REMARK 465 GLY B 131 REMARK 465 GLY B 132 REMARK 465 SER B 133 REMARK 465 GLY B 134 REMARK 465 GLY B 135 REMARK 465 GLY B 136 REMARK 465 GLY B 137 REMARK 465 SER B 138 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 253 REMARK 465 SER B 254 REMARK 465 HIS B 255 REMARK 465 HIS B 256 REMARK 465 HIS B 257 REMARK 465 HIS B 258 REMARK 465 HIS B 259 REMARK 465 HIS B 260 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 496 O HOH B 533 1.83 REMARK 500 O HOH B 490 O HOH B 503 1.92 REMARK 500 O HOH A 417 O HOH A 490 1.96 REMARK 500 OD1 ASN A 179 O HOH A 301 1.97 REMARK 500 O HOH B 467 O HOH B 477 2.01 REMARK 500 O PRO A 185 O HOH A 302 2.03 REMARK 500 O HOH B 311 O HOH B 316 2.03 REMARK 500 O HOH A 479 O HOH A 513 2.04 REMARK 500 O HOH B 467 O HOH B 471 2.09 REMARK 500 O HOH B 353 O HOH B 368 2.12 REMARK 500 O HOH A 455 O HOH A 504 2.13 REMARK 500 O HOH A 459 O HOH A 538 2.19 REMARK 500 O HOH A 449 O HOH B 497 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 B 451 O HOH B 491 2455 2.04 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 LYS B 60 CE LYS B 60 NZ 0.213 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLN A 144 N - CA - C ANGL. DEV. = -19.8 DEGREES REMARK 500 LYS B 60 CD - CE - NZ ANGL. DEV. = -18.4 DEGREES REMARK 500 LYS B 184 C - N - CA ANGL. DEV. = 26.4 DEGREES 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 SER A 32 -4.95 77.76 REMARK 500 ASN A 115 -114.97 59.30 REMARK 500 THR A 196 -49.50 70.79 REMARK 500 ASN A 197 15.24 -143.50 REMARK 500 SER A 238 -47.23 71.09 REMARK 500 ASN A 239 17.64 -148.91 REMARK 500 SER B 32 -6.91 80.66 REMARK 500 ASN B 115 -116.41 59.07 REMARK 500 HIS B 187 31.50 -144.83 REMARK 500 THR B 196 -48.56 71.33 REMARK 500 ASN B 197 15.16 -143.85 REMARK 500 SER B 238 -44.62 68.87 REMARK 500 ASN B 239 16.40 -145.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ASN A 179 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9KAT A 1 260 PDB 9KAT 9KAT 1 260 DBREF 9KAT B 1 260 PDB 9KAT 9KAT 1 260 SEQRES 1 A 260 MET ARG ALA TRP ILE PHE PHE LEU LEU CYS LEU ALA GLY SEQRES 2 A 260 ARG ALA LEU ALA GLN VAL GLN LEU LYS GLU SER GLY PRO SEQRES 3 A 260 GLY LEU VAL ALA PRO SER GLN SER LEU SER ILE THR CYS SEQRES 4 A 260 THR VAL SER GLY LEU SER LEU PRO GLY TYR GLY VAL ASN SEQRES 5 A 260 TRP VAL ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP LEU SEQRES 6 A 260 GLY MET ILE TRP ASP ASP GLY ARG THR ASP TYR ASN SER SEQRES 7 A 260 ALA LEU LYS SER ARG LEU SER ILE SER LYS ASP ASN SER SEQRES 8 A 260 LYS SER GLN VAL PHE LEU LYS MET ASN SER LEU GLN THR SEQRES 9 A 260 ASP ASP THR ALA ARG TYR TYR CYS VAL ARG ASN VAL TYR SEQRES 10 A 260 TRP GLY GLN GLY THR LEU VAL THR VAL SER ALA GLY GLY SEQRES 11 A 260 GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 12 A 260 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 13 A 260 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 14 A 260 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN SEQRES 15 A 260 GLU LYS PRO ASP HIS LEU PHE SER GLY LEU ILE SER GLY SEQRES 16 A 260 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER SEQRES 17 A 260 GLY SER LEU ILE GLY ASP THR ALA ALA LEU THR ILE THR SEQRES 18 A 260 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 19 A 260 LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY GLY SER SEQRES 20 A 260 LYS LEU THR VAL LEU GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 260 MET ARG ALA TRP ILE PHE PHE LEU LEU CYS LEU ALA GLY SEQRES 2 B 260 ARG ALA LEU ALA GLN VAL GLN LEU LYS GLU SER GLY PRO SEQRES 3 B 260 GLY LEU VAL ALA PRO SER GLN SER LEU SER ILE THR CYS SEQRES 4 B 260 THR VAL SER GLY LEU SER LEU PRO GLY TYR GLY VAL ASN SEQRES 5 B 260 TRP VAL ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP LEU SEQRES 6 B 260 GLY MET ILE TRP ASP ASP GLY ARG THR ASP TYR ASN SER SEQRES 7 B 260 ALA LEU LYS SER ARG LEU SER ILE SER LYS ASP ASN SER SEQRES 8 B 260 LYS SER GLN VAL PHE LEU LYS MET ASN SER LEU GLN THR SEQRES 9 B 260 ASP ASP THR ALA ARG TYR TYR CYS VAL ARG ASN VAL TYR SEQRES 10 B 260 TRP GLY GLN GLY THR LEU VAL THR VAL SER ALA GLY GLY SEQRES 11 B 260 GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 12 B 260 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 13 B 260 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 14 B 260 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN SEQRES 15 B 260 GLU LYS PRO ASP HIS LEU PHE SER GLY LEU ILE SER GLY SEQRES 16 B 260 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER SEQRES 17 B 260 GLY SER LEU ILE GLY ASP THR ALA ALA LEU THR ILE THR SEQRES 18 B 260 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 19 B 260 LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY GLY SER SEQRES 20 B 260 LYS LEU THR VAL LEU GLY SER HIS HIS HIS HIS HIS HIS FORMUL 3 HOH *496(H2 O) HELIX 1 AA1 LEU A 80 SER A 82 5 3 HELIX 2 AA2 GLN A 103 THR A 107 5 5 HELIX 3 AA3 THR A 173 TYR A 177 5 5 HELIX 4 AA4 GLN A 224 GLU A 228 5 5 HELIX 5 AA5 SER B 78 LYS B 81 5 4 HELIX 6 AA6 GLN B 103 THR B 107 5 5 HELIX 7 AA7 THR B 173 TYR B 177 5 5 HELIX 8 AA8 GLN B 224 GLU B 228 5 5 SHEET 1 AA1 4 LEU A 21 SER A 24 0 SHEET 2 AA1 4 LEU A 35 VAL A 41 -1 O THR A 40 N LYS A 22 SHEET 3 AA1 4 GLN A 94 MET A 99 -1 O VAL A 95 N CYS A 39 SHEET 4 AA1 4 LEU A 84 ASP A 89 -1 N SER A 87 O PHE A 96 SHEET 1 AA2 6 LEU A 28 VAL A 29 0 SHEET 2 AA2 6 THR A 122 VAL A 126 1 O THR A 125 N VAL A 29 SHEET 3 AA2 6 ALA A 108 ARG A 114 -1 N ALA A 108 O VAL A 124 SHEET 4 AA2 6 VAL A 51 GLN A 56 -1 N ASN A 52 O VAL A 113 SHEET 5 AA2 6 GLU A 63 ILE A 68 -1 O GLU A 63 N ARG A 55 SHEET 6 AA2 6 THR A 74 TYR A 76 -1 O ASP A 75 N MET A 67 SHEET 1 AA3 4 LEU A 28 VAL A 29 0 SHEET 2 AA3 4 THR A 122 VAL A 126 1 O THR A 125 N VAL A 29 SHEET 3 AA3 4 ALA A 108 ARG A 114 -1 N ALA A 108 O VAL A 124 SHEET 4 AA3 4 TYR A 117 TRP A 118 -1 O TYR A 117 N ARG A 114 SHEET 1 AA4 4 VAL A 147 GLN A 149 0 SHEET 2 AA4 4 VAL A 161 SER A 167 -1 O ARG A 166 N THR A 148 SHEET 3 AA4 4 THR A 215 ILE A 220 -1 O ILE A 220 N VAL A 161 SHEET 4 AA4 4 PHE A 207 ILE A 212 -1 N SER A 210 O ALA A 217 SHEET 1 AA5 6 ALA A 152 THR A 155 0 SHEET 2 AA5 6 SER A 247 VAL A 251 1 O THR A 250 N LEU A 153 SHEET 3 AA5 6 ALA A 229 TRP A 236 -1 N ALA A 229 O LEU A 249 SHEET 4 AA5 6 ASN A 179 LYS A 184 -1 N GLU A 183 O ILE A 230 SHEET 5 AA5 6 LEU A 188 SER A 194 -1 O LEU A 192 N TRP A 180 SHEET 6 AA5 6 ASN A 198 ARG A 199 -1 O ASN A 198 N SER A 194 SHEET 1 AA6 4 ALA A 152 THR A 155 0 SHEET 2 AA6 4 SER A 247 VAL A 251 1 O THR A 250 N LEU A 153 SHEET 3 AA6 4 ALA A 229 TRP A 236 -1 N ALA A 229 O LEU A 249 SHEET 4 AA6 4 TRP A 241 PHE A 243 -1 O VAL A 242 N LEU A 235 SHEET 1 AA7 4 GLN B 20 SER B 24 0 SHEET 2 AA7 4 LEU B 35 SER B 42 -1 O THR B 40 N LYS B 22 SHEET 3 AA7 4 GLN B 94 MET B 99 -1 O VAL B 95 N CYS B 39 SHEET 4 AA7 4 LEU B 84 ASP B 89 -1 N SER B 87 O PHE B 96 SHEET 1 AA8 6 LEU B 28 VAL B 29 0 SHEET 2 AA8 6 THR B 122 VAL B 126 1 O THR B 125 N VAL B 29 SHEET 3 AA8 6 ALA B 108 ARG B 114 -1 N ALA B 108 O VAL B 124 SHEET 4 AA8 6 GLY B 50 GLN B 56 -1 N VAL B 54 O TYR B 111 SHEET 5 AA8 6 GLU B 63 TRP B 69 -1 O GLY B 66 N TRP B 53 SHEET 6 AA8 6 THR B 74 TYR B 76 -1 O ASP B 75 N MET B 67 SHEET 1 AA9 4 LEU B 28 VAL B 29 0 SHEET 2 AA9 4 THR B 122 VAL B 126 1 O THR B 125 N VAL B 29 SHEET 3 AA9 4 ALA B 108 ARG B 114 -1 N ALA B 108 O VAL B 124 SHEET 4 AA9 4 TYR B 117 TRP B 118 -1 O TYR B 117 N ARG B 114 SHEET 1 AB1 4 VAL B 147 GLN B 149 0 SHEET 2 AB1 4 THR B 160 SER B 167 -1 O ARG B 166 N THR B 148 SHEET 3 AB1 4 THR B 215 THR B 221 -1 O ILE B 220 N VAL B 161 SHEET 4 AB1 4 PHE B 207 ILE B 212 -1 N SER B 208 O THR B 219 SHEET 1 AB2 6 ALA B 152 THR B 155 0 SHEET 2 AB2 6 SER B 247 VAL B 251 1 O THR B 250 N LEU B 153 SHEET 3 AB2 6 ALA B 229 TRP B 236 -1 N ALA B 229 O LEU B 249 SHEET 4 AB2 6 ASN B 179 LYS B 184 -1 N GLU B 183 O ILE B 230 SHEET 5 AB2 6 LEU B 188 SER B 194 -1 O LEU B 192 N TRP B 180 SHEET 6 AB2 6 ASN B 198 ARG B 199 -1 O ASN B 198 N SER B 194 SHEET 1 AB3 4 ALA B 152 THR B 155 0 SHEET 2 AB3 4 SER B 247 VAL B 251 1 O THR B 250 N LEU B 153 SHEET 3 AB3 4 ALA B 229 TRP B 236 -1 N ALA B 229 O LEU B 249 SHEET 4 AB3 4 TRP B 241 PHE B 243 -1 O VAL B 242 N LEU B 235 SSBOND 1 CYS A 39 CYS A 112 1555 1555 2.07 SSBOND 2 CYS A 165 CYS A 233 1555 1555 2.03 SSBOND 3 CYS B 39 CYS B 112 1555 1555 2.05 SSBOND 4 CYS B 165 CYS B 233 1555 1555 2.06 CISPEP 1 PRO B 185 ASP B 186 0 -9.93 CRYST1 75.077 79.659 85.604 90.00 90.00 90.00 P 21 21 21 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 0.013320 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012554 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011682 0.00000