HEADER IMMUNE SYSTEM 25-NOV-22 8FA7 TITLE CRYSTAL STRUCTURE OF KY15.11 FAB IN COMPLEX WITH CIRCUMSPOROZOITE TITLE 2 PROTEIN KQPA PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: KY15.11 ANTIBODY, HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: KY15.11 ANTIBODY, LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CIRCUMSPOROZOITE PROTEIN KQPA PEPTIDE; COMPND 11 CHAIN: P; COMPND 12 SYNONYM: CS,PFCSP; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM; SOURCE 18 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM; SOURCE 19 ORGANISM_TAXID: 5833 KEYWDS MALARIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR E.THAI,J.P.JULIEN REVDAT 1 01-NOV-23 8FA7 0 JRNL AUTH E.THAI,R.MURUGAN,S.BINTER,C.BURN ASCHNER,K.PRIETO, JRNL AUTH 2 A.KASSARDJIAN,R.W.KANG,A.OBRAZTCOVA,G.COSTA,E.LEVASHINA, JRNL AUTH 3 P.KELLAM,H.WARDEMANN,J.P.JULIEN JRNL TITL MOLECULAR DETERMINANTS OF CROSS-REACTIVITY AND POTENCY BY JRNL TITL 2 VH3-33 ANTIBODIES AGAINST THE PLASMODIUM FALCIPARUM JRNL TITL 3 CIRCUMSPOROZOITE PROTEIN JRNL REF CELL REP 2023 JRNL REFN ESSN 2211-1247 JRNL DOI 10.1016/J.CELREP.2023.113330 REMARK 2 REMARK 2 RESOLUTION. 1.80 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.45 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 45111 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.172 REMARK 3 R VALUE (WORKING SET) : 0.171 REMARK 3 FREE R VALUE : 0.198 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.440 REMARK 3 FREE R VALUE TEST SET COUNT : 2005 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 28.4500 - 4.3300 1.00 3270 157 0.1910 0.1983 REMARK 3 2 4.3300 - 3.4400 1.00 3134 149 0.1487 0.1460 REMARK 3 3 3.4400 - 3.0100 1.00 3106 146 0.1491 0.1973 REMARK 3 4 3.0100 - 2.7300 1.00 3089 143 0.1614 0.1877 REMARK 3 5 2.7300 - 2.5400 1.00 3084 141 0.1713 0.2429 REMARK 3 6 2.5400 - 2.3900 1.00 3067 144 0.1721 0.2179 REMARK 3 7 2.3900 - 2.2700 1.00 3047 145 0.1728 0.2209 REMARK 3 8 2.2700 - 2.1700 1.00 3069 136 0.1598 0.2163 REMARK 3 9 2.1700 - 2.0900 1.00 3036 142 0.1629 0.2064 REMARK 3 10 2.0900 - 2.0100 1.00 3061 137 0.1761 0.2357 REMARK 3 11 2.0100 - 1.9500 1.00 3008 141 0.1857 0.2477 REMARK 3 12 1.9500 - 1.8900 1.00 3051 143 0.2113 0.2602 REMARK 3 13 1.8900 - 1.8500 1.00 3020 145 0.2341 0.2837 REMARK 3 14 1.8500 - 1.8000 1.00 3064 136 0.2701 0.2914 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) : 0.189 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.553 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.14 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.64 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 : 0.014 3675 REMARK 3 ANGLE : 1.191 4987 REMARK 3 CHIRALITY : 0.084 548 REMARK 3 PLANARITY : 0.009 629 REMARK 3 DIHEDRAL : 13.063 1324 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.7803 -38.4308 12.3173 REMARK 3 T TENSOR REMARK 3 T11: 0.1892 T22: 0.1972 REMARK 3 T33: 0.2590 T12: -0.0029 REMARK 3 T13: 0.0181 T23: -0.0205 REMARK 3 L TENSOR REMARK 3 L11: 2.1197 L22: 3.2611 REMARK 3 L33: 4.1336 L12: -0.4790 REMARK 3 L13: -1.1457 L23: 0.5111 REMARK 3 S TENSOR REMARK 3 S11: 0.0456 S12: 0.0829 S13: -0.0081 REMARK 3 S21: 0.0559 S22: -0.0152 S23: 0.1838 REMARK 3 S31: -0.0592 S32: -0.0684 S33: -0.0964 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 114 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.4121 -19.7436 35.8246 REMARK 3 T TENSOR REMARK 3 T11: 0.2168 T22: 0.2931 REMARK 3 T33: 0.2292 T12: -0.0346 REMARK 3 T13: 0.0148 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 5.8971 L22: 5.4239 REMARK 3 L33: 2.3930 L12: -1.8396 REMARK 3 L13: -1.4057 L23: 0.2127 REMARK 3 S TENSOR REMARK 3 S11: -0.1526 S12: 0.1950 S13: 0.0749 REMARK 3 S21: -0.0275 S22: 0.0006 S23: 0.2990 REMARK 3 S31: 0.1142 S32: -0.2418 S33: 0.1073 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 107) REMARK 3 ORIGIN FOR THE GROUP (A): -1.4615 -17.4569 11.0766 REMARK 3 T TENSOR REMARK 3 T11: 0.3416 T22: 0.2300 REMARK 3 T33: 0.3363 T12: -0.0150 REMARK 3 T13: 0.0889 T23: 0.0332 REMARK 3 L TENSOR REMARK 3 L11: 3.0117 L22: 5.1980 REMARK 3 L33: 1.2966 L12: -2.1040 REMARK 3 L13: -0.5895 L23: 0.7221 REMARK 3 S TENSOR REMARK 3 S11: 0.1854 S12: 0.1999 S13: 0.5252 REMARK 3 S21: -0.3770 S22: -0.0278 S23: -0.5788 REMARK 3 S31: -0.3122 S32: 0.0186 S33: -0.1184 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 108 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.3033 -11.3672 41.8245 REMARK 3 T TENSOR REMARK 3 T11: 0.1765 T22: 0.2616 REMARK 3 T33: 0.2793 T12: 0.0211 REMARK 3 T13: 0.0131 T23: -0.0114 REMARK 3 L TENSOR REMARK 3 L11: 1.1655 L22: 2.6792 REMARK 3 L33: 4.0396 L12: 0.6319 REMARK 3 L13: -0.6717 L23: -1.8162 REMARK 3 S TENSOR REMARK 3 S11: 0.0471 S12: -0.1692 S13: 0.1491 REMARK 3 S21: 0.0873 S22: 0.0480 S23: 0.2060 REMARK 3 S31: 0.0908 S32: -0.1067 S33: -0.0940 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 5 THROUGH 15 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.4154 -36.9939 0.9723 REMARK 3 T TENSOR REMARK 3 T11: 0.4580 T22: 0.4124 REMARK 3 T33: 0.3446 T12: -0.0318 REMARK 3 T13: 0.0744 T23: -0.0624 REMARK 3 L TENSOR REMARK 3 L11: 2.4313 L22: 4.3765 REMARK 3 L33: 2.6887 L12: 0.4276 REMARK 3 L13: -1.1773 L23: -3.1361 REMARK 3 S TENSOR REMARK 3 S11: -0.1772 S12: 1.1725 S13: -0.0804 REMARK 3 S21: -1.1071 S22: 0.6583 S23: -0.5922 REMARK 3 S31: -0.0388 S32: 0.7853 S33: -0.6855 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 8FA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-22. REMARK 100 THE DEPOSITION ID IS D_1000270264. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-NOV-20 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) : 1.03323 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45200 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 12.90 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15% GLYCEROL, 25.5% PEG4000, 0.085 M REMARK 280 TRI-SODIUM CITRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293.15K 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 32.17900 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.14950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.07900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.14950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.17900 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.07900 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9130 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P 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 SER H 215 REMARK 465 CYS H 216 REMARK 465 LYS P 1 REMARK 465 GLN P 2 REMARK 465 PRO P 3 REMARK 465 ALA P 4 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 GLN H 3 CG CD OE1 NE2 REMARK 470 GLN H 13 CG CD OE1 NE2 REMARK 470 VAL H 42 CG1 CG2 REMARK 470 SER H 100A OG REMARK 470 SER L 56 OG REMARK 470 LYS L 126 CG CD CE NZ REMARK 470 GLU L 165 CG CD OE1 OE2 REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 CYS L 214 SG REMARK 470 ASP P 5 CG OD1 OD2 REMARK 470 ASN P 15 CG OD1 ND2 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 L 434 O HOH L 499 1.92 REMARK 500 O HOH H 497 O HOH P 706 1.98 REMARK 500 O HOH H 494 O HOH H 500 1.99 REMARK 500 O HOH L 483 O HOH L 490 2.10 REMARK 500 O HOH L 407 O HOH L 469 2.10 REMARK 500 O HOH L 437 O HOH L 487 2.12 REMARK 500 O2 GOL H 302 O HOH H 401 2.18 REMARK 500 O HOH L 451 O HOH L 498 2.19 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 CYS L 194 CB CYS L 194 SG -0.109 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 THR H 100K -144.17 -136.56 REMARK 500 ASP H 144 61.93 65.48 REMARK 500 ASN L 30 -132.15 61.87 REMARK 500 ALA L 51 -39.11 78.59 REMARK 500 ALA L 84 -179.47 -174.16 REMARK 500 TYR L 94 -148.29 55.51 REMARK 500 ASN L 138 72.13 56.20 REMARK 500 ASP L 151 46.04 39.11 REMARK 500 REMARK 500 REMARK: NULL DBREF 8FA7 H 1 216 PDB 8FA7 8FA7 1 216 DBREF 8FA7 L 1 214 PDB 8FA7 8FA7 1 214 DBREF 8FA7 P 1 15 UNP P19597 CSP_PLAFO 95 109 SEQRES 1 H 232 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 232 PRO GLY ARG SER LEU ARG LEU SER CYS GLU ALA SER GLY SEQRES 3 H 232 PHE THR PHE SER ASN PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 232 THR PRO VAL LYS GLY LEU GLU TRP VAL ALA ILE ILE TRP SEQRES 5 H 232 PHE ASP GLY SER TYR LYS TYR TYR THR ASP SER VAL LYS SEQRES 6 H 232 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 232 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 232 ALA VAL TYR TYR CYS ALA ARG ALA ARG LYS GLY GLN ARG SEQRES 9 H 232 SER ASP TYR TYR GLY SER GLU THR SER TYR THR PHE ASP SEQRES 10 H 232 ASN TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 11 H 232 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 H 232 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 H 232 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 H 232 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 H 232 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 H 232 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 H 232 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 H 232 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 213 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 L 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 213 GLN SER ILE ASN GLY TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS PHE LEU ILE TYR LYS ALA SER SEQRES 5 L 213 ILE LEU GLU SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 213 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 213 SER SER TYR TRP THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 L 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS SEQRES 1 P 15 LYS GLN PRO ALA ASP GLY ASN PRO ASP PRO ASN ALA ASN SEQRES 2 P 15 PRO ASN HET GOL H 301 6 HET GOL H 302 6 HET GOL H 303 6 HET GOL H 304 6 HET GOL H 305 6 HET GOL H 306 6 HET GOL L 301 6 HET GOL L 302 6 HET GOL L 303 6 HET GOL L 304 6 HET GOL L 305 6 HET GOL L 306 6 HET GOL L 307 6 HET GOL L 308 6 HET GOL L 309 6 HET GOL P 601 6 HET GOL P 602 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL 17(C3 H8 O3) FORMUL 21 HOH *223(H2 O) HELIX 1 AA1 THR H 28 PHE H 32 5 5 HELIX 2 AA2 ASP H 61 LYS H 64 5 4 HELIX 3 AA3 ARG H 83 THR H 87 5 5 HELIX 4 AA4 SER H 127 LYS H 129 5 3 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 SER H 187 LEU H 189 5 3 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 GLN L 79 PHE L 83 5 5 HELIX 9 AA9 SER L 121 SER L 127 1 7 HELIX 10 AB1 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O GLU H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA2 6 ALA H 88 LYS H 97 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 MET H 34 THR H 40 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLY H 44 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 LYS H 57 TYR H 59 -1 O TYR H 58 N ILE H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA3 4 ALA H 88 LYS H 97 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 TYR H 100J TRP H 103 -1 O THR H 100K N ARG H 96 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 GLU L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 ILE L 53 LEU L 54 -1 O ILE L 53 N TYR L 49 SHEET 1 AA9 4 THR L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA9 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 GLN L 155 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N TRP L 148 O GLN L 155 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O THR L 197 N LYS L 145 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.13 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.08 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.11 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.74 CISPEP 1 PHE H 146 PRO H 147 0 -9.58 CISPEP 2 GLU H 148 PRO H 149 0 -0.35 CISPEP 3 SER L 7 PRO L 8 0 -7.11 CISPEP 4 SER L 7 PRO L 8 0 -6.86 CISPEP 5 TYR L 140 PRO L 141 0 4.80 CRYST1 64.358 84.158 88.299 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015538 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011882 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011325 0.00000