HEADER TRANSPORT PROTEIN/IMMUNE SYSTEM 12-DEC-22 8HPK TITLE CRYSTAL STRUCTURE OF THE BACTERIAL OXALATE TRANSPORTER OXLT IN AN TITLE 2 OXALATE-BOUND OCCLUDED FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: OXALATE:FORMATE ANTIPORTER; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: OFA,OXALATE:FORMATE ANTIPORT PROTEIN,OXALATE:FORMATE COMPND 5 EXCHANGE PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB FRAGMENT HEAVY CHEIN; COMPND 9 CHAIN: H; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FAB FRAGMENT LIGHT CHAIN; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: OXALOBACTER FORMIGENES; SOURCE 3 ORGANISM_TAXID: 847; SOURCE 4 GENE: OXLT; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 14 ORGANISM_TAXID: 10090; SOURCE 15 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10090 KEYWDS MAJOR FACILITATOR SUPERFAMILY MEMBRANE PROTEIN TRANSPORTER, TRANSPORT KEYWDS 2 PROTEIN, TRANSPORT PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.SHIMAMURA,T.HIRAI,A.YAMASHITA REVDAT 1 15-FEB-23 8HPK 0 JRNL AUTH T.JAUNET-LAHARY,T.SHIMAMURA JRNL TITL STRUCTURE AND MECHANISM OF OXALATE TRANSPORTER OXLT IN AN JRNL TITL 2 OXALATE-DEGRADING BACTERIUM IN THE GUT MICROBE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.10 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 74.4 REMARK 3 NUMBER OF REFLECTIONS : 20950 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.241 REMARK 3 R VALUE (WORKING SET) : 0.237 REMARK 3 FREE R VALUE : 0.278 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.870 REMARK 3 FREE R VALUE TEST SET COUNT : 1859 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 21.1000 - 6.9800 1.00 2122 207 0.2382 0.2517 REMARK 3 2 6.9700 - 5.5700 1.00 2029 198 0.2435 0.3214 REMARK 3 3 5.5700 - 4.8800 1.00 1999 194 0.2024 0.2482 REMARK 3 4 4.8800 - 4.4300 1.00 1988 193 0.2013 0.2486 REMARK 3 5 4.4300 - 4.1200 1.00 1973 193 0.2193 0.2495 REMARK 3 6 4.1200 - 3.8800 0.94 1839 179 0.2434 0.2877 REMARK 3 7 3.8800 - 3.6800 0.85 1659 161 0.2423 0.2873 REMARK 3 8 3.6800 - 3.5200 0.71 1402 137 0.2607 0.3091 REMARK 3 9 3.5200 - 3.3900 0.62 1195 115 0.2836 0.3255 REMARK 3 10 3.3900 - 3.2700 0.53 1047 102 0.2689 0.3162 REMARK 3 11 3.2700 - 3.1700 0.40 767 76 0.3053 0.3534 REMARK 3 12 3.1700 - 3.0800 0.31 604 59 0.2896 0.3180 REMARK 3 13 3.0800 - 3.0000 0.25 467 45 0.2962 0.3327 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) : 0.363 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.314 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 46.98 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.17 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 : 0.003 6364 REMARK 3 ANGLE : 0.584 8668 REMARK 3 CHIRALITY : 0.042 977 REMARK 3 PLANARITY : 0.005 1090 REMARK 3 DIHEDRAL : 11.441 875 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 191 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.9095 79.3205 7.5590 REMARK 3 T TENSOR REMARK 3 T11: 0.4231 T22: 0.1560 REMARK 3 T33: 0.2959 T12: 0.0920 REMARK 3 T13: 0.2468 T23: 0.0037 REMARK 3 L TENSOR REMARK 3 L11: 0.4264 L22: 0.8373 REMARK 3 L33: 0.1759 L12: -0.3159 REMARK 3 L13: -0.2008 L23: 0.2850 REMARK 3 S TENSOR REMARK 3 S11: 0.1386 S12: 0.1936 S13: 0.0548 REMARK 3 S21: -0.4099 S22: -0.2332 S23: -0.0661 REMARK 3 S31: 0.0971 S32: -0.0081 S33: -0.1250 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 192 THROUGH 405 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.4657 83.4665 24.1168 REMARK 3 T TENSOR REMARK 3 T11: 0.2144 T22: 0.1342 REMARK 3 T33: 0.3519 T12: -0.0310 REMARK 3 T13: 0.1940 T23: -0.1216 REMARK 3 L TENSOR REMARK 3 L11: 0.7710 L22: 0.9080 REMARK 3 L33: 0.6383 L12: -0.7329 REMARK 3 L13: 0.1965 L23: -0.4341 REMARK 3 S TENSOR REMARK 3 S11: 0.0427 S12: -0.0726 S13: 0.4438 REMARK 3 S21: 0.0588 S22: -0.0397 S23: -0.3254 REMARK 3 S31: -0.2101 S32: 0.1473 S33: -0.5030 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.4115 38.2079 12.6770 REMARK 3 T TENSOR REMARK 3 T11: 0.7178 T22: 0.3719 REMARK 3 T33: 0.2621 T12: 0.2516 REMARK 3 T13: -0.0783 T23: -0.0999 REMARK 3 L TENSOR REMARK 3 L11: 1.9380 L22: 3.1385 REMARK 3 L33: 3.5595 L12: 0.9390 REMARK 3 L13: -0.3724 L23: 1.3001 REMARK 3 S TENSOR REMARK 3 S11: 0.2403 S12: 0.1299 S13: 0.0089 REMARK 3 S21: -0.0855 S22: -0.1976 S23: 0.3046 REMARK 3 S31: 0.0646 S32: -0.2497 S33: 0.1141 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 68 THROUGH 139 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.2391 27.9882 18.1353 REMARK 3 T TENSOR REMARK 3 T11: 0.7771 T22: 0.4142 REMARK 3 T33: 0.2597 T12: 0.1199 REMARK 3 T13: -0.1479 T23: -0.0415 REMARK 3 L TENSOR REMARK 3 L11: 1.0408 L22: 0.2287 REMARK 3 L33: 1.5054 L12: -0.2942 REMARK 3 L13: 0.0364 L23: -0.4803 REMARK 3 S TENSOR REMARK 3 S11: 0.3294 S12: 0.0638 S13: -0.4176 REMARK 3 S21: -0.4002 S22: -0.0489 S23: 0.0168 REMARK 3 S31: 0.8392 S32: 0.1615 S33: 0.0299 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 140 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.6415 9.3196 31.4899 REMARK 3 T TENSOR REMARK 3 T11: 0.9864 T22: 0.3060 REMARK 3 T33: 0.7166 T12: -0.0681 REMARK 3 T13: -0.2098 T23: 0.0138 REMARK 3 L TENSOR REMARK 3 L11: 2.9363 L22: 3.8105 REMARK 3 L33: 2.6163 L12: -1.6686 REMARK 3 L13: 0.8414 L23: 2.1297 REMARK 3 S TENSOR REMARK 3 S11: 0.1594 S12: -0.0309 S13: -0.6866 REMARK 3 S21: -0.5748 S22: -0.0514 S23: 0.8324 REMARK 3 S31: 0.2351 S32: -0.4085 S33: -0.0415 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.0887 45.1075 31.7763 REMARK 3 T TENSOR REMARK 3 T11: 0.1809 T22: 0.1782 REMARK 3 T33: 0.1013 T12: 0.1370 REMARK 3 T13: -0.0274 T23: -0.0697 REMARK 3 L TENSOR REMARK 3 L11: 1.1692 L22: 2.0090 REMARK 3 L33: 0.5313 L12: 0.1988 REMARK 3 L13: -0.4232 L23: 0.3637 REMARK 3 S TENSOR REMARK 3 S11: 0.0349 S12: -0.1771 S13: 0.0116 REMARK 3 S21: 0.1942 S22: 0.0707 S23: -0.2662 REMARK 3 S31: 0.1674 S32: 0.2424 S33: 0.0211 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 77 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.9460 27.6476 32.2861 REMARK 3 T TENSOR REMARK 3 T11: 0.3800 T22: 0.2074 REMARK 3 T33: 0.2753 T12: 0.1202 REMARK 3 T13: 0.1266 T23: 0.0093 REMARK 3 L TENSOR REMARK 3 L11: 0.4915 L22: 1.6538 REMARK 3 L33: 0.8499 L12: -0.7677 REMARK 3 L13: 0.1610 L23: -0.0081 REMARK 3 S TENSOR REMARK 3 S11: -0.0168 S12: -0.0527 S13: -0.2354 REMARK 3 S21: 0.2815 S22: 0.0628 S23: 0.3497 REMARK 3 S31: 0.3669 S32: 0.0292 S33: 0.1701 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 130 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.3356 10.9220 36.7552 REMARK 3 T TENSOR REMARK 3 T11: 0.7449 T22: 0.3275 REMARK 3 T33: 0.5824 T12: 0.1475 REMARK 3 T13: 0.2089 T23: 0.1016 REMARK 3 L TENSOR REMARK 3 L11: 5.0286 L22: 3.3411 REMARK 3 L33: 5.2074 L12: -1.3149 REMARK 3 L13: -0.0633 L23: 3.8024 REMARK 3 S TENSOR REMARK 3 S11: 0.1874 S12: 0.1729 S13: -0.0434 REMARK 3 S21: -1.0120 S22: 0.2367 S23: -0.4126 REMARK 3 S31: 0.3386 S32: 0.6168 S33: -0.3784 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 152 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.6642 5.6950 35.3133 REMARK 3 T TENSOR REMARK 3 T11: 0.7815 T22: 0.4042 REMARK 3 T33: 0.6010 T12: 0.2375 REMARK 3 T13: 0.1819 T23: 0.1106 REMARK 3 L TENSOR REMARK 3 L11: 2.7522 L22: 5.6660 REMARK 3 L33: 0.6083 L12: -0.1789 REMARK 3 L13: 0.6543 L23: 1.5554 REMARK 3 S TENSOR REMARK 3 S11: 0.1163 S12: 0.3300 S13: -0.5250 REMARK 3 S21: -0.6910 S22: -0.0747 S23: -0.7829 REMARK 3 S31: 0.3715 S32: 0.2654 S33: -0.0764 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 8HPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-22. REMARK 100 THE DEPOSITION ID IS D_1300034024. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-JUL-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22609 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 46.600 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9 REMARK 200 DATA REDUNDANCY : 99.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.94 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: NULL REMARK 200 STARTING MODEL: 1PW4, 1XF4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.83 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, PH 5.5, 0.05 M REMARK 280 NACL, 26% (V/V) PEG 400, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 57.47500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 116.59500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.47500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 116.59500 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 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 ASN A 2 REMARK 465 ASN A 3 REMARK 465 PRO A 4 REMARK 465 GLN A 5 REMARK 465 THR A 6 REMARK 465 GLY A 7 REMARK 465 GLN A 8 REMARK 465 SER A 9 REMARK 465 THR A 10 REMARK 465 GLN A 198 REMARK 465 GLY A 199 REMARK 465 ALA A 200 REMARK 465 LYS A 201 REMARK 465 LYS A 202 REMARK 465 LYS A 406 REMARK 465 MET A 407 REMARK 465 VAL A 408 REMARK 465 LYS A 409 REMARK 465 LEU A 410 REMARK 465 SER A 411 REMARK 465 PRO A 412 REMARK 465 GLU A 413 REMARK 465 GLU A 414 REMARK 465 LYS A 415 REMARK 465 ALA A 416 REMARK 465 VAL A 417 REMARK 465 HIS A 418 REMARK 465 HIS A 419 REMARK 465 HIS A 420 REMARK 465 HIS A 421 REMARK 465 HIS A 422 REMARK 465 HIS A 423 REMARK 465 HIS A 424 REMARK 465 HIS A 425 REMARK 465 HIS A 426 REMARK 465 HIS A 427 REMARK 465 GLU H 1 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 SER H 163 REMARK 465 LEU H 164 REMARK 465 SER H 165 REMARK 465 GLY H 219 REMARK 465 PRO H 220 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 LEU H 179 CG CD1 CD2 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 PHE H 29 57.08 -95.18 REMARK 500 ILE H 48 -61.48 -97.15 REMARK 500 ARG H 74 -9.65 76.13 REMARK 500 THR L 52 -12.56 73.38 REMARK 500 SER L 53 -35.85 -130.09 REMARK 500 REMARK 500 REMARK: NULL DBREF 8HPK A 1 418 UNP Q51330 OXLT_OXAFO 1 418 DBREF 8HPK H 1 220 PDB 8HPK 8HPK 1 220 DBREF 8HPK L 1 215 PDB 8HPK 8HPK 1 215 SEQADV 8HPK HIS A 419 UNP Q51330 EXPRESSION TAG SEQADV 8HPK HIS A 420 UNP Q51330 EXPRESSION TAG SEQADV 8HPK HIS A 421 UNP Q51330 EXPRESSION TAG SEQADV 8HPK HIS A 422 UNP Q51330 EXPRESSION TAG SEQADV 8HPK HIS A 423 UNP Q51330 EXPRESSION TAG SEQADV 8HPK HIS A 424 UNP Q51330 EXPRESSION TAG SEQADV 8HPK HIS A 425 UNP Q51330 EXPRESSION TAG SEQADV 8HPK HIS A 426 UNP Q51330 EXPRESSION TAG SEQADV 8HPK HIS A 427 UNP Q51330 EXPRESSION TAG SEQRES 1 A 427 MET ASN ASN PRO GLN THR GLY GLN SER THR GLY LEU LEU SEQRES 2 A 427 GLY ASN ARG TRP PHE TYR LEU VAL LEU ALA VAL LEU LEU SEQRES 3 A 427 MET CYS MET ILE SER GLY VAL GLN TYR SER TRP THR LEU SEQRES 4 A 427 TYR ALA ASN PRO VAL LYS ASP ASN LEU GLY VAL SER LEU SEQRES 5 A 427 ALA ALA VAL GLN THR ALA PHE THR LEU SER GLN VAL ILE SEQRES 6 A 427 GLN ALA GLY SER GLN PRO GLY GLY GLY TYR PHE VAL ASP SEQRES 7 A 427 LYS PHE GLY PRO ARG ILE PRO LEU MET PHE GLY GLY ALA SEQRES 8 A 427 MET VAL LEU ALA GLY TRP THR PHE MET GLY MET VAL ASP SEQRES 9 A 427 SER VAL PRO ALA LEU TYR ALA LEU TYR THR LEU ALA GLY SEQRES 10 A 427 ALA GLY VAL GLY ILE VAL TYR GLY ILE ALA MET ASN THR SEQRES 11 A 427 ALA ASN ARG TRP PHE PRO ASP LYS ARG GLY LEU ALA SER SEQRES 12 A 427 GLY PHE THR ALA ALA GLY TYR GLY LEU GLY VAL LEU PRO SEQRES 13 A 427 PHE LEU PRO LEU ILE SER SER VAL LEU LYS VAL GLU GLY SEQRES 14 A 427 VAL GLY ALA ALA PHE MET TYR THR GLY LEU ILE MET GLY SEQRES 15 A 427 ILE LEU ILE ILE LEU ILE ALA PHE VAL ILE ARG PHE PRO SEQRES 16 A 427 GLY GLN GLN GLY ALA LYS LYS GLN ILE VAL VAL THR ASP SEQRES 17 A 427 LYS ASP PHE ASN SER GLY GLU MET LEU ARG THR PRO GLN SEQRES 18 A 427 PHE TRP VAL LEU TRP THR ALA PHE PHE SER VAL ASN PHE SEQRES 19 A 427 GLY GLY LEU LEU LEU VAL ALA ASN SER VAL PRO TYR GLY SEQRES 20 A 427 ARG SER LEU GLY LEU ALA ALA GLY VAL LEU THR ILE GLY SEQRES 21 A 427 VAL SER ILE GLN ASN LEU PHE ASN GLY GLY CYS ARG PRO SEQRES 22 A 427 PHE TRP GLY PHE VAL SER ASP LYS ILE GLY ARG TYR LYS SEQRES 23 A 427 THR MET SER VAL VAL PHE GLY ILE ASN ALA VAL VAL LEU SEQRES 24 A 427 ALA LEU PHE PRO THR ILE ALA ALA LEU GLY ASP VAL ALA SEQRES 25 A 427 PHE ILE ALA MET LEU ALA ILE ALA PHE PHE THR TRP GLY SEQRES 26 A 427 GLY SER TYR ALA LEU PHE PRO SER THR ASN SER ASP ILE SEQRES 27 A 427 PHE GLY THR ALA TYR SER ALA ARG ASN TYR GLY PHE PHE SEQRES 28 A 427 TRP ALA ALA LYS ALA THR ALA SER ILE PHE GLY GLY GLY SEQRES 29 A 427 LEU GLY ALA ALA ILE ALA THR ASN PHE GLY TRP ASN THR SEQRES 30 A 427 ALA PHE LEU ILE THR ALA ILE THR SER PHE ILE ALA PHE SEQRES 31 A 427 ALA LEU ALA THR PHE VAL ILE PRO ARG MET GLY ARG PRO SEQRES 32 A 427 VAL LYS LYS MET VAL LYS LEU SER PRO GLU GLU LYS ALA SEQRES 33 A 427 VAL HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 H 220 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 220 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER VAL SEQRES 3 H 220 ASN SER PHE THR GLY TYR PHE VAL ASN TRP VAL LYS GLN SEQRES 4 H 220 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ARG VAL HIS SEQRES 5 H 220 PRO TYR ASN GLY ASN THR PHE TYR ASN GLN LYS PHE LYS SEQRES 6 H 220 GLY ARG VAL THR LEU THR VAL ASP ARG SER SER THR THR SEQRES 7 H 220 ALA HIS MET GLU LEU LEU SER LEU THR SER GLU ASP SER SEQRES 8 H 220 ALA VAL TYR TYR CYS GLY ARG ARG ASP ASP TYR ASP THR SEQRES 9 H 220 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SEQRES 10 H 220 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 H 220 PRO GLY CYS GLY ASP THR THR GLY SER SER VAL THR LEU SEQRES 12 H 220 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER VAL THR SEQRES 13 H 220 VAL THR TRP ASN SER GLY SER LEU SER SER SER VAL HIS SEQRES 14 H 220 THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR THR MET SEQRES 15 H 220 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 H 220 GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA SER SER SEQRES 17 H 220 THR THR VAL ASP LYS LYS LEU GLU PRO SER GLY PRO SEQRES 1 L 215 ASP ILE VAL MET THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 L 215 SER LEU GLY GLU ARG VAL THR MET THR CYS THR ALA SER SEQRES 3 L 215 SER SER VAL THR SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 L 215 ARG PRO GLY SER SER PRO LYS LEU TRP ILE TYR SER THR SEQRES 5 L 215 SER ASN LEU ALA SER GLY VAL PRO GLY ARG PHE SER GLY SEQRES 6 L 215 ARG GLY SER GLY THR SER TYR SER LEU THR ILE SER SER SEQRES 7 L 215 MET GLU ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN SEQRES 8 L 215 TYR HIS ARG SER PRO PRO THR PHE GLY GLY GLY THR LYS SEQRES 9 L 215 LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER SEQRES 10 L 215 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY SEQRES 11 L 215 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS SEQRES 12 L 215 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG SEQRES 13 L 215 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU SEQRES 15 L 215 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS SEQRES 16 L 215 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SEQRES 17 L 215 SER PHE ASN ARG ASN GLU CYS HET OXL A 501 6 HETNAM OXL OXALATE ION FORMUL 4 OXL C2 O4 2- HELIX 1 AA1 ASN A 15 SER A 36 1 22 HELIX 2 AA2 SER A 36 GLY A 49 1 14 HELIX 3 AA3 SER A 51 GLY A 81 1 31 HELIX 4 AA4 PRO A 82 PHE A 99 1 18 HELIX 5 AA5 MET A 100 MET A 102 5 3 HELIX 6 AA6 SER A 105 PHE A 135 1 31 HELIX 7 AA7 LYS A 138 GLY A 153 1 16 HELIX 8 AA8 GLY A 153 GLU A 168 1 16 HELIX 9 AA9 GLY A 169 ILE A 192 1 24 HELIX 10 AB1 ASN A 212 THR A 219 1 8 HELIX 11 AB2 THR A 219 GLY A 251 1 33 HELIX 12 AB3 ALA A 253 ILE A 282 1 30 HELIX 13 AB4 GLY A 283 ALA A 307 1 25 HELIX 14 AB5 GLY A 309 PHE A 339 1 31 HELIX 15 AB6 TYR A 343 GLY A 363 1 21 HELIX 16 AB7 GLY A 363 GLY A 374 1 12 HELIX 17 AB8 GLY A 374 PHE A 395 1 22 HELIX 18 AB9 VAL A 396 MET A 400 5 5 HELIX 19 AC1 THR H 87 SER H 91 5 5 HELIX 20 AC2 THR L 30 SER L 32 5 3 HELIX 21 AC3 GLU L 80 ALA L 84 5 5 HELIX 22 AC4 SER L 122 GLY L 129 1 8 HELIX 23 AC5 LYS L 184 ARG L 189 1 6 SHEET 1 AA1 4 GLN H 5 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 LYS H 23 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 4 AA1 4 VAL H 68 VAL H 72 -1 N THR H 71 O HIS H 80 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 112 VAL H 116 1 O SER H 113 N GLU H 10 SHEET 3 AA2 6 ALA H 92 ARG H 99 -1 N ALA H 92 O VAL H 114 SHEET 4 AA2 6 PHE H 33 GLN H 39 -1 N PHE H 33 O ARG H 99 SHEET 5 AA2 6 LEU H 45 VAL H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O PHE H 59 N ARG H 50 SHEET 1 AA3 4 GLU H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 112 VAL H 116 1 O SER H 113 N GLU H 10 SHEET 3 AA3 4 ALA H 92 ARG H 99 -1 N ALA H 92 O VAL H 114 SHEET 4 AA3 4 MET H 105 TRP H 108 -1 O TYR H 107 N ARG H 98 SHEET 1 AA4 4 SER H 125 LEU H 129 0 SHEET 2 AA4 4 SER H 140 TYR H 150 -1 O LEU H 146 N TYR H 127 SHEET 3 AA4 4 LEU H 179 PRO H 189 -1 O MET H 182 N VAL H 147 SHEET 4 AA4 4 VAL H 168 THR H 170 -1 N HIS H 169 O SER H 185 SHEET 1 AA5 4 SER H 125 LEU H 129 0 SHEET 2 AA5 4 SER H 140 TYR H 150 -1 O LEU H 146 N TYR H 127 SHEET 3 AA5 4 LEU H 179 PRO H 189 -1 O MET H 182 N VAL H 147 SHEET 4 AA5 4 LEU H 174 GLN H 176 -1 N GLN H 176 O LEU H 179 SHEET 1 AA6 3 THR H 156 TRP H 159 0 SHEET 2 AA6 3 THR H 199 HIS H 204 -1 O ALA H 203 N THR H 156 SHEET 3 AA6 3 THR H 209 LYS H 214 -1 O VAL H 211 N VAL H 202 SHEET 1 AA7 3 MET L 4 SER L 7 0 SHEET 2 AA7 3 VAL L 19 VAL L 29 -1 O THR L 24 N THR L 5 SHEET 3 AA7 3 PHE L 63 ILE L 76 -1 O TYR L 72 N CYS L 23 SHEET 1 AA8 6 ILE L 10 SER L 14 0 SHEET 2 AA8 6 THR L 103 LYS L 108 1 O LYS L 104 N MET L 11 SHEET 3 AA8 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 6 LEU L 34 GLN L 39 -1 N TYR L 37 O TYR L 88 SHEET 5 AA8 6 PRO L 45 TYR L 50 -1 O ILE L 49 N TRP L 36 SHEET 6 AA8 6 ASN L 54 LEU L 55 -1 O ASN L 54 N TYR L 50 SHEET 1 AA9 4 ILE L 10 SER L 14 0 SHEET 2 AA9 4 THR L 103 LYS L 108 1 O LYS L 104 N MET L 11 SHEET 3 AA9 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA9 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AB1 4 THR L 115 PHE L 119 0 SHEET 2 AB1 4 GLY L 130 PHE L 140 -1 O PHE L 136 N SER L 117 SHEET 3 AB1 4 TYR L 174 THR L 183 -1 O LEU L 182 N ALA L 131 SHEET 4 AB1 4 VAL L 160 TRP L 164 -1 N LEU L 161 O THR L 179 SHEET 1 AB2 4 SER L 154 ARG L 156 0 SHEET 2 AB2 4 ASN L 146 ILE L 151 -1 N ILE L 151 O SER L 154 SHEET 3 AB2 4 SER L 192 THR L 198 -1 O THR L 194 N LYS L 150 SHEET 4 AB2 4 ILE L 206 ASN L 211 -1 O LYS L 208 N CYS L 195 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 2 CYS H 133 CYS L 215 1555 1555 2.03 SSBOND 3 CYS H 145 CYS H 200 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 89 1555 1555 2.03 SSBOND 5 CYS L 135 CYS L 195 1555 1555 2.03 CISPEP 1 PHE H 151 PRO H 152 0 2.86 CISPEP 2 TRP H 193 PRO H 194 0 -4.73 CISPEP 3 SER L 7 PRO L 8 0 -4.94 CISPEP 4 SER L 95 PRO L 96 0 -1.20 CISPEP 5 TYR L 141 PRO L 142 0 -0.75 CRYST1 114.950 233.190 50.770 90.00 90.00 90.00 P 21 21 2 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 0.008699 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004288 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019697 0.00000