HEADER IMMUNE SYSTEM 07-SEP-17 6AXK TITLE CRYSTAL STRUCTURE OF FAB311 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB311 HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB311 LIGHT CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ACE-ASN-PRO-ASN-ALA-ASN-PRO-ASN-ALA-ASN-PRO-ASN; COMPND 11 CHAIN: E; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM; SOURCE 14 ORGANISM_TAXID: 5833 KEYWDS FAB FRAGMENT, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR D.OYEN,I.A.WILSON REVDAT 1 22-NOV-17 6AXK 0 JRNL AUTH D.OYEN,J.L.TORRES,U.WILLE-REECE,C.OCKENHOUSE,D.EMERLING, JRNL AUTH 2 J.GLANVILLE,W.VOLKMUTH,A.B.WARD,C.R.KING,I.A.WILSON JRNL TITL STRUCTURAL BASIS FOR ANTIBODY RECOGNITION OF THE NANP JRNL TITL 2 REPEATS IN PLASMODIUM FALCIPARUM CIRCUMSPOROZOITE PROTEIN. JRNL REF PROC.NATL.ACAD.SCI.USA 2017 JRNL REFN ESSN 1091-6490 JRNL DOI 10.1073/PNAS.1715812114 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???) 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.52 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 31966 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.205 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020 REMARK 3 FREE R VALUE TEST SET COUNT : 1606 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 46.5311 - 4.6757 0.99 3032 164 0.1758 0.2068 REMARK 3 2 4.6757 - 3.7118 0.99 2872 163 0.1565 0.1996 REMARK 3 3 3.7118 - 3.2427 0.98 2809 155 0.1886 0.2087 REMARK 3 4 3.2427 - 2.9463 0.98 2797 132 0.2216 0.2363 REMARK 3 5 2.9463 - 2.7351 0.99 2799 159 0.2273 0.2546 REMARK 3 6 2.7351 - 2.5739 0.98 2779 145 0.2254 0.2520 REMARK 3 7 2.5739 - 2.4450 0.99 2792 142 0.2346 0.3136 REMARK 3 8 2.4450 - 2.3386 0.97 2745 147 0.2446 0.2701 REMARK 3 9 2.3386 - 2.2485 0.97 2709 143 0.2517 0.3170 REMARK 3 10 2.2485 - 2.1709 0.96 2702 145 0.2687 0.2989 REMARK 3 11 2.1709 - 2.1031 0.83 2324 111 0.3103 0.3664 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.280 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.790 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 : 0.002 3496 REMARK 3 ANGLE : 0.663 4775 REMARK 3 CHIRALITY : 0.044 524 REMARK 3 PLANARITY : 0.004 610 REMARK 3 DIHEDRAL : 18.521 2072 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 2 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.7669 19.7255 -38.2482 REMARK 3 T TENSOR REMARK 3 T11: 0.2227 T22: 0.3077 REMARK 3 T33: 0.3662 T12: -0.0323 REMARK 3 T13: 0.0258 T23: -0.0789 REMARK 3 L TENSOR REMARK 3 L11: 1.8178 L22: 1.8989 REMARK 3 L33: 2.4197 L12: 0.3345 REMARK 3 L13: -0.2877 L23: 0.7224 REMARK 3 S TENSOR REMARK 3 S11: 0.0637 S12: -0.2514 S13: 0.1597 REMARK 3 S21: 0.1189 S22: -0.2226 S23: 0.4649 REMARK 3 S31: 0.1049 S32: -0.4353 S33: 0.1466 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.6740 37.8212 -3.3909 REMARK 3 T TENSOR REMARK 3 T11: 0.2189 T22: 0.2860 REMARK 3 T33: 0.3013 T12: -0.0061 REMARK 3 T13: 0.0000 T23: -0.0433 REMARK 3 L TENSOR REMARK 3 L11: 1.0523 L22: 1.3927 REMARK 3 L33: 3.7650 L12: -0.8449 REMARK 3 L13: -0.6243 L23: 0.9491 REMARK 3 S TENSOR REMARK 3 S11: -0.0433 S12: 0.2354 S13: 0.0123 REMARK 3 S21: -0.0080 S22: 0.0079 S23: -0.0916 REMARK 3 S31: -0.1421 S32: -0.0697 S33: 0.0633 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.4226 42.6304 3.9484 REMARK 3 T TENSOR REMARK 3 T11: 0.2458 T22: 0.2045 REMARK 3 T33: 0.2860 T12: 0.0294 REMARK 3 T13: 0.0121 T23: -0.0191 REMARK 3 L TENSOR REMARK 3 L11: 7.9741 L22: 4.3051 REMARK 3 L33: 4.4977 L12: -0.2947 REMARK 3 L13: 1.8354 L23: 1.6615 REMARK 3 S TENSOR REMARK 3 S11: -0.2602 S12: 0.0853 S13: 0.4107 REMARK 3 S21: 0.0952 S22: -0.1645 S23: -0.0312 REMARK 3 S31: -0.3971 S32: -0.0159 S33: 0.2536 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.9846 23.0692 -24.1188 REMARK 3 T TENSOR REMARK 3 T11: 0.2125 T22: 0.2226 REMARK 3 T33: 0.1554 T12: 0.0457 REMARK 3 T13: -0.0582 T23: 0.0202 REMARK 3 L TENSOR REMARK 3 L11: 0.2157 L22: 6.7480 REMARK 3 L33: 6.1899 L12: 0.1158 REMARK 3 L13: 0.7610 L23: 1.3668 REMARK 3 S TENSOR REMARK 3 S11: 0.4121 S12: -0.4240 S13: 0.2020 REMARK 3 S21: 0.9523 S22: -0.5201 S23: 0.1694 REMARK 3 S31: 0.1794 S32: -0.2932 S33: 0.0511 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 89 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.8454 20.6951 -33.9866 REMARK 3 T TENSOR REMARK 3 T11: 0.2331 T22: 0.1847 REMARK 3 T33: 0.1889 T12: 0.0054 REMARK 3 T13: 0.0035 T23: 0.0190 REMARK 3 L TENSOR REMARK 3 L11: 2.6308 L22: 2.6307 REMARK 3 L33: 2.4758 L12: 0.9382 REMARK 3 L13: 0.4945 L23: 0.2094 REMARK 3 S TENSOR REMARK 3 S11: 0.0720 S12: -0.1684 S13: -0.0803 REMARK 3 S21: 0.1150 S22: -0.1248 S23: -0.2255 REMARK 3 S31: 0.2343 S32: 0.1024 S33: 0.0507 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.5316 21.7735 -22.0663 REMARK 3 T TENSOR REMARK 3 T11: 0.3382 T22: 0.2311 REMARK 3 T33: 0.2930 T12: -0.0428 REMARK 3 T13: 0.0206 T23: 0.0058 REMARK 3 L TENSOR REMARK 3 L11: 0.1821 L22: 0.5130 REMARK 3 L33: 2.2468 L12: 0.0923 REMARK 3 L13: 0.4847 L23: 1.7232 REMARK 3 S TENSOR REMARK 3 S11: -0.1003 S12: 0.0021 S13: -0.0524 REMARK 3 S21: 0.0754 S22: -0.0082 S23: 0.1133 REMARK 3 S31: 0.3310 S32: 0.0557 S33: -0.0204 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.3269 27.7341 -2.6969 REMARK 3 T TENSOR REMARK 3 T11: 0.2417 T22: 0.2250 REMARK 3 T33: 0.2402 T12: -0.0243 REMARK 3 T13: 0.0074 T23: -0.0562 REMARK 3 L TENSOR REMARK 3 L11: 4.6876 L22: 1.3466 REMARK 3 L33: 3.7582 L12: 0.8878 REMARK 3 L13: -2.6625 L23: -0.9884 REMARK 3 S TENSOR REMARK 3 S11: 0.1031 S12: 0.4039 S13: 0.0254 REMARK 3 S21: 0.0275 S22: 0.0284 S23: 0.2538 REMARK 3 S31: -0.0278 S32: -0.3547 S33: 0.0557 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 151 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.1720 24.8282 -4.2474 REMARK 3 T TENSOR REMARK 3 T11: 0.2488 T22: 0.2174 REMARK 3 T33: 0.2673 T12: -0.0056 REMARK 3 T13: 0.0079 T23: -0.0978 REMARK 3 L TENSOR REMARK 3 L11: 4.7435 L22: 2.2316 REMARK 3 L33: 3.5325 L12: 0.7387 REMARK 3 L13: -1.6469 L23: -0.7823 REMARK 3 S TENSOR REMARK 3 S11: -0.1649 S12: 0.2184 S13: -0.3987 REMARK 3 S21: -0.0456 S22: 0.0043 S23: 0.1079 REMARK 3 S31: 0.2672 S32: -0.0682 S33: 0.1626 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 12 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.6596 9.8095 -47.2254 REMARK 3 T TENSOR REMARK 3 T11: 0.3500 T22: 0.3012 REMARK 3 T33: 0.3134 T12: 0.0252 REMARK 3 T13: 0.0259 T23: -0.0102 REMARK 3 L TENSOR REMARK 3 L11: 9.8765 L22: 4.4347 REMARK 3 L33: 3.5303 L12: -2.7727 REMARK 3 L13: 4.3079 L23: 1.2283 REMARK 3 S TENSOR REMARK 3 S11: 0.0163 S12: 0.5264 S13: 0.4089 REMARK 3 S21: -0.4784 S22: -0.5654 S23: -0.3200 REMARK 3 S31: -0.4004 S32: 1.0204 S33: 0.6572 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 6AXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-17. REMARK 100 THE DEPOSITION ID IS D_1000229960. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-MAR-17 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-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32026 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 46.520 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.17400 REMARK 200 FOR THE DATA SET : 11.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14 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) : 0.92100 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: HOMOLOGY MODEL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.0 36% PEG400 5% PEG3000, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K 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 33.05850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.03950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.36450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.03950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.05850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.36450 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 300 REMARK: TRIMER BY ISOTHERMAL TITRATION CALORIMETRY 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: 6550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 CYS A 216 REMARK 465 GLU B 210 REMARK 465 CYS B 211 REMARK 465 SER B 212 REMARK 465 ALA E 13 REMARK 465 NH2 E 14 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 LYS B 156 CG CD CE NZ REMARK 470 LYS B 163 CG CD CE NZ REMARK 470 ARG B 189 CG CD NE CZ NH1 NH2 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 H GLN B 167 O LYS B 171 1.54 REMARK 500 O HOH B 488 O HOH B 528 2.09 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 GLN B 126 NZ LYS B 171 4465 2.18 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 TYR A 98 -104.23 -113.88 REMARK 500 ASP A 144 73.37 62.97 REMARK 500 THR A 191 -67.38 -129.46 REMARK 500 ASN B 27B -94.69 -128.49 REMARK 500 ASN B 51 -45.19 79.37 REMARK 500 SER B 90 -151.12 -157.31 REMARK 500 ASP B 138 43.68 72.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 1PE A 302 REMARK 610 1PE B 303 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 303 DBREF 6AXK A 1 216 PDB 6AXK 6AXK 1 216 DBREF 6AXK B 1 212 PDB 6AXK 6AXK 1 212 DBREF 6AXK E 1 14 PDB 6AXK 6AXK 1 14 SEQRES 1 A 224 PCA VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL PRO SEQRES 2 A 224 PRO GLY ARG SER LEU ARG LEU SER CYS ALA THR SER GLY SEQRES 3 A 224 PHE THR PHE SER ASN TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 A 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ILE ILE TRP SEQRES 5 A 224 TYR ASP GLY SER ARG ASN PHE TYR ALA ALA SER VAL GLU SEQRES 6 A 224 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 224 LEU TYR LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 A 224 ALA VAL TYR TYR CYS ALA ARG ALA ALA TYR TYR ASP THR SEQRES 9 A 224 SER GLY TYR GLY ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 A 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 A 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 A 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 A 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 A 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 A 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 A 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 A 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 A 224 LYS SER CYS SEQRES 1 B 218 PCA SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 B 218 PRO GLY GLN THR VAL THR ILE SER CYS THR GLY GLY SER SEQRES 3 B 218 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 B 218 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 B 218 ASN ILE ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 B 218 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 B 218 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 B 218 SER TYR ASP ARG ARG LEU SER GLY SER TRP VAL PHE GLY SEQRES 9 B 218 GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA SEQRES 10 B 218 ALA PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU SEQRES 11 B 218 LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU VAL SER SEQRES 12 B 218 ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA SEQRES 13 B 218 ASP GLY SER PRO VAL LYS VAL GLY VAL GLU THR THR LYS SEQRES 14 B 218 PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER SEQRES 15 B 218 TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SEQRES 16 B 218 SER TYR SER CYS ARG VAL THR HIS GLU GLY SER THR VAL SEQRES 17 B 218 GLU LYS THR VAL ALA PRO ALA GLU CYS SER SEQRES 1 E 14 ACE ASN PRO ASN ALA ASN PRO ASN ALA ASN PRO ASN ALA SEQRES 2 E 14 NH2 HET PCA A 1 14 HET PCA B 1 14 HET ACE E 1 3 HET MES A 301 25 HET 1PE A 302 22 HET MES B 301 25 HET MES B 302 25 HET 1PE B 303 19 HETNAM PCA PYROGLUTAMIC ACID HETNAM ACE ACETYL GROUP HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID HETNAM 1PE PENTAETHYLENE GLYCOL HETSYN 1PE PEG400 FORMUL 1 PCA 2(C5 H7 N O3) FORMUL 3 ACE C2 H4 O FORMUL 4 MES 3(C6 H13 N O4 S) FORMUL 5 1PE 2(C10 H22 O6) FORMUL 9 HOH *242(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASN A 73 LYS A 75 5 3 HELIX 3 AA3 ARG A 83 THR A 87 5 5 HELIX 4 AA4 SER A 156 ALA A 158 5 3 HELIX 5 AA5 SER A 187 LEU A 189 5 3 HELIX 6 AA6 LYS A 201 ASN A 204 5 4 HELIX 7 AA7 ASN B 27B GLY B 30 5 5 HELIX 8 AA8 GLN B 79 GLU B 83 5 5 HELIX 9 AA9 SER B 121 ALA B 127 1 7 HELIX 10 AB1 THR B 181 SER B 187 1 7 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AA1 4 PHE A 67 ASP A 72 -1 N THR A 68 O GLN A 81 SHEET 1 AA2 6 VAL A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA2 6 ALA A 88 TYR A 97 -1 N TYR A 90 O THR A 107 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 91 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O VAL A 48 N TRP A 36 SHEET 6 AA2 6 ASN A 57 TYR A 59 -1 O PHE A 58 N ILE A 50 SHEET 1 AA3 4 VAL A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA3 4 ALA A 88 TYR A 97 -1 N TYR A 90 O THR A 107 SHEET 4 AA3 4 GLY A 100B TRP A 103 -1 O TYR A 102 N ARG A 94 SHEET 1 AA4 4 SER A 120 SER A 127 0 SHEET 2 AA4 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA4 4 TYR A 176 PRO A 185 -1 O VAL A 182 N LEU A 138 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AA5 4 SER A 120 SER A 127 0 SHEET 2 AA5 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA5 4 TYR A 176 PRO A 185 -1 O VAL A 182 N LEU A 138 SHEET 4 AA5 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AA6 3 THR A 205 LYS A 210 -1 O VAL A 207 N VAL A 198 SHEET 1 AA7 5 SER B 9 GLY B 13 0 SHEET 2 AA7 5 THR B 102 VAL B 106 1 O LYS B 103 N VAL B 11 SHEET 3 AA7 5 ALA B 84 SER B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AA7 5 HIS B 34 GLN B 38 -1 N GLN B 38 O ASP B 85 SHEET 5 AA7 5 LYS B 45 ILE B 48 -1 O LYS B 45 N GLN B 37 SHEET 1 AA8 4 SER B 9 GLY B 13 0 SHEET 2 AA8 4 THR B 102 VAL B 106 1 O LYS B 103 N VAL B 11 SHEET 3 AA8 4 ALA B 84 SER B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AA8 4 VAL B 97 PHE B 98 -1 O VAL B 97 N SER B 90 SHEET 1 AA9 3 VAL B 19 THR B 24 0 SHEET 2 AA9 3 SER B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 3 AA9 3 PHE B 62 SER B 67 -1 N SER B 63 O ALA B 74 SHEET 1 AB1 4 SER B 114 PHE B 118 0 SHEET 2 AB1 4 ALA B 130 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 AB1 4 TYR B 172 LEU B 180 -1 O ALA B 174 N VAL B 136 SHEET 4 AB1 4 VAL B 159 THR B 161 -1 N GLU B 160 O TYR B 177 SHEET 1 AB2 4 SER B 114 PHE B 118 0 SHEET 2 AB2 4 ALA B 130 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 AB2 4 TYR B 172 LEU B 180 -1 O ALA B 174 N VAL B 136 SHEET 4 AB2 4 SER B 165 LYS B 166 -1 N SER B 165 O ALA B 173 SHEET 1 AB3 4 SER B 153 VAL B 155 0 SHEET 2 AB3 4 THR B 145 ALA B 150 -1 N ALA B 150 O SER B 153 SHEET 3 AB3 4 TYR B 191 HIS B 197 -1 O ARG B 194 N ALA B 147 SHEET 4 AB3 4 SER B 200 VAL B 206 -1 O SER B 200 N HIS B 197 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.03 SSBOND 2 CYS A 140 CYS A 196 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 4 CYS B 134 CYS B 193 1555 1555 2.03 LINK C PCA A 1 N VAL A 2 1555 1555 1.33 LINK C PCA B 1 N SER B 2 1555 1555 1.33 LINK C ACE E 1 N ASN E 2 1555 1555 1.33 CISPEP 1 PHE A 146 PRO A 147 0 -6.64 CISPEP 2 GLU A 148 PRO A 149 0 -5.40 CISPEP 3 TYR B 140 PRO B 141 0 1.07 SITE 1 AC1 6 SER A 156 ASN A 197 ASP A 208 HOH A 404 SITE 2 AC1 6 ARG B 194 GLU B 203 SITE 1 AC2 3 SER A 55 ARG A 56 ASN A 57 SITE 1 AC3 6 SER A 120 SER A 130 SER A 132 SER B 114 SITE 2 AC3 6 VAL B 115 LYS B 204 SITE 1 AC4 4 ASP B 85 TYR B 87 GLY B 100 GLY B 101 SITE 1 AC5 3 TYR A 91 PRO B 40 GLY B 41 CRYST1 66.117 44.729 186.079 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 0.015125 0.000000 0.000000 0.00000 SCALE2 0.000000 0.022357 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005374 0.00000