HEADER CELL INVASION 16-MAY-20 6Z2L TITLE STRUCTURE OF PLASMODIUM FALCIPARUM P113 BOUND TO ANTIBODY P3.2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SURFACE PROTEIN P113; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: LYS METHYLATION METHOD WAS USED RESULTING ON COMPND 6 METHYLATION OF SOME LYS RESIDUES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB FRAGMENT - VL CHAIN; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FAB FRAGMENT - VH CHAIN; COMPND 13 CHAIN: C; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 3 ORGANISM_TAXID: 36329; SOURCE 4 GENE: P113, PF3D7_1420700; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 18 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 19 ORGANISM_TAXID: 10090; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS PROTEIN COMPLEX, FAB-ANTIGEN, INVASION, CELL INVASION EXPDTA X-RAY DIFFRACTION AUTHOR I.CAMPEOTTO,K.M.HIGGINS REVDAT 1 22-JUL-20 6Z2L 0 JRNL AUTH I.CAMPEOTTO,F.GALAWAY,S.MEHMOOD,L.K.BARFOD,D.QUINKERT, JRNL AUTH 2 V.KOTRAIAH,T.W.PHARES,K.E.WRIGHT,A.P.SNIJDERS,S.J.DRAPER, JRNL AUTH 3 K.M.HIGGINS,G.J.WRIGHT JRNL TITL STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF PLASMODIUM JRNL TITL 2 FALCIPARUM P113 IDENTIFIES THE LOCATION OF THE RH5 BINDING JRNL TITL 3 SITE JRNL REF BIORXIV 2020 JRNL REFN JRNL DOI 10.1101/2020.06.12.149534V1 REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.3 (19-MAR-2020) REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.95 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 62481 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.205 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 3110 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 51 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.96 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.77 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1250 REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1190 REMARK 3 BIN R VALUE (WORKING SET) : 0.2353 REMARK 3 BIN FREE R VALUE : 0.2673 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 60 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4929 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 5 REMARK 3 SOLVENT ATOMS : 395 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.14 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.20670 REMARK 3 B22 (A**2) : 4.20670 REMARK 3 B33 (A**2) : -8.41350 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.290 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.150 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.131 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.143 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.128 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 5043 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 6848 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1713 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 854 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 5039 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 674 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 4475 ; 0.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 1.13 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.33 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.15 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 10.5179 51.0550 -17.6815 REMARK 3 T TENSOR REMARK 3 T11: -0.0482 T22: -0.0913 REMARK 3 T33: -0.0586 T12: 0.0037 REMARK 3 T13: -0.0461 T23: -0.0508 REMARK 3 L TENSOR REMARK 3 L11: 0.6507 L22: 0.0000 REMARK 3 L33: 0.4115 L12: 0.2665 REMARK 3 L13: -0.0669 L23: 0.1285 REMARK 3 S TENSOR REMARK 3 S11: 0.0881 S12: -0.0268 S13: 0.1974 REMARK 3 S21: -0.0689 S22: -0.1142 S23: 0.1064 REMARK 3 S31: 0.1579 S32: 0.0070 S33: 0.0261 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): 0.4426 0.2223 -14.9419 REMARK 3 T TENSOR REMARK 3 T11: -0.0803 T22: -0.0654 REMARK 3 T33: -0.0512 T12: -0.0062 REMARK 3 T13: 0.0121 T23: -0.0162 REMARK 3 L TENSOR REMARK 3 L11: 0.0669 L22: 0.5160 REMARK 3 L33: 0.3165 L12: 0.4001 REMARK 3 L13: 0.3620 L23: 0.1383 REMARK 3 S TENSOR REMARK 3 S11: 0.0940 S12: -0.1442 S13: -0.0612 REMARK 3 S21: 0.0620 S22: -0.1315 S23: -0.0117 REMARK 3 S31: 0.0015 S32: -0.0098 S33: 0.0374 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|* } REMARK 3 ORIGIN FOR THE GROUP (A): 7.5240 6.8685 -29.5479 REMARK 3 T TENSOR REMARK 3 T11: -0.0775 T22: -0.0868 REMARK 3 T33: -0.0392 T12: 0.0373 REMARK 3 T13: 0.0040 T23: -0.0292 REMARK 3 L TENSOR REMARK 3 L11: 0.0220 L22: 0.4017 REMARK 3 L33: 0.1910 L12: 0.3175 REMARK 3 L13: 0.0969 L23: 0.0287 REMARK 3 S TENSOR REMARK 3 S11: -0.0415 S12: -0.0423 S13: -0.1155 REMARK 3 S21: -0.0236 S22: -0.0022 S23: -0.0784 REMARK 3 S31: -0.0949 S32: -0.0459 S33: 0.0437 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6Z2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAY-20. REMARK 100 THE DEPOSITION ID IS D_1292108764. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-DEC-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 : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762 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 : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62481 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 63.950 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.01600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.3100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.43870 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: 4U0R REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NH4SO4, 0.1M MES PH=6.5, 20% W/V REMARK 280 PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 88.94900 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.46050 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.46050 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.47450 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.46050 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.46050 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 133.42350 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.46050 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.46050 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.47450 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.46050 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.46050 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 133.42350 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 88.94900 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: 5470 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 LEU B 1 REMARK 465 LEU B 2 REMARK 465 LEU B 3 REMARK 465 CYS B 4 REMARK 465 PHE B 5 REMARK 465 GLN B 6 REMARK 465 GLY B 7 REMARK 465 THR B 8 REMARK 465 ARG B 9 REMARK 465 CYS B 10 REMARK 465 CYS B 224 REMARK 465 MET C 1 REMARK 465 GLY C 2 REMARK 465 TRP C 3 REMARK 465 THR C 4 REMARK 465 TYR C 5 REMARK 465 ILE C 6 REMARK 465 ILE C 7 REMARK 465 LEU C 8 REMARK 465 PHE C 9 REMARK 465 LEU C 10 REMARK 465 VAL C 11 REMARK 465 ALA C 12 REMARK 465 ALA C 13 REMARK 465 VAL C 14 REMARK 465 THR C 15 REMARK 465 GLY C 16 REMARK 465 VAL C 17 REMARK 465 HIS C 18 REMARK 465 SER C 19 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 81 -73.36 -64.42 REMARK 500 GLU A 90 138.55 -172.53 REMARK 500 THR B 61 -49.93 75.44 REMARK 500 SER B 211 146.88 -176.76 REMARK 500 ALA C 111 162.74 176.03 REMARK 500 THR C 214 -76.97 -108.10 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 201 DBREF 6Z2L A 1 197 UNP Q8ILP3 P113_PLAF7 23 219 DBREF 6Z2L B 1 224 PDB 6Z2L 6Z2L 1 224 DBREF 6Z2L C 1 240 PDB 6Z2L 6Z2L 1 240 SEQADV 6Z2L ALA A 187 UNP Q8ILP3 SER 209 CONFLICT SEQRES 1 A 197 TYR VAL HIS ASN ASP VAL ILE LYS PHE GLY GLU GLU ASN SEQRES 2 A 197 SER LEU LYS CYS SER GLN GLY ASN LEU TYR VAL LEU HIS SEQRES 3 A 197 CYS GLU VAL GLN CYS LEU ASN GLY ASN ASN GLU ILE ILE SEQRES 4 A 197 HIS LYS ARG CYS ASN ASP ASP ILE GLU LYS LYS CYS ASN SEQRES 5 A 197 GLY ASN ASN LYS CYS ILE TYR PHE PHE GLU TYR GLU LEU SEQRES 6 A 197 ARG LYS LYS THR GLN SER PHE ARG ASN LYS ASN SER ILE SEQRES 7 A 197 GLU ILE SER GLU CYS VAL GLU SER GLU GLN ASN GLU VAL SEQRES 8 A 197 LYS THR SER THR THR CYS LEU LEU SER ASN SER PHE ILE SEQRES 9 A 197 LEU ASP GLU ALA PHE ILE GLN TYR PHE PHE PHE ILE MLY SEQRES 10 A 197 ASN MLY ASN GLU GLU PRO VAL ILE CYS LYS ASP GLY ASN SEQRES 11 A 197 ILE ASN ILE LYS SER ALA LEU LEU HIS SER PRO PHE CYS SEQRES 12 A 197 GLU ILE LYS LEU MLY ASP ILE SER GLU TYR ILE ARG LYS SEQRES 13 A 197 MLY CYS ASP ASN ASN LYS GLU CYS LEU ILE ASP PRO LEU SEQRES 14 A 197 ASP VAL GLN LYS ASN LEU LEU ASN GLU GLU ASP PRO CYS SEQRES 15 A 197 TYR ILE ASN ASN ALA TYR VAL SER VAL ASN VAL VAL CYS SEQRES 16 A 197 ASN LYS SEQRES 1 B 224 LEU LEU LEU CYS PHE GLN GLY THR ARG CYS ASP ILE GLN SEQRES 2 B 224 MET THR GLN THR THR SER SER LEU SER ALA SER LEU GLY SEQRES 3 B 224 ASP ARG VAL THR ILE SER CYS ARG ALA SER GLN ASP ILE SEQRES 4 B 224 SER ASN TYR LEU ASN TRP TYR GLN GLN LYS PRO ASP GLY SEQRES 5 B 224 THR VAL LYS LEU LEU ILE TYR TYR THR SER ARG LEU HIS SEQRES 6 B 224 SER GLY VAL SER SER ARG PHE SER GLY SER GLY SER GLY SEQRES 7 B 224 THR ASP TYR SER LEU THR ILE LYS ASN LEU GLU GLN GLU SEQRES 8 B 224 ASP ILE ALA THR TYR PHE CYS GLN GLN VAL ASN ALA LEU SEQRES 9 B 224 PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU ILE LYS SEQRES 10 B 224 ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO PRO SEQRES 11 B 224 SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL VAL SEQRES 12 B 224 CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN VAL SEQRES 13 B 224 LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY VAL SEQRES 14 B 224 LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER THR SEQRES 15 B 224 TYR SER MET SER SER THR LEU THR LEU THR LYS ASP GLU SEQRES 16 B 224 TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR HIS SEQRES 17 B 224 LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN ARG SEQRES 18 B 224 ASN GLU CYS SEQRES 1 C 240 MET GLY TRP THR TYR ILE ILE LEU PHE LEU VAL ALA ALA SEQRES 2 C 240 VAL THR GLY VAL HIS SER GLN VAL GLN LEU GLN GLN PRO SEQRES 3 C 240 GLY ALA GLU LEU VAL LYS PRO GLY ALA SER VAL ARG LEU SEQRES 4 C 240 SER CYS LYS ALA SER GLY TYR THR PHE THR SER TYR PHE SEQRES 5 C 240 MET TYR TRP VAL ARG GLN ARG PRO GLY GLN GLY LEU GLN SEQRES 6 C 240 SER ILE GLY GLY ILE ASN PRO ASN ASN GLY GLY SER ASN SEQRES 7 C 240 PHE ASN GLU ARG PHE LYS THR LYS ALA THR LEU THR VAL SEQRES 8 C 240 ASP LYS SER SER SER ILE ALA TYR LEU GLN LEU ASN SER SEQRES 9 C 240 LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS THR ARG SEQRES 10 C 240 ARG GLY LEU GLY TYR ASP TYR GLY GLY PHE ALA TYR TRP SEQRES 11 C 240 GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS THR SEQRES 12 C 240 THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA SEQRES 13 C 240 ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU VAL SEQRES 14 C 240 LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SEQRES 15 C 240 SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA SEQRES 16 C 240 VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL SEQRES 17 C 240 THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL THR SEQRES 18 C 240 CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP SEQRES 19 C 240 LYS LYS ILE VAL PRO ARG MODRES 6Z2L MLY A 117 LYS MODIFIED RESIDUE MODRES 6Z2L MLY A 119 LYS MODIFIED RESIDUE MODRES 6Z2L MLY A 148 LYS MODIFIED RESIDUE MODRES 6Z2L MLY A 157 LYS MODIFIED RESIDUE HET MLY A 117 11 HET MLY A 119 11 HET MLY A 148 11 HET MLY A 157 11 HET SO4 A 201 5 HETNAM MLY N-DIMETHYL-LYSINE HETNAM SO4 SULFATE ION FORMUL 1 MLY 4(C8 H18 N2 O2) FORMUL 4 SO4 O4 S 2- FORMUL 5 HOH *395(H2 O) HELIX 1 AA1 CYS A 43 ASN A 52 1 10 HELIX 2 AA2 SER A 71 LYS A 75 5 5 HELIX 3 AA3 ILE A 150 ASP A 159 1 10 HELIX 4 AA4 ASP A 167 LEU A 175 1 9 HELIX 5 AA5 ASP A 180 ALA A 187 1 8 HELIX 6 AA6 GLU B 89 ILE B 93 5 5 HELIX 7 AA7 SER B 131 SER B 137 1 7 HELIX 8 AA8 LYS B 193 ARG B 198 1 6 HELIX 9 AA9 THR C 47 TYR C 51 5 5 HELIX 10 AB1 GLU C 81 LYS C 84 5 4 HELIX 11 AB2 THR C 106 SER C 110 5 5 HELIX 12 AB3 SER C 183 SER C 185 5 3 HELIX 13 AB4 PRO C 227 SER C 230 5 4 SHEET 1 AA1 4 VAL A 2 ILE A 7 0 SHEET 2 AA1 4 GLU A 90 LEU A 98 -1 O THR A 93 N ASP A 5 SHEET 3 AA1 4 ASN A 21 LEU A 32 -1 N ASN A 21 O LEU A 98 SHEET 4 AA1 4 ILE A 38 ARG A 42 -1 O ILE A 39 N CYS A 31 SHEET 1 AA2 3 ASN A 13 LYS A 16 0 SHEET 2 AA2 3 LYS A 56 TYR A 63 -1 O TYR A 59 N ASN A 13 SHEET 3 AA2 3 SER A 77 ILE A 80 1 O ILE A 78 N GLU A 62 SHEET 1 AA3 3 ILE A 104 LEU A 105 0 SHEET 2 AA3 3 VAL A 124 CYS A 126 1 O ILE A 125 N LEU A 105 SHEET 3 AA3 3 GLU A 163 CYS A 164 -1 O CYS A 164 N VAL A 124 SHEET 1 AA4 4 TYR A 112 ILE A 116 0 SHEET 2 AA4 4 TYR A 188 ASN A 196 -1 O VAL A 193 N TYR A 112 SHEET 3 AA4 4 ASN A 130 HIS A 139 -1 N HIS A 139 O TYR A 188 SHEET 4 AA4 4 LEU A 147 ASP A 149 -1 O MLY A 148 N LEU A 138 SHEET 1 AA5 4 MET B 14 THR B 15 0 SHEET 2 AA5 4 VAL B 29 ALA B 35 -1 O ARG B 34 N THR B 15 SHEET 3 AA5 4 ASP B 80 ILE B 85 -1 O LEU B 83 N ILE B 31 SHEET 4 AA5 4 PHE B 72 SER B 77 -1 N SER B 73 O THR B 84 SHEET 1 AA6 6 SER B 20 ALA B 23 0 SHEET 2 AA6 6 THR B 112 ILE B 116 1 O GLU B 115 N LEU B 21 SHEET 3 AA6 6 ALA B 94 GLN B 100 -1 N TYR B 96 O THR B 112 SHEET 4 AA6 6 LEU B 43 GLN B 48 -1 N GLN B 48 O THR B 95 SHEET 5 AA6 6 VAL B 54 TYR B 59 -1 O LEU B 57 N TRP B 45 SHEET 6 AA6 6 ARG B 63 LEU B 64 -1 O ARG B 63 N TYR B 59 SHEET 1 AA7 4 SER B 20 ALA B 23 0 SHEET 2 AA7 4 THR B 112 ILE B 116 1 O GLU B 115 N LEU B 21 SHEET 3 AA7 4 ALA B 94 GLN B 100 -1 N TYR B 96 O THR B 112 SHEET 4 AA7 4 THR B 107 PHE B 108 -1 O THR B 107 N GLN B 100 SHEET 1 AA8 4 THR B 124 PHE B 128 0 SHEET 2 AA8 4 GLY B 139 PHE B 149 -1 O VAL B 143 N PHE B 128 SHEET 3 AA8 4 TYR B 183 THR B 192 -1 O LEU B 189 N VAL B 142 SHEET 4 AA8 4 VAL B 169 TRP B 173 -1 N SER B 172 O SER B 186 SHEET 1 AA9 4 SER B 163 ARG B 165 0 SHEET 2 AA9 4 ASN B 155 ILE B 160 -1 N ILE B 160 O SER B 163 SHEET 3 AA9 4 SER B 201 THR B 207 -1 O THR B 207 N ASN B 155 SHEET 4 AA9 4 ILE B 215 ASN B 220 -1 O ILE B 215 N ALA B 206 SHEET 1 AB1 4 GLN C 22 GLN C 24 0 SHEET 2 AB1 4 VAL C 37 SER C 44 -1 O LYS C 42 N GLN C 24 SHEET 3 AB1 4 ILE C 97 LEU C 102 -1 O LEU C 100 N LEU C 39 SHEET 4 AB1 4 ALA C 87 ASP C 92 -1 N THR C 88 O GLN C 101 SHEET 1 AB2 6 ALA C 28 VAL C 31 0 SHEET 2 AB2 6 THR C 134 VAL C 138 1 O THR C 137 N VAL C 31 SHEET 3 AB2 6 ALA C 111 ARG C 118 -1 N ALA C 111 O VAL C 136 SHEET 4 AB2 6 MET C 53 GLN C 58 -1 N VAL C 56 O TYR C 114 SHEET 5 AB2 6 GLN C 65 ILE C 70 -1 O GLN C 65 N ARG C 57 SHEET 6 AB2 6 SER C 77 PHE C 79 -1 O ASN C 78 N GLY C 69 SHEET 1 AB3 4 ALA C 28 VAL C 31 0 SHEET 2 AB3 4 THR C 134 VAL C 138 1 O THR C 137 N VAL C 31 SHEET 3 AB3 4 ALA C 111 ARG C 118 -1 N ALA C 111 O VAL C 136 SHEET 4 AB3 4 PHE C 127 TRP C 130 -1 O TYR C 129 N ARG C 117 SHEET 1 AB4 4 SER C 147 LEU C 151 0 SHEET 2 AB4 4 VAL C 163 TYR C 172 -1 O LYS C 170 N SER C 147 SHEET 3 AB4 4 LEU C 201 VAL C 210 -1 O VAL C 208 N LEU C 165 SHEET 4 AB4 4 VAL C 190 THR C 192 -1 N HIS C 191 O SER C 207 SHEET 1 AB5 4 SER C 147 LEU C 151 0 SHEET 2 AB5 4 VAL C 163 TYR C 172 -1 O LYS C 170 N SER C 147 SHEET 3 AB5 4 LEU C 201 VAL C 210 -1 O VAL C 208 N LEU C 165 SHEET 4 AB5 4 VAL C 196 GLN C 198 -1 N GLN C 198 O LEU C 201 SHEET 1 AB6 3 THR C 178 TRP C 181 0 SHEET 2 AB6 3 THR C 221 HIS C 226 -1 O ASN C 223 N THR C 180 SHEET 3 AB6 3 THR C 231 LYS C 236 -1 O VAL C 233 N VAL C 224 SSBOND 1 CYS A 17 CYS A 97 1555 1555 2.05 SSBOND 2 CYS A 27 CYS A 43 1555 1555 1.91 SSBOND 3 CYS A 31 CYS A 83 1555 1555 2.06 SSBOND 4 CYS A 51 CYS A 57 1555 1555 2.09 SSBOND 5 CYS A 126 CYS A 195 1555 1555 2.07 SSBOND 6 CYS A 143 CYS A 182 1555 1555 2.04 SSBOND 7 CYS A 158 CYS A 164 1555 1555 2.03 SSBOND 8 CYS B 33 CYS B 98 1555 1555 2.27 SSBOND 9 CYS B 144 CYS B 204 1555 1555 2.06 SSBOND 10 CYS C 41 CYS C 115 1555 1555 2.06 SSBOND 11 CYS C 167 CYS C 222 1555 1555 2.11 LINK C ILE A 116 N MLY A 117 1555 1555 1.33 LINK C MLY A 117 N ASN A 118 1555 1555 1.33 LINK C ASN A 118 N MLY A 119 1555 1555 1.33 LINK C MLY A 119 N ASN A 120 1555 1555 1.33 LINK C LEU A 147 N MLY A 148 1555 1555 1.33 LINK C MLY A 148 N ASP A 149 1555 1555 1.33 LINK C LYS A 156 N MLY A 157 1555 1555 1.33 LINK C MLY A 157 N CYS A 158 1555 1555 1.33 CISPEP 1 LEU B 104 PRO B 105 0 -1.00 CISPEP 2 TYR B 150 PRO B 151 0 4.73 CISPEP 3 PHE C 173 PRO C 174 0 -8.67 CISPEP 4 GLU C 175 PRO C 176 0 2.19 CISPEP 5 TRP C 215 PRO C 216 0 2.20 SITE 1 AC1 5 MLY A 148 ASP A 149 HOH A 330 ASN C 73 SITE 2 AC1 5 ASN C 74 CRYST1 96.921 96.921 177.898 90.00 90.00 90.00 P 41 21 2 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 0.010318 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010318 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005621 0.00000