HEADER IMMUNE SYSTEM 24-JUN-22 8DGR TITLE CRYSTAL STRUCTURE OF SCFV(F8) ANTIBODY FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: SCFV F8; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: HIS6X-TAG & TEV CUT COMPND 6 SITE:MGSSHHHHHHSSGENLYFQGHM;HEAVY(VH) COMPND 7 :QVQLQESGGDLVQPGGSLKLSCAASGFTFSSYGMSWVRQTPDKRLELVATINSNGGSTFYPDSVKGRF COMPND 8 TISRDNAKNTLYLQMSSLKSEDTAMYYCARRRNYPYYYGSRGYFDYWGQGTTVTVSS;LINKER: COMPND 9 GGGGSGGGGSGGGGS;LIGHT (VL) COMPND 10 :DIELTQSPASLAVSLGQRATISCRASESVDSYGNSFMHWYQQKPGQPPKLLIYRALNLESGIPARFSG COMPND 11 SGSRTDFTLTINPVEADDVAIYYCQQSNEDPWTFGGGTKLEIKR SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARTICHOKE MOTTLED CRINKLE VIRUS; SOURCE 3 ORGANISM_TAXID: 12142; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY FRAGMENT, SCFV, SHORT CHAIN VARIABLE FRAGMENT, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.MROZEK,H.W.PARK REVDAT 1 05-JUL-23 8DGR 0 JRNL AUTH A.MROZEK,H.W.PARK JRNL TITL SCFV(F8) ANTIBODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.56 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0350 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.53 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 38641 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.175 REMARK 3 FREE R VALUE : 0.195 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.873 REMARK 3 FREE R VALUE TEST SET COUNT : 1883 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.56 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.60 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2582 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.52 REMARK 3 BIN R VALUE (WORKING SET) : 0.1720 REMARK 3 BIN FREE R VALUE SET COUNT : 125 REMARK 3 BIN FREE R VALUE : 0.1970 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1845 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 150 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.00200 REMARK 3 B22 (A**2) : -0.00200 REMARK 3 B33 (A**2) : 0.00500 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.073 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.071 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1902 ; 0.012 ; 0.011 REMARK 3 BOND LENGTHS OTHERS (A): 1641 ; 0.002 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2582 ; 1.736 ; 1.647 REMARK 3 BOND ANGLES OTHERS (DEGREES): 3843 ; 0.616 ; 1.551 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 239 ; 6.539 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 13 ;10.886 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 304 ;12.641 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 273 ; 0.087 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2204 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 400 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 257 ; 0.197 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 53 ; 0.158 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 916 ; 0.182 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 89 ; 0.151 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 950 ; 1.605 ; 1.465 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 950 ; 1.521 ; 1.465 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1185 ; 2.220 ; 2.201 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1186 ; 2.219 ; 2.202 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 952 ; 3.283 ; 1.757 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 953 ; 3.282 ; 1.760 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1395 ; 4.788 ; 2.514 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1396 ; 4.786 ; 2.517 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 8DGR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-22. REMARK 100 THE DEPOSITION ID IS D_1000266241. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-MAR-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979340 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 367580 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560 REMARK 200 RESOLUTION RANGE LOW (A) : 43.530 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 19.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.17480 REMARK 200 FOR THE DATA SET : 10708.80 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.17200 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: MOLREP REMARK 200 STARTING MODEL: 5B3N REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 0.2 M REMARK 280 MAGNESIUM CHLORIDE, 0.1 M HEPES, 5 % GLYCEROL, PH 7.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 3555 -Y,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X,Z+3/4 REMARK 290 5555 -X+1/2,Y,-Z+3/4 REMARK 290 6555 X,-Y+1/2,-Z+1/4 REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X,-Y,Z REMARK 290 11555 -Y+1/2,X,Z+3/4 REMARK 290 12555 Y,-X+1/2,Z+1/4 REMARK 290 13555 -X,Y+1/2,-Z+1/4 REMARK 290 14555 X+1/2,-Y,-Z+3/4 REMARK 290 15555 Y,X,-Z REMARK 290 16555 -Y+1/2,-X+1/2,-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 59.82200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 59.82200 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.42800 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 59.82200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.71400 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 59.82200 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.14200 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 59.82200 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 56.14200 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.82200 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 18.71400 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 59.82200 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 59.82200 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 37.42800 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 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 59.82200 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 59.82200 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.42800 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 59.82200 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 56.14200 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 59.82200 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 18.71400 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 59.82200 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 18.71400 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 59.82200 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 56.14200 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 59.82200 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 59.82200 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 37.42800 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 SER A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 HIS A -11 REMARK 465 HIS A -10 REMARK 465 SER A -9 REMARK 465 SER A -8 REMARK 465 GLY A -7 REMARK 465 GLU A -6 REMARK 465 ASN A -5 REMARK 465 LEU A -4 REMARK 465 TYR A -3 REMARK 465 PHE A -2 REMARK 465 GLN A -1 REMARK 465 GLY A 0 REMARK 465 HIS A 1 REMARK 465 MET A 2 REMARK 465 GLY A 127A REMARK 465 GLY A 127B REMARK 465 GLY A 127C REMARK 465 GLY A 127D REMARK 465 SER A 127E REMARK 465 GLY A 127F REMARK 465 GLY A 127G REMARK 465 GLY A 127H REMARK 465 GLY A 127I REMARK 465 SER A 127J REMARK 465 GLY A 127K REMARK 465 GLY A 127L REMARK 465 GLY A 127M REMARK 465 GLY A 127N 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 HH TYR A 62 H ILE A 72 1.10 REMARK 500 HG1 THR A 93 H VAL A 125 1.16 REMARK 500 HD1 HIS A 176 H ARG A 192 1.30 REMARK 500 OE1 GLU A 235 O HOH A 301 1.74 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 NH1 ARG A 210 HH11 ARG A 210 6546 1.23 REMARK 500 NH1 ARG A 210 HH12 ARG A 210 6546 1.50 REMARK 500 NH1 ARG A 210 NH1 ARG A 210 6546 1.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 111 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG A 111 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA A 193 -36.98 78.32 REMARK 500 ARG A 210 -95.18 61.95 REMARK 500 ALA A 226 174.82 179.95 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 46 0.11 SIDE CHAIN REMARK 500 ARG A 102 0.10 SIDE CHAIN REMARK 500 ARG A 111 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 8DGR A -19 249 PDB 8DGR 8DGR -19 249 SEQRES 1 A 273 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 273 GLU ASN LEU TYR PHE GLN GLY HIS MET GLN VAL GLN LEU SEQRES 3 A 273 GLN GLU SER GLY GLY ASP LEU VAL GLN PRO GLY GLY SER SEQRES 4 A 273 LEU LYS LEU SER CYS ALA ALA SER GLY PHE THR PHE SER SEQRES 5 A 273 SER TYR GLY MET SER TRP VAL ARG GLN THR PRO ASP LYS SEQRES 6 A 273 ARG LEU GLU LEU VAL ALA THR ILE ASN SER ASN GLY GLY SEQRES 7 A 273 SER THR PHE TYR PRO ASP SER VAL LYS GLY ARG PHE THR SEQRES 8 A 273 ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU GLN SEQRES 9 A 273 MET SER SER LEU LYS SER GLU ASP THR ALA MET TYR TYR SEQRES 10 A 273 CYS ALA ARG ARG ARG ASN TYR PRO TYR TYR TYR GLY SER SEQRES 11 A 273 ARG GLY TYR PHE ASP TYR TRP GLY GLN GLY THR THR VAL SEQRES 12 A 273 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 13 A 273 SER GLY GLY GLY GLY SER ASP ILE GLU LEU THR GLN SER SEQRES 14 A 273 PRO ALA SER LEU ALA VAL SER LEU GLY GLN ARG ALA THR SEQRES 15 A 273 ILE SER CYS ARG ALA SER GLU SER VAL ASP SER TYR GLY SEQRES 16 A 273 ASN SER PHE MET HIS TRP TYR GLN GLN LYS PRO GLY GLN SEQRES 17 A 273 PRO PRO LYS LEU LEU ILE TYR ARG ALA LEU ASN LEU GLU SEQRES 18 A 273 SER GLY ILE PRO ALA ARG PHE SER GLY SER GLY SER ARG SEQRES 19 A 273 THR ASP PHE THR LEU THR ILE ASN PRO VAL GLU ALA ASP SEQRES 20 A 273 ASP VAL ALA ILE TYR TYR CYS GLN GLN SER ASN GLU ASP SEQRES 21 A 273 PRO TRP THR PHE GLY GLY GLY THR LYS LEU GLU ILE LYS FORMUL 2 HOH *150(H2 O) HELIX 1 AA1 THR A 30 TYR A 34 5 5 HELIX 2 AA2 LYS A 89 THR A 93 5 5 HELIX 3 AA3 GLU A 221 VAL A 225 5 5 SHEET 1 AA1 4 GLN A 5 SER A 9 0 SHEET 2 AA1 4 LEU A 20 SER A 27 -1 O SER A 23 N SER A 9 SHEET 3 AA1 4 THR A 80 MET A 85 -1 O MET A 85 N LEU A 20 SHEET 4 AA1 4 PHE A 70 ASP A 75 -1 N SER A 73 O TYR A 82 SHEET 1 AA2 6 LEU A 13 VAL A 14 0 SHEET 2 AA2 6 THR A 121 VAL A 125 1 O THR A 124 N VAL A 14 SHEET 3 AA2 6 ALA A 94 ARG A 102 -1 N TYR A 96 O THR A 121 SHEET 4 AA2 6 MET A 36 GLN A 41 -1 N VAL A 39 O TYR A 97 SHEET 5 AA2 6 LEU A 47 ILE A 53 -1 O GLU A 48 N ARG A 40 SHEET 6 AA2 6 THR A 60 PHE A 61 -1 O PHE A 61 N THR A 52 SHEET 1 AA3 4 LEU A 13 VAL A 14 0 SHEET 2 AA3 4 THR A 121 VAL A 125 1 O THR A 124 N VAL A 14 SHEET 3 AA3 4 ALA A 94 ARG A 102 -1 N TYR A 96 O THR A 121 SHEET 4 AA3 4 TYR A 113 TRP A 117 -1 O TYR A 113 N ARG A 102 SHEET 1 AA4 4 LEU A 142 SER A 145 0 SHEET 2 AA4 4 ALA A 157 ALA A 163 -1 O SER A 160 N SER A 145 SHEET 3 AA4 4 ASP A 212 ILE A 217 -1 O LEU A 215 N ILE A 159 SHEET 4 AA4 4 PHE A 204 SER A 209 -1 N SER A 205 O THR A 216 SHEET 1 AA5 6 SER A 148 VAL A 151 0 SHEET 2 AA5 6 THR A 244 ILE A 248 1 O LYS A 245 N LEU A 149 SHEET 3 AA5 6 ALA A 226 GLN A 232 -1 N ALA A 226 O LEU A 246 SHEET 4 AA5 6 MET A 175 GLN A 180 -1 N GLN A 180 O ILE A 227 SHEET 5 AA5 6 LYS A 187 TYR A 191 -1 O LEU A 189 N TRP A 177 SHEET 6 AA5 6 ASN A 195 LEU A 196 -1 O ASN A 195 N TYR A 191 SHEET 1 AA6 4 SER A 148 VAL A 151 0 SHEET 2 AA6 4 THR A 244 ILE A 248 1 O LYS A 245 N LEU A 149 SHEET 3 AA6 4 ALA A 226 GLN A 232 -1 N ALA A 226 O LEU A 246 SHEET 4 AA6 4 THR A 239 PHE A 240 -1 O THR A 239 N GLN A 232 SHEET 1 AA7 2 ASP A 168 SER A 169 0 SHEET 2 AA7 2 ASN A 172 SER A 173 -1 O ASN A 172 N SER A 169 SSBOND 1 CYS A 24 CYS A 98 1555 1555 2.13 SSBOND 2 CYS A 161 CYS A 230 1555 1555 2.22 CISPEP 1 TYR A 104 PRO A 105 0 -12.77 CISPEP 2 SER A 145 PRO A 146 0 -11.32 CISPEP 3 ASN A 218 PRO A 219 0 -9.76 CISPEP 4 ASP A 236 PRO A 237 0 -3.67 CRYST1 119.644 119.644 74.856 90.00 90.00 90.00 I 41 2 2 16 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 0.008358 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008358 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013359 0.00000