HEADER IMMUNE SYSTEM 28-NOV-19 6TKD TITLE CHILOB 7/4 H2 HC-C228S F(AB')2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHILOB 7/4 H2 HEAVY CHAIN C228S; COMPND 3 CHAIN: HHH; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CHILOB 7/4 H2 KAPPA CHAIN; COMPND 7 CHAIN: LLL; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS ----, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.M.ORR,H.FISHER,I.TEWS JRNL AUTH C.M.ORR,H.FISHER,Y.GAO,C.CHAN,P.DURIEZ,I.MOCKERIDGE, JRNL AUTH 2 C.PENFOLD,A.L.WHITE,X.YU,A.R.PEARSON,M.S.CRAGG,I.TEWS JRNL TITL A COVALENT ACTIVITY SWITCH MECHANISM IN IGG2 ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 128.19 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 45413 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.875 REMARK 3 FREE R VALUE TEST SET COUNT : 2214 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) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3109 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.26 REMARK 3 BIN R VALUE (WORKING SET) : 0.2130 REMARK 3 BIN FREE R VALUE SET COUNT : 162 REMARK 3 BIN FREE R VALUE : 0.2200 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3315 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 401 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.55 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.01700 REMARK 3 B22 (A**2) : 0.01700 REMARK 3 B33 (A**2) : -0.05600 REMARK 3 B12 (A**2) : 0.00900 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): 0.126 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3609 ; 0.011 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3134 ; 0.037 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4942 ; 1.699 ; 1.645 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7359 ; 2.577 ; 1.568 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 477 ; 7.891 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 156 ;38.433 ;24.359 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 580 ;13.261 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;19.972 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 487 ; 0.080 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4138 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 717 ; 0.012 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 554 ; 0.189 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 55 ; 0.184 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1626 ; 0.164 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 355 ; 0.194 ; 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): 1853 ; 2.632 ; 2.736 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1852 ; 2.631 ; 2.736 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2339 ; 3.710 ; 4.075 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2340 ; 3.709 ; 4.075 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1756 ; 3.377 ; 3.097 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1757 ; 3.376 ; 3.098 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2600 ; 5.040 ; 4.489 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2601 ; 5.039 ; 4.489 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 6TKD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292104719. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-JUL-16 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 : 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) : 0.976 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 : 45431 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 128.190 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 6.900 REMARK 200 R MERGE (I) : 0.10900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94 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 : 2.500 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: 6FAX REMARK 200 REMARK 200 REMARK: NEEDLE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM SULPHATE, PH 7.5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3610 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: HHH, LLL 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH H 392 LIES ON A SPECIAL POSITION. 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 GLY H 103 REMARK 465 ARG H 104 REMARK 465 SER H 139 REMARK 465 THR H 140 REMARK 465 SER H 228 REMARK 465 PRO H 229 REMARK 465 PRO H 230 REMARK 465 CYS H 231 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 HIS H 41 CG ND1 CD2 CE1 NE2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 ARG H 138 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 223 CD CE NZ REMARK 470 ASP L 1 N REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOHHH 472 O HOHLL 488 1.81 REMARK 500 O HOHHH 408 O HOHHH 477 1.96 REMARK 500 O HOHHH 339 O HOHHH 366 2.05 REMARK 500 O HOHHH 354 O HOHHH 454 2.08 REMARK 500 O HOHHH 419 O HOHHH 427 2.12 REMARK 500 OE1 GLUHH 46 O HOHHH 301 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLULL 81 CD GLULL 81 OE1 0.070 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 ARGLL 142 NE - CZ - NH1 ANGL. DEV. = 3.2 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 HISHH 41 -75.48 -19.42 REMARK 500 LYSHH 43 -169.96 -126.51 REMARK 500 ASPHH 153 61.64 66.98 REMARK 500 THRHH 200 -26.21 89.24 REMARK 500 THRLL 51 -47.68 76.60 REMARK 500 THRLL 51 -49.16 76.60 REMARK 500 ALALL 84 173.21 177.12 REMARK 500 REMARK 500 REMARK: NULL DBREF 6TKDHH 1 231 PDB 6TKD 6TKD 1 231 DBREF 6TKDLL 1 214 PDB 6TKD 6TKD 1 214 SEQRES 1HH 231 GLU VAL GLN LEU GLN GLN SER GLY PRO ASP LEU VAL LYS SEQRES 2HH 231 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3HH 231 TYR THR PHE THR GLU TYR ILE MET HIS TRP VAL LYS GLN SEQRES 4HH 231 SER HIS GLY LYS SER LEU GLU TRP ILE GLY GLY ILE ILE SEQRES 5HH 231 PRO ASN ASN GLY GLY THR SER TYR ASN GLN LYS PHE LYS SEQRES 6HH 231 ASP LYS ALA THR MET THR VAL ASP LYS SER SER SER THR SEQRES 7HH 231 GLY TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8HH 231 ALA VAL TYR TYR CYS THR ARG ARG GLU VAL TYR GLY ARG SEQRES 9HH 231 ASN TYR TYR ALA LEU ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10HH 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11HH 231 PHE PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER SEQRES 12HH 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13HH 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14HH 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15HH 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16HH 231 SER ASN PHE GLY THR GLN THR TYR THR CYS ASN VAL ASP SEQRES 17HH 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS THR VAL GLU SEQRES 18HH 231 ARG LYS CYS CYS VAL GLU SER PRO PRO CYS SEQRES 1LL 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2LL 214 SER LEU GLY ASP ARG VAL THR ILE THR CYS SER ALA SER SEQRES 3LL 214 GLN GLY ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4LL 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5LL 214 SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6LL 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7LL 214 GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8LL 214 SER ASN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9LL 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10LL 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11LL 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12LL 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13LL 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14LL 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15LL 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16LL 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17LL 214 PHE ASN ARG GLY GLU CYS FORMUL 3 HOH *401(H2 O) HELIX 1 AA1 THRHH 28 TYRHH 32 5 5 HELIX 2 AA2 GLNHH 62 LYSHH 65 5 4 HELIX 3 AA3 LYSHH 74 SERHH 76 5 3 HELIX 4 AA4 THRHH 87 SERHH 91 5 5 HELIX 5 AA5 SERHH 165 ALAHH 167 5 3 HELIX 6 AA6 SERHH 196 GLNHH 201 5 6 HELIX 7 AA7 LYSHH 210 ASNHH 213 5 4 HELIX 8 AA8 GLULL 79 ILELL 83 5 5 HELIX 9 AA9 SERLL 121 LYSLL 126 1 6 HELIX 10 AB1 LYSLL 183 LYSLL 188 1 6 SHEET 1 AA1 4 GLNHH 3 GLNHH 6 0 SHEET 2 AA1 4 VALHH 18 SERHH 25 -1 O LYSHH 23 N GLNHH 5 SHEET 3 AA1 4 THRHH 78 LEUHH 83 -1 O METHH 81 N ILEHH 20 SHEET 4 AA1 4 ALAHH 68 ASPHH 73 -1 N THRHH 71 O TYRHH 80 SHEET 1 AA2 6 ASPHH 10 VALHH 12 0 SHEET 2 AA2 6 THRHH 116 VALHH 120 1 O THRHH 119 N ASPHH 10 SHEET 3 AA2 6 ALAHH 92 VALHH 101 -1 N ALAHH 92 O VALHH 118 SHEET 4 AA2 6 METHH 34 GLNHH 39 -1 N GLNHH 39 O VALHH 93 SHEET 5 AA2 6 LEUHH 45 ILEHH 51 -1 O GLYHH 49 N TRPHH 36 SHEET 6 AA2 6 THRHH 58 TYRHH 60 -1 O SERHH 59 N GLYHH 50 SHEET 1 AA3 4 ASPHH 10 VALHH 12 0 SHEET 2 AA3 4 THRHH 116 VALHH 120 1 O THRHH 119 N ASPHH 10 SHEET 3 AA3 4 ALAHH 92 VALHH 101 -1 N ALAHH 92 O VALHH 118 SHEET 4 AA3 4 TYRHH 107 TRPHH 112 -1 O ALAHH 108 N GLUHH 100 SHEET 1 AA4 4 SERHH 129 LEUHH 133 0 SHEET 2 AA4 4 THRHH 144 TYRHH 154 -1 O LYSHH 152 N SERHH 129 SHEET 3 AA4 4 TYRHH 185 PROHH 194 -1 O TYRHH 185 N TYRHH 154 SHEET 4 AA4 4 VALHH 172 THRHH 174 -1 N HISHH 173 O VALHH 190 SHEET 1 AA5 4 SERHH 129 LEUHH 133 0 SHEET 2 AA5 4 THRHH 144 TYRHH 154 -1 O LYSHH 152 N SERHH 129 SHEET 3 AA5 4 TYRHH 185 PROHH 194 -1 O TYRHH 185 N TYRHH 154 SHEET 4 AA5 4 VALHH 178 LEUHH 179 -1 N VALHH 178 O SERHH 186 SHEET 1 AA6 3 THRHH 160 TRPHH 163 0 SHEET 2 AA6 3 THRHH 204 HISHH 209 -1 O ASNHH 206 N SERHH 162 SHEET 3 AA6 3 THRHH 214 THRHH 219 -1 O VALHH 216 N VALHH 207 SHEET 1 AA7 4 METLL 4 THRLL 5 0 SHEET 2 AA7 4 VALLL 19 ALALL 25 -1 O SERLL 24 N THRLL 5 SHEET 3 AA7 4 ASPLL 70 ILELL 75 -1 O TYRLL 71 N CYSLL 23 SHEET 4 AA7 4 PHELL 62 SERLL 67 -1 N SERLL 63 O THRLL 74 SHEET 1 AA8 6 SERLL 10 SERLL 14 0 SHEET 2 AA8 6 THRLL 102 LYSLL 107 1 O LYSLL 103 N LEULL 11 SHEET 3 AA8 6 THRLL 85 GLNLL 90 -1 N TYRLL 86 O THRLL 102 SHEET 4 AA8 6 LEULL 33 GLNLL 38 -1 N GLNLL 38 O THRLL 85 SHEET 5 AA8 6 VALLL 44 TYRLL 49 -1 O LEULL 47 N TRPLL 35 SHEET 6 AA8 6 SERLL 53 LEULL 54 -1 O SERLL 53 N TYRLL 49 SHEET 1 AA9 4 SERLL 10 SERLL 14 0 SHEET 2 AA9 4 THRLL 102 LYSLL 107 1 O LYSLL 103 N LEULL 11 SHEET 3 AA9 4 THRLL 85 GLNLL 90 -1 N TYRLL 86 O THRLL 102 SHEET 4 AA9 4 THRLL 97 PHELL 98 -1 O THRLL 97 N GLNLL 90 SHEET 1 AB1 4 SERLL 114 PHELL 118 0 SHEET 2 AB1 4 THRLL 129 PHELL 139 -1 O VALLL 133 N PHELL 118 SHEET 3 AB1 4 TYRLL 173 SERLL 182 -1 O SERLL 177 N CYSLL 134 SHEET 4 AB1 4 SERLL 159 VALLL 163 -1 N SERLL 162 O SERLL 176 SHEET 1 AB2 4 ALALL 153 LEULL 154 0 SHEET 2 AB2 4 LYSLL 145 VALLL 150 -1 N VALLL 150 O ALALL 153 SHEET 3 AB2 4 VALLL 191 THRLL 197 -1 O GLULL 195 N GLNLL 147 SHEET 4 AB2 4 VALLL 205 ASNLL 210 -1 O VALLL 205 N VALLL 196 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.09 SSBOND 2 CYSHH 136 CYSHH 225 1555 5555 2.17 SSBOND 3 CYSHH 149 CYSHH 205 1555 1555 2.05 SSBOND 4 CYSLL 23 CYSLL 88 1555 1555 2.14 SSBOND 5 CYSLL 134 CYSLL 194 1555 1555 2.01 CISPEP 1 PHEHH 155 PROHH 156 0 -3.01 CISPEP 2 GLUHH 157 PROHH 158 0 -2.27 CISPEP 3 GLUHH 157 PROHH 158 0 -4.04 CISPEP 4 LEULL 94 PROLL 95 0 -1.34 CISPEP 5 TYRLL 140 PROLL 141 0 3.79 CRYST1 148.021 148.021 46.139 90.00 90.00 120.00 P 3 2 1 6 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 0.006756 0.003900 0.000000 0.00000 SCALE2 0.000000 0.007801 0.000000 0.00000 SCALE3 0.000000 0.000000 0.021674 0.00000