HEADER IMMUNE SYSTEM 28-NOV-19 6TKB TITLE CHILOB 7/4 H2 HC-C224S F(AB')2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHILOB 7/4 H2 HEAVY CHAIN C224S; COMPND 3 CHAIN: HHH, III; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CHILOB 7/4 H2 KAPPA CHAIN; COMPND 7 CHAIN: LLL, MMM; 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 IMMUNOLOGY, ANTIBODY, IGG, IGG2, 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. 2.00 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) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.64 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 73078 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) : 0.182 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.952 REMARK 3 FREE R VALUE TEST SET COUNT : 3619 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5085 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79 REMARK 3 BIN R VALUE (WORKING SET) : 0.2490 REMARK 3 BIN FREE R VALUE SET COUNT : 250 REMARK 3 BIN FREE R VALUE : 0.3010 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6703 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 457 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.68 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.18500 REMARK 3 B22 (A**2) : 1.47700 REMARK 3 B33 (A**2) : -0.29200 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): 0.156 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150 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 : 0.964 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6867 ; 0.010 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 6055 ; 0.037 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9345 ; 1.615 ; 1.647 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14183 ; 2.434 ; 1.571 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 873 ; 8.338 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 294 ;33.483 ;23.776 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1125 ;13.818 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;18.145 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 926 ; 0.071 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7669 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1354 ; 0.010 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1064 ; 0.188 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 39 ; 0.186 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3302 ; 0.162 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 457 ; 0.162 ; 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): 3504 ; 3.718 ; 4.391 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3503 ; 3.718 ; 4.390 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4373 ; 5.042 ; 6.563 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4374 ; 5.041 ; 6.565 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3363 ; 4.425 ; 4.815 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3362 ; 4.411 ; 4.814 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4972 ; 6.493 ; 7.031 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4972 ; 6.493 ; 7.031 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 : NULL 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 6TKB 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_1292104741. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-FEB-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID30B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.8 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 : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76835 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 47.641 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 29.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 25.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04 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 : 2.300 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: IRREGULAR ROD WITH CENTRAL NEEDLE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CACODYLATE, PH 6, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K 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 37.37900 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.24450 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.59550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.24450 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.37900 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.59550 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 3860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19760 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 350 REMARK 350 BIOMOLECULE: 2 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: 3390 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: III, MMM 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 H 228 REMARK 465 PRO H 229 REMARK 465 PRO H 230 REMARK 465 CYS H 231 REMARK 465 TYR I 102 REMARK 465 GLY I 103 REMARK 465 ARG I 104 REMARK 465 ASN I 105 REMARK 465 TYR I 106 REMARK 465 TYR I 107 REMARK 465 CYS I 228 REMARK 465 PRO I 229 REMARK 465 PRO I 230 REMARK 465 CYS I 231 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 VAL I 101 CG1 CG2 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 HD1 HISII 35 HE1 TRPII 47 1.06 REMARK 500 O LYSMM 190 H ARGMM 211 1.45 REMARK 500 H LEUII 4 O HOHII 310 1.56 REMARK 500 H VALMM 19 O ILEMM 75 1.56 REMARK 500 O HOHHH 346 O HOHHH 456 2.13 REMARK 500 O HOHLL 383 O HOHLL 431 2.13 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 TYRLL 96 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 TYRLL 96 CB - CG - CD1 ANGL. DEV. = 4.0 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 ASNHH 105 34.06 -144.06 REMARK 500 THRHH 169 -41.48 -130.94 REMARK 500 THRLL 51 -44.68 72.23 REMARK 500 THRLL 51 -44.80 72.23 REMARK 500 SERLL 52 -5.36 -140.83 REMARK 500 ASNLL 138 67.23 62.54 REMARK 500 ASNLL 152 -8.30 76.45 REMARK 500 LYSLL 169 -65.37 -101.09 REMARK 500 ASPII 153 55.15 72.29 REMARK 500 THRMM 51 -46.05 78.19 REMARK 500 SERMM 52 -13.41 -144.79 REMARK 500 ASNMM 152 -14.58 68.42 REMARK 500 LYSMM 188 31.10 -96.01 REMARK 500 REMARK 500 REMARK: NULL DBREF 6TKBHH 1 231 PDB 6TKB 6TKB 1 231 DBREF 6TKBLL 1 214 PDB 6TKB 6TKB 1 214 DBREF 6TKBII 1 231 PDB 6TKB 6TKB 1 231 DBREF 6TKBMM 1 214 PDB 6TKB 6TKB 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 SER CYS VAL GLU CYS 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 SEQRES 1II 231 GLU VAL GLN LEU GLN GLN SER GLY PRO ASP LEU VAL LYS SEQRES 2II 231 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3II 231 TYR THR PHE THR GLU TYR ILE MET HIS TRP VAL LYS GLN SEQRES 4II 231 SER HIS GLY LYS SER LEU GLU TRP ILE GLY GLY ILE ILE SEQRES 5II 231 PRO ASN ASN GLY GLY THR SER TYR ASN GLN LYS PHE LYS SEQRES 6II 231 ASP LYS ALA THR MET THR VAL ASP LYS SER SER SER THR SEQRES 7II 231 GLY TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8II 231 ALA VAL TYR TYR CYS THR ARG ARG GLU VAL TYR GLY ARG SEQRES 9II 231 ASN TYR TYR ALA LEU ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10II 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11II 231 PHE PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER SEQRES 12II 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13II 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14II 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15II 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16II 231 SER ASN PHE GLY THR GLN THR TYR THR CYS ASN VAL ASP SEQRES 17II 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS THR VAL GLU SEQRES 18II 231 ARG LYS SER CYS VAL GLU CYS PRO PRO CYS SEQRES 1MM 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2MM 214 SER LEU GLY ASP ARG VAL THR ILE THR CYS SER ALA SER SEQRES 3MM 214 GLN GLY ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4MM 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5MM 214 SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6MM 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7MM 214 GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8MM 214 SER ASN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9MM 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10MM 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11MM 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12MM 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13MM 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14MM 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15MM 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16MM 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17MM 214 PHE ASN ARG GLY GLU CYS FORMUL 5 HOH *457(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 ASNHH 197 GLNHH 201 5 5 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 HELIX 11 AB2 THRII 28 THRII 30 5 3 HELIX 12 AB3 GLNII 62 LYSII 65 5 4 HELIX 13 AB4 LYSII 74 SERII 76 5 3 HELIX 14 AB5 THRII 87 SERII 91 5 5 HELIX 15 AB6 SERII 165 ALAII 167 5 3 HELIX 16 AB7 SERII 196 GLNII 201 5 6 HELIX 17 AB8 LYSII 210 ASNII 213 5 4 HELIX 18 AB9 GLUMM 79 ILEMM 83 5 5 HELIX 19 AC1 SERMM 121 LYSMM 126 1 6 HELIX 20 AC2 LYSMM 183 LYSMM 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 TYRHH 102 -1 N ALAHH 92 O VALHH 118 SHEET 4 AA2 6 ILEHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 95 SHEET 5 AA2 6 LEUHH 45 ILEHH 51 -1 O GLUHH 46 N LYSHH 38 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 TYRHH 102 -1 N ALAHH 92 O VALHH 118 SHEET 4 AA3 4 TYRHH 106 TRPHH 112 -1 O TYRHH 106 N TYRHH 102 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 LEUHH 187 N VALHH 151 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 LEUHH 187 N VALHH 151 SHEET 4 AA5 4 VALHH 178 LEUHH 179 -1 N VALHH 178 O SERHH 186 SHEET 1 AA6 2 SERHH 137 ARGHH 138 0 SHEET 2 AA6 2 CYSHH 225 VALHH 226 1 O CYSHH 225 N ARGHH 138 SHEET 1 AA7 3 THRHH 160 TRPHH 163 0 SHEET 2 AA7 3 THRHH 204 HISHH 209 -1 O ASNHH 206 N SERHH 162 SHEET 3 AA7 3 THRHH 214 THRHH 219 -1 O VALHH 216 N VALHH 207 SHEET 1 AA8 4 METLL 4 THRLL 5 0 SHEET 2 AA8 4 VALLL 19 ALALL 25 -1 O SERLL 24 N THRLL 5 SHEET 3 AA8 4 ASPLL 70 ILELL 75 -1 O TYRLL 71 N CYSLL 23 SHEET 4 AA8 4 PHELL 62 SERLL 67 -1 N SERLL 63 O THRLL 74 SHEET 1 AA9 6 SERLL 10 ALALL 13 0 SHEET 2 AA9 6 THRLL 102 ILELL 106 1 O LYSLL 103 N LEULL 11 SHEET 3 AA9 6 ALALL 84 GLNLL 90 -1 N TYRLL 86 O THRLL 102 SHEET 4 AA9 6 LEULL 33 GLNLL 38 -1 N GLNLL 38 O THRLL 85 SHEET 5 AA9 6 VALLL 44 TYRLL 49 -1 O ILELL 48 N TRPLL 35 SHEET 6 AA9 6 SERLL 53 LEULL 54 -1 O SERLL 53 N TYRLL 49 SHEET 1 AB1 4 SERLL 10 ALALL 13 0 SHEET 2 AB1 4 THRLL 102 ILELL 106 1 O LYSLL 103 N LEULL 11 SHEET 3 AB1 4 ALALL 84 GLNLL 90 -1 N TYRLL 86 O THRLL 102 SHEET 4 AB1 4 THRLL 97 PHELL 98 -1 O THRLL 97 N GLNLL 90 SHEET 1 AB2 4 SERLL 114 PHELL 118 0 SHEET 2 AB2 4 THRLL 129 PHELL 139 -1 O ASNLL 137 N SERLL 114 SHEET 3 AB2 4 TYRLL 173 SERLL 182 -1 O LEULL 179 N VALLL 132 SHEET 4 AB2 4 SERLL 159 VALLL 163 -1 N GLNLL 160 O THRLL 178 SHEET 1 AB3 4 ALALL 153 LEULL 154 0 SHEET 2 AB3 4 LYSLL 145 VALLL 150 -1 N VALLL 150 O ALALL 153 SHEET 3 AB3 4 VALLL 191 THRLL 197 -1 O GLULL 195 N GLNLL 147 SHEET 4 AB3 4 VALLL 205 ASNLL 210 -1 O VALLL 205 N VALLL 196 SHEET 1 AB4 4 GLNII 3 GLNII 6 0 SHEET 2 AB4 4 VALII 18 SERII 25 -1 O LYSII 23 N GLNII 5 SHEET 3 AB4 4 THRII 78 LEUII 83 -1 O LEUII 83 N VALII 18 SHEET 4 AB4 4 ALAII 68 ASPII 73 -1 N THRII 71 O TYRII 80 SHEET 1 AB5 6 ASPII 10 VALII 12 0 SHEET 2 AB5 6 THRII 116 VALII 120 1 O THRII 119 N ASPII 10 SHEET 3 AB5 6 ALAII 92 GLUII 100 -1 N ALAII 92 O VALII 118 SHEET 4 AB5 6 TYRII 32 GLNII 39 -1 N VALII 37 O TYRII 95 SHEET 5 AB5 6 LEUII 45 ILEII 52 -1 O GLUII 46 N LYSII 38 SHEET 6 AB5 6 GLYII 57 TYRII 60 -1 O GLYII 57 N ILEII 52 SHEET 1 AB6 4 SERII 129 LEUII 133 0 SHEET 2 AB6 4 THRII 144 TYRII 154 -1 O LYSII 152 N SERII 129 SHEET 3 AB6 4 TYRII 185 PROII 194 -1 O LEUII 187 N VALII 151 SHEET 4 AB6 4 VALII 172 THRII 174 -1 N HISII 173 O VALII 190 SHEET 1 AB7 4 SERII 129 LEUII 133 0 SHEET 2 AB7 4 THRII 144 TYRII 154 -1 O LYSII 152 N SERII 129 SHEET 3 AB7 4 TYRII 185 PROII 194 -1 O LEUII 187 N VALII 151 SHEET 4 AB7 4 VALII 178 LEUII 179 -1 N VALII 178 O SERII 186 SHEET 1 AB8 3 THRII 160 TRPII 163 0 SHEET 2 AB8 3 THRII 204 HISII 209 -1 O ASNII 206 N SERII 162 SHEET 3 AB8 3 THRII 214 THRII 219 -1 O THRII 214 N HISII 209 SHEET 1 AB9 4 METMM 4 THRMM 5 0 SHEET 2 AB9 4 VALMM 19 ALAMM 25 -1 O SERMM 24 N THRMM 5 SHEET 3 AB9 4 ASPMM 70 ILEMM 75 -1 O ILEMM 75 N VALMM 19 SHEET 4 AB9 4 PHEMM 62 SERMM 67 -1 N SERMM 63 O THRMM 74 SHEET 1 AC1 6 SERMM 10 ALAMM 13 0 SHEET 2 AC1 6 THRMM 102 ILEMM 106 1 O LYSMM 103 N LEUMM 11 SHEET 3 AC1 6 ALAMM 84 GLNMM 90 -1 N ALAMM 84 O LEUMM 104 SHEET 4 AC1 6 LEUMM 33 GLNMM 38 -1 N GLNMM 38 O THRMM 85 SHEET 5 AC1 6 VALMM 44 TYRMM 49 -1 O LYSMM 45 N GLNMM 37 SHEET 6 AC1 6 SERMM 53 LEUMM 54 -1 O SERMM 53 N TYRMM 49 SHEET 1 AC2 4 SERMM 10 ALAMM 13 0 SHEET 2 AC2 4 THRMM 102 ILEMM 106 1 O LYSMM 103 N LEUMM 11 SHEET 3 AC2 4 ALAMM 84 GLNMM 90 -1 N ALAMM 84 O LEUMM 104 SHEET 4 AC2 4 THRMM 97 PHEMM 98 -1 O THRMM 97 N GLNMM 90 SHEET 1 AC3 4 SERMM 114 PHEMM 118 0 SHEET 2 AC3 4 THRMM 129 PHEMM 139 -1 O ASNMM 137 N SERMM 114 SHEET 3 AC3 4 TYRMM 173 SERMM 182 -1 O TYRMM 173 N PHEMM 139 SHEET 4 AC3 4 SERMM 159 VALMM 163 -1 N SERMM 162 O SERMM 176 SHEET 1 AC4 4 ALAMM 153 LEUMM 154 0 SHEET 2 AC4 4 LYSMM 145 VALMM 150 -1 N VALMM 150 O ALAMM 153 SHEET 3 AC4 4 VALMM 191 THRMM 197 -1 O GLUMM 195 N GLNMM 147 SHEET 4 AC4 4 VALMM 205 ASNMM 210 -1 O VALMM 205 N VALMM 196 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.15 SSBOND 2 CYSHH 136 CYSLL 214 1555 1555 2.05 SSBOND 3 CYSHH 149 CYSHH 205 1555 1555 2.08 SSBOND 4 CYSHH 225 CYSII 225 1555 1555 2.06 SSBOND 5 CYSLL 23 CYSLL 88 1555 1555 2.20 SSBOND 6 CYSLL 134 CYSLL 194 1555 1555 2.09 SSBOND 7 CYSII 22 CYSII 96 1555 1555 2.09 SSBOND 8 CYSII 136 CYSMM 214 1555 1555 2.05 SSBOND 9 CYSII 149 CYSII 205 1555 1555 2.04 SSBOND 10 CYSMM 23 CYSMM 88 1555 1555 2.15 SSBOND 11 CYSMM 134 CYSMM 194 1555 1555 2.08 CISPEP 1 PHEHH 155 PROHH 156 0 -8.36 CISPEP 2 GLUHH 157 PROHH 158 0 -1.06 CISPEP 3 LEULL 94 PROLL 95 0 -1.95 CISPEP 4 TYRLL 140 PROLL 141 0 6.81 CISPEP 5 PHEII 155 PROII 156 0 -7.16 CISPEP 6 GLUII 157 PROII 158 0 -5.26 CISPEP 7 LEUMM 94 PROMM 95 0 -5.77 CISPEP 8 TYRMM 140 PROMM 141 0 4.65 CRYST1 74.758 95.191 150.489 90.00 90.00 90.00 P 21 21 21 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 0.013376 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010505 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006645 0.00000