HEADER IMMUNE SYSTEM 29-JUN-20 6ZJG TITLE CRYSTAL STRUCTURE OF ACPA E4 IN COMPLEX WITH CII-C-48-CIT COMPND MOL_ID: 1; COMPND 2 MOLECULE: CII-C-48-CIT; COMPND 3 CHAIN: CCC; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ACPA E4 FAB FRAGMENT - HEAVY CHAIN; COMPND 7 CHAIN: HHH; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ACPA E4 FAB FRAGMENT - LIGHT CHAIN; COMPND 11 CHAIN: LLL; COMPND 12 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 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: EXPI 293F(TM); SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PCEP4; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: EXPI 293F(TM); SOURCE 25 EXPRESSION_SYSTEM_PLASMID: PCEP4 KEYWDS ANTI-CITRULLINATED PROTEIN ANTIBODY FAB FRAGMENT, CITRULLINATED KEYWDS 2 COLLAGEN TYPE II, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.GE,R.HOLMDAHL JRNL AUTH C.GE,H.RIKARD JRNL TITL CRYSTAL STRUCTURE OF ACPA E4 IN COMPLEX WITH CII-C-48-CIT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.45 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) : 2.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.89 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 21353 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.287 REMARK 3 FREE R VALUE TEST SET COUNT : 1129 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) : 2.45 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1479 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.74 REMARK 3 BIN R VALUE (WORKING SET) : 0.2940 REMARK 3 BIN FREE R VALUE SET COUNT : 77 REMARK 3 BIN FREE R VALUE : 0.3330 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3277 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 39 REMARK 3 SOLVENT ATOMS : 45 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.54 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.07600 REMARK 3 B22 (A**2) : -0.46200 REMARK 3 B33 (A**2) : 0.53900 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): 0.392 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.270 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.210 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.828 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3407 ; 0.008 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3039 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4656 ; 1.626 ; 1.664 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7098 ; 1.188 ; 1.582 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 430 ; 8.202 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;33.153 ;22.059 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 507 ;16.652 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.621 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 466 ; 0.064 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3763 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 687 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 472 ; 0.192 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 20 ; 0.269 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1562 ; 0.163 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 79 ; 0.166 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.242 ; 0.200 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): 1738 ; 1.618 ; 3.676 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1737 ; 1.618 ; 3.674 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2162 ; 2.627 ; 5.504 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2163 ; 2.627 ; 5.507 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1669 ; 1.701 ; 3.791 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1670 ; 1.701 ; 3.791 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2494 ; 2.587 ; 5.615 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2495 ; 2.586 ; 5.615 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 : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : CC 4 CC 12 REMARK 3 ORIGIN FOR THE GROUP (A): 28.6837 36.3179 17.4662 REMARK 3 T TENSOR REMARK 3 T11: 0.6427 T22: 0.4824 REMARK 3 T33: 0.5596 T12: 0.0016 REMARK 3 T13: -0.0449 T23: -0.1401 REMARK 3 L TENSOR REMARK 3 L11: 0.6863 L22: 0.0371 REMARK 3 L33: 4.4746 L12: 0.0636 REMARK 3 L13: 1.7385 L23: 0.1924 REMARK 3 S TENSOR REMARK 3 S11: -0.1962 S12: -0.0024 S13: 0.0669 REMARK 3 S21: 0.0792 S22: 0.0794 S23: 0.0103 REMARK 3 S31: -0.4907 S32: 0.1781 S33: 0.1168 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : HH 2 HH 221 REMARK 3 ORIGIN FOR THE GROUP (A): 13.7611 18.6185 -6.0252 REMARK 3 T TENSOR REMARK 3 T11: 0.1818 T22: 0.0427 REMARK 3 T33: 0.2131 T12: 0.0058 REMARK 3 T13: -0.0614 T23: 0.0266 REMARK 3 L TENSOR REMARK 3 L11: 1.9451 L22: 2.6092 REMARK 3 L33: 3.1857 L12: -0.1580 REMARK 3 L13: 1.4860 L23: 0.8239 REMARK 3 S TENSOR REMARK 3 S11: -0.1769 S12: -0.2239 S13: 0.1531 REMARK 3 S21: 0.2866 S22: 0.0075 S23: 0.0144 REMARK 3 S31: -0.3238 S32: -0.2479 S33: 0.1695 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : LL 1 LL 216 REMARK 3 ORIGIN FOR THE GROUP (A): 30.5928 18.5331 -7.8639 REMARK 3 T TENSOR REMARK 3 T11: 0.1323 T22: 0.0676 REMARK 3 T33: 0.2610 T12: -0.0755 REMARK 3 T13: -0.1014 T23: 0.1175 REMARK 3 L TENSOR REMARK 3 L11: 1.6015 L22: 1.7380 REMARK 3 L33: 4.2881 L12: -0.5035 REMARK 3 L13: 1.0546 L23: -0.2223 REMARK 3 S TENSOR REMARK 3 S11: -0.1821 S12: 0.0996 S13: 0.3031 REMARK 3 S21: 0.1175 S22: -0.1762 S23: -0.3714 REMARK 3 S31: -0.5853 S32: 0.3397 S33: 0.3582 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 6ZJG 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_1292109533. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-SEP-16 REMARK 200 TEMPERATURE (KELVIN) : 293 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) : 0.97625 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS 0.7.4, XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21382 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450 REMARK 200 RESOLUTION RANGE LOW (A) : 97.070 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 9.200 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 8.83 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 97.07 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 8.20 REMARK 200 R MERGE FOR SHELL (I) : 0.03500 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: NULL REMARK 200 STARTING MODEL: 5OCY(EARLY MODEL) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: (20% (W/V) PEG 3350, 0.1M BIS-TRIS REMARK 280 PROPANE, PH 6.5, 0.2M POTASSIUM THIOCYANATE, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 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 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.53300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.53300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 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 38.59150 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.88700 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.59150 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.88700 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.53300 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.59150 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 75.88700 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.53300 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.59150 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 75.88700 REMARK 290 SMTRY3 8 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: CCC, HHH, LLL, 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 CYS C 0 REMARK 465 GLU C 1 REMARK 465 ALA C 2 REMARK 465 GLY C 3 REMARK 465 CIR C 8 REMARK 465 HIS C 13 REMARK 465 ARG C 14 REMARK 465 GLY C 15 REMARK 465 CYS C 16 REMARK 465 ALA C 17 REMARK 465 GLN H 1 REMARK 465 SER H 165 REMARK 465 LEU H 166 REMARK 465 SER H 167 REMARK 465 SER H 168 REMARK 465 GLY L 24 REMARK 465 ASP L 25 REMARK 465 CYS L 215 REMARK 465 SER L 216 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 H GLYCC 9 C1 CIRCC 101 1.08 REMARK 500 H2 GLNLL 1 HD21 ASNLL 93 1.31 REMARK 500 C GLUCC 7 HN21 CIRCC 101 1.36 REMARK 500 C GLUCC 7 HN22 CIRCC 101 1.36 REMARK 500 HH22 ARGLL 81 O HOHLL 401 1.38 REMARK 500 H SERHH 156 O HOHHH 303 1.58 REMARK 500 O GLUCC 7 N2 CIRCC 101 2.02 REMARK 500 NH2 ARGLL 81 O HOHLL 401 2.04 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 SERHH 15 -18.56 93.95 REMARK 500 PHEHH 27 131.08 -170.00 REMARK 500 LYSHH 44 -167.46 -109.11 REMARK 500 SERHH 104 -70.07 -65.64 REMARK 500 THRHH 138 35.04 -92.17 REMARK 500 SERHH 179 75.02 2.84 REMARK 500 ASPLL 51 53.53 38.79 REMARK 500 ASPLL 52 -41.53 75.52 REMARK 500 ALALL 91 144.19 -174.26 REMARK 500 SERLL 97 62.18 34.89 REMARK 500 LYSLL 114 136.38 -38.56 REMARK 500 REMARK 500 REMARK: NULL DBREF 6ZJGCC 0 17 PDB 6ZJG 6ZJG 0 17 DBREF 6ZJGHH 1 221 PDB 6ZJG 6ZJG 1 221 DBREF 6ZJGLL 1 216 PDB 6ZJG 6ZJG 1 216 SEQRES 1CC 18 CYS GLU ALA GLY GLU PRO GLY GLU CIR GLY LEU LYS GLY SEQRES 2CC 18 HIS ARG GLY CYS ALA SEQRES 1HH 221 GLN VAL GLN LEU GLU GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2HH 221 PRO SER GLU THR LEU SER LEU SER CYS THR VAL SER GLY SEQRES 3HH 221 PHE PRO MET ASN GLU SER TYR PHE TRP GLY TRP ILE ARG SEQRES 4HH 221 GLN SER PRO GLY LYS GLY LEU GLU TRP LEU GLY SER VAL SEQRES 5HH 221 ILE HIS THR GLY THR THR TYR TYR ARG PRO SER LEU GLU SEQRES 6HH 221 SER ARG LEU THR ILE ALA MET ASP PRO SER LYS ASN GLN SEQRES 7HH 221 VAL SER LEU SER LEU THR SER VAL THR VAL ALA ASP SER SEQRES 8HH 221 ALA MET TYR TYR CYS VAL ARG ILE ARG GLY GLY SER SER SEQRES 9HH 221 ASN TRP LEU ASP PRO TRP GLY PRO GLY ILE VAL VAL THR SEQRES 10HH 221 ALA SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11HH 221 LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL SEQRES 12HH 221 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER SEQRES 13HH 221 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER SEQRES 14HH 221 VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR SEQRES 15HH 221 THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16HH 221 PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA SEQRES 17HH 221 SER SER THR THR VAL ASP LYS LYS ILE GLU PRO ARG PRO SEQRES 1LL 216 GLN SER VAL TRP THR GLN PRO PRO SER VAL SER ALA ALA SEQRES 2LL 216 PRO GLY GLN ASN VAL THR ILE SER CYS SER GLY ASP ASP SEQRES 3LL 216 SER ILE LEU ARG SER ALA PHE VAL SER TRP TYR GLN GLN SEQRES 4LL 216 VAL PRO GLY SER ALA PRO LYS LEU VAL ILE PHE ASP ASP SEQRES 5LL 216 ARG GLN ARG PRO SER GLY ILE PRO ALA ARG PHE SER GLY SEQRES 6LL 216 SER ASN SER GLY THR THR ALA THR LEU ASP ILE ALA GLY SEQRES 7LL 216 LEU GLN ARG GLY ASP GLU ALA ASP TYR TYR CYS ALA ALA SEQRES 8LL 216 TRP ASN GLY ARG LEU SER ALA PHE VAL PHE GLY SER GLY SEQRES 9LL 216 THR LYS LEU THR VAL LEU GLY GLN PRO LYS SER SER PRO SEQRES 10LL 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLU SEQRES 11LL 216 THR ASN LYS ALA THR LEU VAL CYS THR ILE THR ASP PHE SEQRES 12LL 216 TYR PRO GLY VAL VAL THR VAL ASP TRP LYS VAL ASP GLY SEQRES 13LL 216 THR PRO VAL THR GLN GLY MET GLU THR THR GLN PRO SER SEQRES 14LL 216 LYS GLN SER ASN ASN LYS TYR MET ALA SER SER TYR LEU SEQRES 15LL 216 THR LEU THR ALA ARG ALA TRP GLU ARG HIS SER SER TYR SEQRES 16LL 216 SER CYS GLN VAL THR HIS GLU GLY HIS THR VAL GLU LYS SEQRES 17LL 216 SER LEU SER ARG ALA ASP CYS SER HET CIR CC 101 23 HET NAG A 1 27 HET NAG A 2 28 HETNAM CIR CITRULLINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 4 CIR C6 H13 N3 O3 FORMUL 5 NAG 2(C8 H15 N O6) FORMUL 6 HOH *45(H2 O) HELIX 1 AA1 PROHH 62 SERHH 66 5 5 HELIX 2 AA2 PROHH 74 LYSHH 76 5 3 HELIX 3 AA3 THRHH 87 SERHH 91 5 5 HELIX 4 AA4 SERHH 193 TRPHH 195 5 3 HELIX 5 AA5 PROHH 207 SERHH 210 5 4 HELIX 6 AA6 GLNLL 80 GLULL 84 5 5 HELIX 7 AA7 SERLL 125 GLULL 130 1 6 HELIX 8 AA8 ALALL 186 HISLL 192 1 7 SHEET 1 AA1 4 GLNHH 3 SERHH 7 0 SHEET 2 AA1 4 LEUHH 18 SERHH 25 -1 O SERHH 21 N SERHH 7 SHEET 3 AA1 4 GLNHH 78 LEUHH 83 -1 O LEUHH 83 N LEUHH 18 SHEET 4 AA1 4 LEUHH 68 ASPHH 73 -1 N ALAHH 71 O SERHH 80 SHEET 1 AA2 6 LEUHH 11 VALHH 12 0 SHEET 2 AA2 6 ILEHH 114 ALAHH 118 1 O THRHH 117 N VALHH 12 SHEET 3 AA2 6 ALAHH 92 ARGHH 100 -1 N TYRHH 94 O ILEHH 114 SHEET 4 AA2 6 PHEHH 34 GLNHH 40 -1 N PHEHH 34 O ILEHH 99 SHEET 5 AA2 6 LEUHH 46 VALHH 52 -1 O VALHH 52 N TRPHH 35 SHEET 6 AA2 6 THRHH 58 TYRHH 60 -1 O TYRHH 59 N SERHH 51 SHEET 1 AA3 4 LEUHH 11 VALHH 12 0 SHEET 2 AA3 4 ILEHH 114 ALAHH 118 1 O THRHH 117 N VALHH 12 SHEET 3 AA3 4 ALAHH 92 ARGHH 100 -1 N TYRHH 94 O ILEHH 114 SHEET 4 AA3 4 TRPHH 106 TRPHH 110 -1 O ASPHH 108 N ARGHH 98 SHEET 1 AA4 4 SERHH 127 LEUHH 131 0 SHEET 2 AA4 4 SERHH 142 TYRHH 152 -1 O LYSHH 150 N SERHH 127 SHEET 3 AA4 4 LEUHH 181 PROHH 191 -1 O VALHH 188 N LEUHH 145 SHEET 4 AA4 4 VALHH 170 THRHH 172 -1 N HISHH 171 O SERHH 187 SHEET 1 AA5 4 SERHH 127 LEUHH 131 0 SHEET 2 AA5 4 SERHH 142 TYRHH 152 -1 O LYSHH 150 N SERHH 127 SHEET 3 AA5 4 LEUHH 181 PROHH 191 -1 O VALHH 188 N LEUHH 145 SHEET 4 AA5 4 LEUHH 176 GLNHH 178 -1 N GLNHH 178 O LEUHH 181 SHEET 1 AA6 3 THRHH 158 TRPHH 161 0 SHEET 2 AA6 3 THRHH 201 HISHH 206 -1 O SERHH 203 N THRHH 160 SHEET 3 AA6 3 THRHH 211 LYSHH 216 -1 O VALHH 213 N VALHH 204 SHEET 1 AA7 5 SERLL 9 ALALL 12 0 SHEET 2 AA7 5 THRLL 105 VALLL 109 1 O LYSLL 106 N VALLL 10 SHEET 3 AA7 5 ALALL 85 ASNLL 93 -1 N TYRLL 87 O THRLL 105 SHEET 4 AA7 5 SERLL 35 GLNLL 39 -1 N GLNLL 39 O ASPLL 86 SHEET 5 AA7 5 LYSLL 46 ILELL 49 -1 O VALLL 48 N TRPLL 36 SHEET 1 AA8 4 SERLL 9 ALALL 12 0 SHEET 2 AA8 4 THRLL 105 VALLL 109 1 O LYSLL 106 N VALLL 10 SHEET 3 AA8 4 ALALL 85 ASNLL 93 -1 N TYRLL 87 O THRLL 105 SHEET 4 AA8 4 ALALL 98 PHELL 101 -1 O VALLL 100 N ALALL 91 SHEET 1 AA9 3 VALLL 18 CYSLL 22 0 SHEET 2 AA9 3 ALALL 72 ILELL 76 -1 O LEULL 74 N ILELL 20 SHEET 3 AA9 3 PHELL 63 ASNLL 67 -1 N SERLL 64 O ASPLL 75 SHEET 1 AB1 4 SERLL 118 PHELL 122 0 SHEET 2 AB1 4 LYSLL 133 PHELL 143 -1 O VALLL 137 N PHELL 122 SHEET 3 AB1 4 TYRLL 176 THRLL 185 -1 O LEULL 184 N ALALL 134 SHEET 4 AB1 4 METLL 163 THRLL 165 -1 N GLULL 164 O TYRLL 181 SHEET 1 AB2 4 SERLL 118 PHELL 122 0 SHEET 2 AB2 4 LYSLL 133 PHELL 143 -1 O VALLL 137 N PHELL 122 SHEET 3 AB2 4 TYRLL 176 THRLL 185 -1 O LEULL 184 N ALALL 134 SHEET 4 AB2 4 SERLL 169 LYSLL 170 -1 N SERLL 169 O METLL 177 SHEET 1 AB3 4 THRLL 157 PROLL 158 0 SHEET 2 AB3 4 THRLL 149 VALLL 154 -1 N VALLL 154 O THRLL 157 SHEET 3 AB3 4 SERLL 194 HISLL 201 -1 O GLNLL 198 N ASPLL 151 SHEET 4 AB3 4 HISLL 204 SERLL 211 -1 O HISLL 204 N HISLL 201 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.06 SSBOND 2 CYSHH 147 CYSHH 202 1555 1555 2.03 SSBOND 3 CYSLL 22 CYSLL 89 1555 1555 2.06 SSBOND 4 CYSLL 138 CYSLL 197 1555 1555 2.03 LINK C GLUCC 7 N2 CIRCC 101 1555 1555 1.27 LINK N GLYCC 9 C1 CIRCC 101 1555 1555 1.29 LINK ND2 ASNLL 17 C1 NAG A 1 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.45 CISPEP 1 ASPHH 108 PROHH 109 0 -2.57 CISPEP 2 PHEHH 153 PROHH 154 0 -5.36 CISPEP 3 GLUHH 155 SERHH 156 0 -4.47 CISPEP 4 TRPHH 195 PROHH 196 0 7.54 CISPEP 5 TYRLL 144 PROLL 145 0 -2.02 CRYST1 77.183 151.774 97.066 90.00 90.00 90.00 C 2 2 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 0.012956 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006589 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010302 0.00000