HEADER IMMUNE SYSTEM 03-MAY-20 6YXM TITLE CRYSTAL STRUCTURE OF ACPA 1F2 IN COMPLEX WITH CII-C-39-CIT CAVEAT 6YXM NAG A 2 HAS WRONG CHIRALITY AT ATOM C1 BMA A 3 HAS WRONG CAVEAT 2 6YXM CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CII-C-39-CIT; COMPND 3 CHAIN: BBB; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ACPA 1F2 FAB FRAGMENT - HEAVY CHAIN; COMPND 7 CHAIN: HHH; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ACPA 1F2 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_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTI-CITRULLINATED PROTEIN ANTIBODY, COLLAGEN TYPE II, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.GE,R.HOLMDAHL JRNL AUTH C.GE,R.HOLMDAHL JRNL TITL N-LINKED GLYCOSYLATION OF THE IMMUNOGLOBULIN VARIABLE DOMAIN JRNL TITL 2 AFFECTS ANTIGEN BINDING AND AUTOREACTIVE B CELL ACTIVATION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.85 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) : 2.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.22 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 3 NUMBER OF REFLECTIONS : 13539 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) : 0.210 REMARK 3 FREE R VALUE : 0.276 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.712 REMARK 3 FREE R VALUE TEST SET COUNT : 638 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) : 2.85 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92 REMARK 3 REFLECTION IN BIN (WORKING SET) : 939 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.61 REMARK 3 BIN R VALUE (WORKING SET) : 0.2590 REMARK 3 BIN FREE R VALUE SET COUNT : 54 REMARK 3 BIN FREE R VALUE : 0.3570 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3274 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 64 REMARK 3 SOLVENT ATOMS : 33 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.04 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.81000 REMARK 3 B22 (A**2) : 0.63000 REMARK 3 B33 (A**2) : 0.18000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.412 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.283 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.017 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3425 ; 0.004 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3009 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4660 ; 1.333 ; 1.669 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7023 ; 1.122 ; 1.593 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 427 ; 8.123 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 143 ;33.407 ;22.448 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 512 ;16.446 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.154 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 467 ; 0.044 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3790 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 706 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 489 ; 0.185 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 21 ; 0.273 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1588 ; 0.159 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 78 ; 0.117 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.107 ; 0.200 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): 3 ; 0.112 ; 0.200 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): 1726 ; 0.646 ; 2.972 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1725 ; 0.645 ; 2.972 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2147 ; 1.143 ; 4.457 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2148 ; 1.143 ; 4.457 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1699 ; 0.656 ; 3.049 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1700 ; 0.656 ; 3.049 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2513 ; 1.045 ; 4.544 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2514 ; 1.044 ; 4.544 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 : BB 597 BB 605 REMARK 3 ORIGIN FOR THE GROUP (A): 26.0732 14.9513 23.9391 REMARK 3 T TENSOR REMARK 3 T11: 0.2018 T22: 0.2570 REMARK 3 T33: 0.2540 T12: 0.0112 REMARK 3 T13: 0.0845 T23: -0.0553 REMARK 3 L TENSOR REMARK 3 L11: 0.6819 L22: 0.0430 REMARK 3 L33: 1.7948 L12: -0.1361 REMARK 3 L13: 1.0985 L23: -0.2322 REMARK 3 S TENSOR REMARK 3 S11: 0.0507 S12: 0.1869 S13: -0.0849 REMARK 3 S21: -0.0024 S22: 0.0156 S23: -0.0066 REMARK 3 S31: 0.0835 S32: 0.2751 S33: -0.0663 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 1 HH 230 REMARK 3 ORIGIN FOR THE GROUP (A): 5.8350 40.4590 15.7579 REMARK 3 T TENSOR REMARK 3 T11: 0.0272 T22: 0.1162 REMARK 3 T33: 0.0692 T12: -0.0068 REMARK 3 T13: -0.0274 T23: 0.0208 REMARK 3 L TENSOR REMARK 3 L11: 0.6200 L22: 4.3543 REMARK 3 L33: 0.7875 L12: -0.2441 REMARK 3 L13: -0.1323 L23: -0.5282 REMARK 3 S TENSOR REMARK 3 S11: -0.0258 S12: -0.0073 S13: 0.0424 REMARK 3 S21: 0.0341 S22: -0.0094 S23: 0.2153 REMARK 3 S31: -0.1051 S32: -0.1294 S33: 0.0352 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 212 REMARK 3 ORIGIN FOR THE GROUP (A): 21.6387 43.9806 12.7694 REMARK 3 T TENSOR REMARK 3 T11: 0.0590 T22: 0.0407 REMARK 3 T33: 0.1009 T12: 0.0021 REMARK 3 T13: 0.0327 T23: 0.0273 REMARK 3 L TENSOR REMARK 3 L11: 0.3634 L22: 2.9820 REMARK 3 L33: 0.1730 L12: -0.6874 REMARK 3 L13: 0.1150 L23: 0.2337 REMARK 3 S TENSOR REMARK 3 S11: -0.0461 S12: -0.0206 S13: -0.0247 REMARK 3 S21: -0.1862 S22: 0.0238 S23: 0.0238 REMARK 3 S31: -0.0754 S32: -0.0074 S33: 0.0224 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 6YXM 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_1292108467. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-MAR-18 REMARK 200 TEMPERATURE (KELVIN) : 210 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) : 0.97662 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 : AIMLESS, XDS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13893 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850 REMARK 200 RESOLUTION RANGE LOW (A) : 118.750 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 8.800 REMARK 200 R MERGE (I) : 0.14600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 9.01 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 118.7 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 7.70 REMARK 200 R MERGE FOR SHELL (I) : 0.07400 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: 5OCX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM TRIS PH 7.4, 20MMNACL, 20% (W/V) REMARK 280 PEG 6000, 0.1M HEPES 7.0 PH 7.0, 0.01M ZINC CHLORIDE., 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 26.50500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.34000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.82500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.34000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.50500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.82500 REMARK 290 SMTRY3 4 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: 5960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19850 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: BBB, 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 B 600A REMARK 465 ILE B 600B REMARK 465 ARG B 600C REMARK 465 CYS H 137 REMARK 465 GLY H 138 REMARK 465 ASP H 139 REMARK 465 THR H 140 REMARK 465 THR H 141 REMARK 465 GLY H 166 REMARK 465 SER H 167 REMARK 465 LEU H 168 REMARK 465 SER H 169 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 H 120 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 HISHH 84 ZN ZNHH 305 1.08 REMARK 500 HE2 HISHH 82 ZN ZNHH 305 1.10 REMARK 500 HE2 HISHH 173 ZN ZNHH 306 1.19 REMARK 500 C GLNBB 600 HN22 CIRBB 701 1.26 REMARK 500 O4 NAG A 2 H1 BMA A 3 1.27 REMARK 500 H GLYBB 602 C1 CIRBB 701 1.39 REMARK 500 HE2 HISHH 3 ZN ZNHH 307 1.44 REMARK 500 HO4 NAG A 2 C1 BMA A 3 1.44 REMARK 500 O4 NAG A 1 H1 NAG A 2 1.46 REMARK 500 C GLNBB 600 HN21 CIRBB 701 1.52 REMARK 500 O GLNBB 600 N2 CIRBB 701 2.15 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 HD2 HISLL 192 ZN ZNBB 702 3655 1.60 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 ARGBB 604 -133.79 -163.47 REMARK 500 SERHH 7 160.17 -46.38 REMARK 500 TYRHH 27 147.30 -175.92 REMARK 500 THRHH 53 0.40 -65.91 REMARK 500 ALAHH 56 6.88 83.94 REMARK 500 SERHH 108 48.17 -85.58 REMARK 500 PROHH 156 -159.21 -83.77 REMARK 500 CYSLL 22 86.97 -156.64 REMARK 500 VALLL 48 -42.47 -134.61 REMARK 500 ASPLL 52 -51.58 85.98 REMARK 500 ASPLL 53 15.40 -148.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 702 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 603 OE1 REMARK 620 2 GLU B 603 OE2 53.4 REMARK 620 3 ASP L 31 OD1 90.1 84.6 REMARK 620 4 ASP L 31 OD2 79.0 117.4 54.5 REMARK 620 5 ASP L 155 OD2 80.3 129.6 75.8 21.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 307 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 3 NE2 REMARK 620 2 GLU H 5 OE1 112.0 REMARK 620 3 HOH H 401 O 113.9 109.5 REMARK 620 4 ASP L 61 OD1 82.0 165.2 58.2 REMARK 620 5 ASP L 61 OD2 79.0 166.9 58.3 3.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 305 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 82 NE2 REMARK 620 2 HIS H 84 ND1 132.5 REMARK 620 3 HOH H 408 O 97.0 98.7 REMARK 620 4 GLU L 130 OE2 101.4 31.0 105.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 306 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 173 NE2 REMARK 620 2 HOH H 415 O 95.7 REMARK 620 3 ASP L 142 OD1 108.6 114.2 REMARK 620 4 HOH L 303 O 104.2 139.1 92.9 REMARK 620 N 1 2 3 DBREF 6YXMBB 597 605 PDB 6YXM 6YXM 597 605 DBREF 6YXMHH 1 222 PDB 6YXM 6YXM 1 222 DBREF 6YXMLL 1 212 PDB 6YXM 6YXM 1 212 SEQRES 1BB 11 LEU PRO GLY GLN CYS ILE ARG GLY GLU ARG GLY SEQRES 1HH 222 GLN VAL HIS LEU GLU GLN SER GLY SER GLU LEU LYS LYS SEQRES 2HH 222 PRO GLY ALA SER VAL THR ILE SER CYS LYS THR SER GLY SEQRES 3HH 222 TYR ASN PHE SER HIS PHE ALA ILE ASN TRP VAL ARG GLN SEQRES 4HH 222 ALA PRO GLY GLN GLY LEU GLN TRP MET GLY TRP ILE ASN SEQRES 5HH 222 THR LYS THR ALA ASN LEU THR TYR ALA GLN THR PHE THR SEQRES 6HH 222 GLY ARG PHE VAL PHE SER PHE ASP THR SER VAL SER THR SEQRES 7HH 222 ALA TYR LEU HIS ILE HIS GLY LEU LYS THR GLU ASP THR SEQRES 8HH 222 ALA MET TYR TYR CYS VAL ARG GLY GLY SER LEU GLY ILE SEQRES 9HH 222 PHE GLY GLY SER VAL GLY TYR TRP GLY GLN GLY ALA LEU SEQRES 10HH 222 VAL SER VAL SER SER ALA LYS THR THR PRO PRO SER VAL SEQRES 11HH 222 TYR PRO LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SEQRES 12HH 222 SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO SEQRES 13HH 222 GLU SER VAL THR VAL THR TRP ASN SER GLY SER LEU SER SEQRES 14HH 222 SER SER VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY SEQRES 15HH 222 LEU TYR THR MET SER SER SER VAL THR VAL PRO SER SER SEQRES 16HH 222 THR TRP PRO SER GLN THR VAL THR CYS SER VAL ALA HIS SEQRES 17HH 222 PRO ALA SER SER THR THR VAL ASP LYS LYS ILE GLU PRO SEQRES 18HH 222 ARG SEQRES 1LL 212 ASN LEU THR LEU ILE GLN SER ARG SER VAL SER GLY SER SEQRES 2LL 212 PRO GLY GLN THR VAL SER ILE SER CYS THR ALA ASN GLY SEQRES 3LL 212 ALA HIS ILE GLY ASP SER TYR VAL GLN TRP PHE GLN GLN SEQRES 4LL 212 ARG PRO GLY SER ALA PRO ARG SER VAL ILE PHE GLU ASP SEQRES 5LL 212 ASP LYS ARG PRO SER GLY VAL PRO ASP ARG LEU SER GLY SEQRES 6LL 212 SER THR ASP PHE SER SER ASN SER ALA SER LEU THR ILE SEQRES 7LL 212 SER GLY LEU GLU SER GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8LL 212 GLN SER TYR TYR ARG GLY ASP TRP VAL LEU GLY GLY GLY SEQRES 9LL 212 THR LYS LEU THR VAL LEU GLY GLN PRO LYS SER SER PRO SEQRES 10LL 212 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLU SEQRES 11LL 212 THR ASN LYS ALA THR LEU VAL CYS THR ILE THR ASP PHE SEQRES 12LL 212 TYR PRO GLY VAL VAL THR VAL ASP TRP LYS VAL ASP GLY SEQRES 13LL 212 THR PRO VAL THR GLN GLY MET GLU THR THR GLN PRO SER SEQRES 14LL 212 LYS GLN SER ASN ASN LYS TYR MET ALA SER SER TYR LEU SEQRES 15LL 212 THR LEU THR ALA ARG ALA TRP GLU ARG HIS SER SER TYR SEQRES 16LL 212 SER CYS GLN VAL THR HIS GLU GLY HIS THR VAL GLU LYS SEQRES 17LL 212 SER LEU SER ARG HET CIR BB 701 23 HET ZN BB 702 1 HET ZN HH 305 1 HET ZN HH 306 1 HET ZN HH 307 1 HET NAG A 1 28 HET NAG A 2 28 HET BMA A 3 22 HET FUC A 4 21 HETNAM CIR CITRULLINE HETNAM ZN ZINC ION HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM FUC ALPHA-L-FUCOSE FORMUL 4 CIR C6 H13 N3 O3 FORMUL 5 ZN 4(ZN 2+) FORMUL 9 NAG 2(C8 H15 N O6) FORMUL 9 BMA C6 H12 O6 FORMUL 9 FUC C6 H12 O5 FORMUL 10 HOH *33(H2 O) HELIX 1 AA1 ASNHH 28 SERHH 30 5 3 HELIX 2 AA2 GLNHH 62 THRHH 65 5 4 HELIX 3 AA3 THRHH 74 VALHH 76 5 3 HELIX 4 AA4 LYSHH 87 THRHH 91 5 5 HELIX 5 AA5 HISLL 28 SERLL 32 5 5 HELIX 6 AA6 GLULL 82 GLULL 86 5 5 HELIX 7 AA7 SERLL 125 GLULL 130 1 6 HELIX 8 AA8 ALALL 186 HISLL 192 1 7 SHEET 1 AA1 4 HISHH 3 GLNHH 6 0 SHEET 2 AA1 4 VALHH 18 SERHH 25 -1 O LYSHH 23 N GLUHH 5 SHEET 3 AA1 4 THRHH 78 ILEHH 83 -1 O LEUHH 81 N ILEHH 20 SHEET 4 AA1 4 PHEHH 68 ASPHH 73 -1 N SERHH 71 O TYRHH 80 SHEET 1 AA2 6 GLUHH 10 LYSHH 12 0 SHEET 2 AA2 6 ALAHH 116 VALHH 120 1 O SERHH 119 N LYSHH 12 SHEET 3 AA2 6 ALAHH 92 SERHH 101 -1 N ALAHH 92 O VALHH 118 SHEET 4 AA2 6 PHEHH 32 GLNHH 39 -1 N ALAHH 33 O GLYHH 99 SHEET 5 AA2 6 GLNHH 46 ILEHH 51 -1 O GLNHH 46 N ARGHH 38 SHEET 6 AA2 6 LEUHH 58 TYRHH 60 -1 O THRHH 59 N TRPHH 50 SHEET 1 AA3 4 SERHH 129 LEUHH 133 0 SHEET 2 AA3 4 SERHH 144 TYRHH 154 -1 O GLYHH 148 N LEUHH 133 SHEET 3 AA3 4 LEUHH 183 PROHH 193 -1 O TYRHH 184 N TYRHH 154 SHEET 4 AA3 4 VALHH 172 THRHH 174 -1 N HISHH 173 O SERHH 189 SHEET 1 AA4 4 SERHH 129 LEUHH 133 0 SHEET 2 AA4 4 SERHH 144 TYRHH 154 -1 O GLYHH 148 N LEUHH 133 SHEET 3 AA4 4 LEUHH 183 PROHH 193 -1 O TYRHH 184 N TYRHH 154 SHEET 4 AA4 4 LEUHH 178 GLNHH 180 -1 N LEUHH 178 O THRHH 185 SHEET 1 AA5 3 THRHH 160 ASNHH 164 0 SHEET 2 AA5 3 THRHH 203 HISHH 208 -1 O ALAHH 207 N THRHH 160 SHEET 3 AA5 3 THRHH 213 LYSHH 218 -1 O VALHH 215 N VALHH 206 SHEET 1 AA6 4 THRLL 3 GLNLL 6 0 SHEET 2 AA6 4 VALLL 18 ASNLL 25 -1 O THRLL 23 N ILELL 5 SHEET 3 AA6 4 SERLL 73 ILELL 78 -1 O LEULL 76 N ILELL 20 SHEET 4 AA6 4 LEULL 63 ASPLL 68 -1 N ASPLL 68 O SERLL 73 SHEET 1 AA7 5 SERLL 9 GLYLL 12 0 SHEET 2 AA7 5 THRLL 105 VALLL 109 1 O LYSLL 106 N VALLL 10 SHEET 3 AA7 5 ALALL 87 TYRLL 95 -1 N TYRLL 89 O THRLL 105 SHEET 4 AA7 5 GLNLL 35 GLNLL 39 -1 N PHELL 37 O TYRLL 90 SHEET 5 AA7 5 ARGLL 46 ILELL 49 -1 O ILELL 49 N TRPLL 36 SHEET 1 AA8 4 SERLL 9 GLYLL 12 0 SHEET 2 AA8 4 THRLL 105 VALLL 109 1 O LYSLL 106 N VALLL 10 SHEET 3 AA8 4 ALALL 87 TYRLL 95 -1 N TYRLL 89 O THRLL 105 SHEET 4 AA8 4 ASPLL 98 LEULL 101 -1 O VALLL 100 N SERLL 93 SHEET 1 AA9 4 SERLL 118 PHELL 122 0 SHEET 2 AA9 4 LYSLL 133 PHELL 143 -1 O VALLL 137 N PHELL 122 SHEET 3 AA9 4 TYRLL 176 THRLL 185 -1 O LEULL 182 N LEULL 136 SHEET 4 AA9 4 METLL 163 THRLL 165 -1 N GLULL 164 O TYRLL 181 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 182 N LEULL 136 SHEET 4 AB1 4 SERLL 169 LYSLL 170 -1 N SERLL 169 O METLL 177 SHEET 1 AB2 4 THRLL 157 PROLL 158 0 SHEET 2 AB2 4 THRLL 149 VALLL 154 -1 N VALLL 154 O THRLL 157 SHEET 3 AB2 4 SERLL 194 HISLL 201 -1 O THRLL 200 N THRLL 149 SHEET 4 AB2 4 HISLL 204 SERLL 211 -1 O LYSLL 208 N CYSLL 197 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.03 SSBOND 2 CYSHH 149 CYSHH 204 1555 1555 2.03 SSBOND 3 CYSLL 22 CYSLL 91 1555 1555 2.08 SSBOND 4 CYSLL 138 CYSLL 197 1555 1555 2.08 LINK C GLNBB 600 N2 CIRBB 701 1555 1555 1.31 LINK N GLYBB 602 C1 CIRBB 701 1555 1555 1.33 LINK ND2 ASNHH 28 C1 NAG A 1 1555 1555 1.43 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.36 LINK O6 NAG A 1 C1 FUC A 4 1555 1555 1.38 LINK O4 NAG A 2 C1 BMA A 3 1555 1555 1.38 LINK OE1 GLUBB 603 ZN ZNBB 702 1555 1555 2.43 LINK OE2 GLUBB 603 ZN ZNBB 702 1555 1555 2.41 LINK ZN ZNBB 702 OD1 ASPLL 31 1555 1555 1.98 LINK ZN ZNBB 702 OD2 ASPLL 31 1555 1555 2.67 LINK ZN ZNBB 702 OD2 ASPLL 155 3655 1555 2.01 LINK NE2 HISHH 3 ZN ZNHH 307 1555 1555 1.91 LINK OE1 GLUHH 5 ZN ZNHH 307 1555 1555 2.60 LINK NE2 HISHH 82 ZN ZNHH 305 1555 1555 1.97 LINK ND1 HISHH 84 ZN ZNHH 305 1555 1555 1.97 LINK NE2 HISHH 173 ZN ZNHH 306 1555 1555 1.93 LINK ZN ZNHH 305 O HOHHH 408 1555 1555 1.96 LINK ZN ZNHH 305 OE2 GLULL 130 3555 1555 1.84 LINK ZN ZNHH 306 O HOHHH 415 1555 1555 2.70 LINK ZN ZNHH 306 OD1 ASPLL 142 1555 1555 2.48 LINK ZN ZNHH 306 O HOHLL 303 1555 1555 2.13 LINK ZN ZNHH 307 O HOHHH 401 1555 1555 2.27 LINK ZN ZNHH 307 OD1 ASPLL 61 4555 1555 2.13 LINK ZN ZNHH 307 OD2 ASPLL 61 4555 1555 2.48 CISPEP 1 PHEHH 155 PROHH 156 0 -12.10 CISPEP 2 TRPHH 197 PROHH 198 0 4.19 CISPEP 3 TYRLL 144 PROLL 145 0 -4.76 CRYST1 53.010 89.650 118.680 90.00 90.00 90.00 P 21 21 21 4 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 0.018864 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011154 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008426 0.00000