HEADER IMMUNE SYSTEM 03-MAY-20 6YXL TITLE CRYSTAL STRUCTURE OF ACPA F3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACPA F3 FAB FRAGMENT - HEAVY CHAIN; COMPND 3 CHAIN: HHH; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ACPA F3 FAB FRAGMENT - LIGHT 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 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 KEYWDS ANTI-CITRULLINATED PROTEIN ANTIBODY FAB FRAGMENT, 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. 2.10 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.53 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 31497 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) : 0.199 REMARK 3 FREE R VALUE : 0.231 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.924 REMARK 3 FREE R VALUE TEST SET COUNT : 1551 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2144 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.2480 REMARK 3 BIN FREE R VALUE SET COUNT : 136 REMARK 3 BIN FREE R VALUE : 0.2980 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3262 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 11 REMARK 3 SOLVENT ATOMS : 189 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.45 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.09800 REMARK 3 B22 (A**2) : -0.09800 REMARK 3 B33 (A**2) : 0.19600 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): 0.197 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.969 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3345 ; 0.011 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3018 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4551 ; 1.757 ; 1.651 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7025 ; 1.349 ; 1.572 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 419 ; 8.386 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;33.190 ;21.950 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 523 ;14.320 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;18.741 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 444 ; 0.072 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3719 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 692 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 533 ; 0.253 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 35 ; 0.283 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1584 ; 0.165 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 172 ; 0.146 ; 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): 1700 ; 1.695 ; 3.053 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1698 ; 1.694 ; 3.050 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2111 ; 2.516 ; 4.568 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2111 ; 2.516 ; 4.568 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1641 ; 2.338 ; 3.344 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1642 ; 2.337 ; 3.345 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2435 ; 3.724 ; 4.900 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2436 ; 3.723 ; 4.901 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 : 2 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 : HH 1 HH 231 REMARK 3 ORIGIN FOR THE GROUP (A): -0.7520 25.3698 27.5061 REMARK 3 T TENSOR REMARK 3 T11: 0.0229 T22: 0.0337 REMARK 3 T33: 0.0449 T12: -0.0047 REMARK 3 T13: -0.0115 T23: -0.0028 REMARK 3 L TENSOR REMARK 3 L11: 1.7360 L22: 2.7410 REMARK 3 L33: 1.1043 L12: -1.5820 REMARK 3 L13: -0.4377 L23: 1.0409 REMARK 3 S TENSOR REMARK 3 S11: -0.1218 S12: -0.1640 S13: 0.0823 REMARK 3 S21: 0.1598 S22: 0.0852 S23: 0.1116 REMARK 3 S31: 0.0609 S32: 0.0017 S33: 0.0366 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 : LL 1 LL 213 REMARK 3 ORIGIN FOR THE GROUP (A): -11.0687 35.7976 16.1860 REMARK 3 T TENSOR REMARK 3 T11: 0.0347 T22: 0.1281 REMARK 3 T33: 0.1131 T12: 0.0232 REMARK 3 T13: -0.0264 T23: 0.0286 REMARK 3 L TENSOR REMARK 3 L11: 1.2275 L22: 2.2959 REMARK 3 L33: 1.4346 L12: -1.2672 REMARK 3 L13: -0.6083 L23: 1.2680 REMARK 3 S TENSOR REMARK 3 S11: 0.0329 S12: 0.2271 S13: 0.1580 REMARK 3 S21: -0.0739 S22: -0.2052 S23: 0.1129 REMARK 3 S31: -0.0741 S32: -0.1323 S33: 0.1722 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 6YXL 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_1292108466. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-NOV-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 : MAX IV REMARK 200 BEAMLINE : BIOMAX REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91840 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS 0.7.4, XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31556 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 65.529 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 16.40 REMARK 200 R MERGE (I) : 0.15500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 8.91 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 65.44 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 13.30 REMARK 200 R MERGE FOR SHELL (I) : 0.05500 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 (%): 55.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM TRIS PH 7.4, 50MM NACL, 0.2M REMARK 280 POTASSIUM THIOCYANATE, 2.2M AMMONIUM SULFATE), VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 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 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.51300 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 65.44300 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 65.44300 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 15.25650 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 65.44300 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 65.44300 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.76950 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 65.44300 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.44300 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 15.25650 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 65.44300 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.44300 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.76950 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 30.51300 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: 3860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 461 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 489 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 498 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 SER H 143 REMARK 465 SER H 144 REMARK 465 LYS H 145 REMARK 465 SER H 146 REMARK 465 THR H 147 REMARK 465 SER H 148 REMARK 465 GLY H 149 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 C HISHH 55 H ASNHH 60 1.26 REMARK 500 HE ARGHH 110 HH TYRLL 33 1.29 REMARK 500 O1 SO4HH 302 O HOHHH 401 2.12 REMARK 500 C PROHH 229 O HOHHH 406 2.19 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 HB3 GLULL 82 HB3 GLULL 82 8555 1.23 REMARK 500 HH11 ARGHH 19 HH11 ARGHH 19 7556 1.29 REMARK 500 O3 SO4HH 302 O4 SO4HH 302 7555 1.36 REMARK 500 OH TYRHH 116 OH TYRHH 116 8555 1.62 REMARK 500 O1 SO4HH 302 O1 SO4HH 302 7555 2.08 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 VALHH 29 C THRHH 31 N 0.271 REMARK 500 HISHH 55 C ASNHH 60 N 0.292 REMARK 500 SERHH 127 C ALAHH 129 N 0.191 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 PHEHH 27 CA - C - O ANGL. DEV. = -13.0 DEGREES REMARK 500 VALHH 29 O - C - N ANGL. DEV. = -13.8 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 ASPHH 71 -46.25 97.85 REMARK 500 SERHH 104 -145.03 -105.82 REMARK 500 ASNHH 220 55.42 38.20 REMARK 500 ARGLL 41 -127.82 60.86 REMARK 500 ALALL 52 -37.36 73.84 REMARK 500 ASNLL 139 61.31 68.12 REMARK 500 SERLL 157 118.48 -175.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEUHH 69 GLNHH 70 -147.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 VALHH 29 -20.44 REMARK 500 HISHH 55 -15.95 REMARK 500 SERHH 127 -13.00 REMARK 500 REMARK 500 REMARK: NULL DBREF 6YXLHH 1 229 PDB 6YXL 6YXL 1 229 DBREF 6YXLLL 1 213 PDB 6YXL 6YXL 1 213 SEQRES 1HH 221 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2HH 221 PRO GLY ALA SER VAL ARG VAL SER CYS LYS ALA SER GLY SEQRES 3HH 221 PHE VAL THR ASP TYR PHE ILE GLN TRP VAL ARG GLN ALA SEQRES 4HH 221 PRO GLY GLN GLY PRO GLU TRP MET ALA TRP ILE ASN PRO SEQRES 5HH 221 HIS ASN GLY GLU THR ASP TYR ALA PRO LYS LEU GLN ASP SEQRES 6HH 221 ARG VAL THR VAL THR CYS ASP THR SER THR ASN THR ALA SEQRES 7HH 221 PHE MET GLU LEU SER ARG LEU THR SER ASP ASP THR ALA SEQRES 8HH 221 LEU TYR TYR CYS GLY ARG SER GLY ARG THR ASP ALA ARG SEQRES 9HH 221 ARG ALA PRO VAL SER TYR TRP GLY GLN GLY ALA LEU VAL SEQRES 10HH 221 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11HH 221 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12HH 221 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13HH 221 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14HH 221 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15HH 221 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16HH 221 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17HH 221 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 1LL 213 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2LL 213 SER PRO GLY ALA ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3LL 213 GLN THR VAL ARG GLY ASN TYR LEU ALA TRP PHE GLN GLN SEQRES 4LL 213 LYS ARG GLY GLN PRO PRO ARG LEU LEU ILE TYR LEU ALA SEQRES 5LL 213 SER ASN ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6LL 213 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7LL 213 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8LL 213 TYR VAL ASN THR PRO GLU THR PHE GLY GLN GLY THR ARG SEQRES 9LL 213 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10LL 213 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11LL 213 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12LL 213 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13LL 213 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14LL 213 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15LL 213 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16LL 213 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17LL 213 SER PHE ASN ARG GLY HET GOL HH 301 14 HET SO4 HH 302 5 HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL C3 H8 O3 FORMUL 4 SO4 O4 S 2- FORMUL 5 HOH *189(H2 O) HELIX 1 AA1 THRHH 92 THRHH 96 5 5 HELIX 2 AA2 SERHH 172 ALAHH 174 5 3 HELIX 3 AA3 SERHH 203 LEUHH 205 5 3 HELIX 4 AA4 LYSHH 217 ASNHH 220 5 4 HELIX 5 AA5 VALLL 29 ASNLL 32 5 4 HELIX 6 AA6 GLULL 80 PHELL 84 5 5 HELIX 7 AA7 SERLL 122 SERLL 128 1 7 HELIX 8 AA8 LYSLL 184 GLULL 188 1 5 SHEET 1 AA1 4 GLNHH 3 GLNHH 6 0 SHEET 2 AA1 4 VALHH 18 SERHH 25 -1 O LYSHH 23 N VALHH 5 SHEET 3 AA1 4 THRHH 83 LEUHH 88 -1 O METHH 86 N VALHH 20 SHEET 4 AA1 4 VALHH 73 ASPHH 78 -1 N ASPHH 78 O THRHH 83 SHEET 1 AA2 6 GLUHH 10 LYSHH 12 0 SHEET 2 AA2 6 ALAHH 121 VALHH 125 1 O THRHH 124 N GLUHH 10 SHEET 3 AA2 6 ALAHH 97 ARGHH 106 -1 N ALAHH 97 O VALHH 123 SHEET 4 AA2 6 TYRHH 33 GLNHH 40 -1 N VALHH 38 O TYRHH 100 SHEET 5 AA2 6 PROHH 46 ILEHH 52 -1 O GLUHH 47 N ARGHH 39 SHEET 6 AA2 6 THRHH 63 TYRHH 65 -1 O ASPHH 64 N TRPHH 51 SHEET 1 AA3 4 GLUHH 10 LYSHH 12 0 SHEET 2 AA3 4 ALAHH 121 VALHH 125 1 O THRHH 124 N GLUHH 10 SHEET 3 AA3 4 ALAHH 97 ARGHH 106 -1 N ALAHH 97 O VALHH 123 SHEET 4 AA3 4 TYRHH 116 TRPHH 117 -1 O TYRHH 116 N ARGHH 103 SHEET 1 AA4 4 SERHH 135 LEUHH 139 0 SHEET 2 AA4 4 THRHH 151 TYRHH 161 -1 O LYSHH 159 N SERHH 135 SHEET 3 AA4 4 TYRHH 192 PROHH 201 -1 O LEUHH 194 N VALHH 158 SHEET 4 AA4 4 VALHH 179 THRHH 181 -1 N HISHH 180 O VALHH 197 SHEET 1 AA5 4 SERHH 135 LEUHH 139 0 SHEET 2 AA5 4 THRHH 151 TYRHH 161 -1 O LYSHH 159 N SERHH 135 SHEET 3 AA5 4 TYRHH 192 PROHH 201 -1 O LEUHH 194 N VALHH 158 SHEET 4 AA5 4 VALHH 185 LEUHH 186 -1 N VALHH 185 O SERHH 193 SHEET 1 AA6 3 THRHH 167 TRPHH 170 0 SHEET 2 AA6 3 TYRHH 210 HISHH 216 -1 O ASNHH 213 N SERHH 169 SHEET 3 AA6 3 THRHH 221 VALHH 227 -1 O THRHH 221 N HISHH 216 SHEET 1 AA7 4 LEULL 4 SERLL 7 0 SHEET 2 AA7 4 ALALL 19 ALALL 25 -1 O ARGLL 24 N THRLL 5 SHEET 3 AA7 4 ASPLL 71 ILELL 76 -1 O LEULL 74 N LEULL 21 SHEET 4 AA7 4 PHELL 63 SERLL 68 -1 N SERLL 64 O THRLL 75 SHEET 1 AA8 6 THRLL 10 LEULL 13 0 SHEET 2 AA8 6 THRLL 103 ILELL 107 1 O GLULL 106 N LEULL 11 SHEET 3 AA8 6 ALALL 85 GLNLL 91 -1 N TYRLL 87 O THRLL 103 SHEET 4 AA8 6 LEULL 34 GLNLL 39 -1 N ALALL 35 O GLNLL 90 SHEET 5 AA8 6 ARGLL 46 TYRLL 50 -1 O LEULL 48 N TRPLL 36 SHEET 6 AA8 6 ASNLL 54 ARGLL 55 -1 O ASNLL 54 N TYRLL 50 SHEET 1 AA9 4 SERLL 115 PHELL 119 0 SHEET 2 AA9 4 THRLL 130 PHELL 140 -1 O LEULL 136 N PHELL 117 SHEET 3 AA9 4 TYRLL 174 SERLL 183 -1 O LEULL 182 N ALALL 131 SHEET 4 AA9 4 SERLL 160 VALLL 164 -1 N GLNLL 161 O THRLL 179 SHEET 1 AB1 4 ALALL 154 LEULL 155 0 SHEET 2 AB1 4 LYSLL 146 VALLL 151 -1 N VALLL 151 O ALALL 154 SHEET 3 AB1 4 VALLL 192 THRLL 198 -1 O GLULL 196 N GLNLL 148 SHEET 4 AB1 4 VALLL 206 ASNLL 211 -1 O VALLL 206 N VALLL 197 SSBOND 1 CYSHH 22 CYSHH 101 1555 1555 2.12 SSBOND 2 CYSHH 156 CYSHH 212 1555 1555 2.07 SSBOND 3 CYSLL 23 CYSLL 89 1555 1555 2.22 SSBOND 4 CYSLL 135 CYSLL 195 1555 1555 2.09 CISPEP 1 PHEHH 162 PROHH 163 0 -9.74 CISPEP 2 GLUHH 164 PROHH 165 0 -8.45 CISPEP 3 SERLL 7 PROLL 8 0 -7.93 CISPEP 4 THRLL 95 PROLL 96 0 0.88 CISPEP 5 TYRLL 141 PROLL 142 0 3.82 CRYST1 130.886 130.886 61.026 90.00 90.00 90.00 P 41 21 2 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 0.007640 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007640 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016386 0.00000