HEADER IMMUNE SYSTEM 31-JAN-25 9I6Q TITLE STRUCTURE OF FAB-FRAGMENT GB11 AGAINS TUMOUR ASSOCIATED CARBOHYDRATE TITLE 2 ANTIGENS. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: FAB FRAGMENT VARIABLE CHAIN; COMPND 6 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 ORGAN: SPLEEN; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_TAXID: 10090; SOURCE 8 ORGAN: SPLEEN KEYWDS ANTIBODY, FAB FRAGMENT, APO, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.FREITAG,S.K.KHILJI,R.NEDIELKOV,S.M.KUMAR,M.KRUMMHAAR,J.LUEHLE, AUTHOR 2 F.GOERDELER,J.ARNDT,C.KAMPHUES,M.A.MROGINSKI,C.ROTH,P.H.SEEBERGER, AUTHOR 3 H.M.MOELLER,O.MOSCOVITZ REVDAT 1 18-FEB-26 9I6Q 0 JRNL AUTH A.FREITAG,S.K.KHILJI,R.NEDIELKOV,S.M.KUMAR,M.KRUMMHAAR, JRNL AUTH 2 J.LUEHLE,F.GOERDELER,J.ARNDT,C.KAMPHUES,M.A.MROGINSKI, JRNL AUTH 3 C.ROTH,P.H.SEEBERGER,H.M.MOELLER,O.MOSCOVITZ JRNL TITL AN INTEGRATIVE APPROACH TO DEVELOP AND CHARACTERIZE JRNL TITL 2 ANTIBODIES AGAINST CANCER ASSOCIATED CARBOHYDRATE ANTIGEN JRNL TITL 3 SIALYL LEWIS A. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.86 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0405 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.87 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 40382 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) : 0.200 REMARK 3 FREE R VALUE : 0.239 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.851 REMARK 3 FREE R VALUE TEST SET COUNT : 1959 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.86 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2840 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93 REMARK 3 BIN R VALUE (WORKING SET) : 0.3310 REMARK 3 BIN FREE R VALUE SET COUNT : 137 REMARK 3 BIN FREE R VALUE : 0.3560 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3304 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 138 REMARK 3 SOLVENT ATOMS : 202 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.95 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.98800 REMARK 3 B22 (A**2) : 0.98800 REMARK 3 B33 (A**2) : -1.97600 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): 0.148 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.137 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.622 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3521 ; 0.011 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3230 ; 0.002 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4712 ; 1.804 ; 1.647 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7486 ; 0.643 ; 1.562 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 427 ; 8.397 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 16 ; 9.840 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 543 ;16.098 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 508 ; 0.083 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3946 ; 0.011 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 774 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 566 ; 0.194 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 73 ; 0.127 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1665 ; 0.176 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 189 ; 0.144 ; 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): 1714 ; 2.213 ; 1.973 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1714 ; 2.210 ; 1.973 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2139 ; 3.301 ; 3.528 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2140 ; 3.302 ; 3.530 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1807 ; 3.611 ; 2.495 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1808 ; 3.610 ; 2.497 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2573 ; 5.001 ; 4.230 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2574 ; 5.001 ; 4.231 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 : H 12 H 228 REMARK 3 ORIGIN FOR THE GROUP (A): 45.5252 16.8846 9.6818 REMARK 3 T TENSOR REMARK 3 T11: 0.0558 T22: 0.0041 REMARK 3 T33: 0.1462 T12: -0.0082 REMARK 3 T13: 0.0001 T23: -0.0016 REMARK 3 L TENSOR REMARK 3 L11: 0.5869 L22: 2.2956 REMARK 3 L33: 0.7500 L12: 0.1052 REMARK 3 L13: 0.0564 L23: -0.3716 REMARK 3 S TENSOR REMARK 3 S11: 0.0290 S12: 0.0196 S13: -0.1058 REMARK 3 S21: -0.0126 S22: 0.0228 S23: 0.0469 REMARK 3 S31: 0.1900 S32: -0.0405 S33: -0.0518 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 28.1874 14.5939 12.9196 REMARK 3 T TENSOR REMARK 3 T11: 0.1456 T22: 0.0723 REMARK 3 T33: 0.3977 T12: -0.0521 REMARK 3 T13: 0.0281 T23: -0.0029 REMARK 3 L TENSOR REMARK 3 L11: 0.4721 L22: 1.9048 REMARK 3 L33: 0.4716 L12: -0.8484 REMARK 3 L13: 0.3155 L23: -0.2628 REMARK 3 S TENSOR REMARK 3 S11: 0.0535 S12: -0.0758 S13: -0.2646 REMARK 3 S21: 0.0961 S22: 0.0323 S23: 0.5077 REMARK 3 S31: 0.2012 S32: -0.1420 S33: -0.0858 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 9I6Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1292145034. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-DEC-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : BESSY REMARK 200 BEAMLINE : 14.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40412 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860 REMARK 200 RESOLUTION RANGE LOW (A) : 54.580 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 11.60 REMARK 200 R MERGE (I) : 0.20200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 11.20 REMARK 200 R MERGE FOR SHELL (I) : 2.72100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: DL-MALIC ACID, CITRIC ACID, PEG 3350, REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,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 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 521 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 229 REMARK 465 LEU H 230 REMARK 465 SER H 231 REMARK 465 SER H 232 REMARK 465 GLY H 233 REMARK 465 VAL H 234 REMARK 465 HIS H 235 REMARK 465 THR H 236 REMARK 465 PHE H 237 REMARK 465 PRO H 238 REMARK 465 ALA H 239 REMARK 465 VAL H 240 REMARK 465 LEU H 241 REMARK 465 GLN H 242 REMARK 465 SER H 243 REMARK 465 ASP H 244 REMARK 465 LEU H 245 REMARK 465 TYR H 246 REMARK 465 THR H 247 REMARK 465 LEU H 248 REMARK 465 SER H 249 REMARK 465 SER H 250 REMARK 465 SER H 251 REMARK 465 VAL H 252 REMARK 465 THR H 253 REMARK 465 VAL H 254 REMARK 465 PRO H 255 REMARK 465 SER H 256 REMARK 465 SER H 257 REMARK 465 PRO H 258 REMARK 465 ARG H 259 REMARK 465 PRO H 260 REMARK 465 SER H 261 REMARK 465 GLU H 262 REMARK 465 THR H 263 REMARK 465 VAL H 264 REMARK 465 THR H 265 REMARK 465 CYS H 266 REMARK 465 ASN H 267 REMARK 465 VAL H 268 REMARK 465 ALA H 269 REMARK 465 HIS H 270 REMARK 465 PRO H 271 REMARK 465 ALA H 272 REMARK 465 SER H 273 REMARK 465 SER H 274 REMARK 465 THR H 275 REMARK 465 LYS H 276 REMARK 465 VAL H 277 REMARK 465 ASP H 278 REMARK 465 LYS H 279 REMARK 465 LYS H 280 REMARK 465 ILE H 281 REMARK 465 VAL H 282 REMARK 465 PRO H 283 REMARK 465 ARG H 284 REMARK 465 ASP H 285 REMARK 465 CYS H 286 REMARK 465 GLY H 287 REMARK 465 CYS H 288 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 HH TYR H 73 H ILE H 83 1.10 REMARK 500 HE22 GLN L 124 HG SER L 131 1.22 REMARK 500 HD2 HIS L 198 HG1 THR L 200 1.31 REMARK 500 HO1 PEG H 301 C4 PEG L 301 1.58 REMARK 500 O HIS L 189 HH11 ARG L 211 1.59 REMARK 500 C4 PEG H 308 HO1 PEG H 309 1.59 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 HG1 THR H 217 HZ2 LYS H 221 2655 1.20 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 GLU L 93 CD GLU L 93 OE2 0.118 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 PHE H 113 16.09 54.01 REMARK 500 THR H 145 -147.03 -82.36 REMARK 500 SER H 174 110.58 -33.91 REMARK 500 SER H 216 55.14 37.07 REMARK 500 ALA L 51 -36.33 66.67 REMARK 500 ASN L 52 13.53 -147.92 REMARK 500 SER L 77 101.42 -160.28 REMARK 500 ASN L 190 -62.05 -124.08 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 ALA H 142 ALA H 143 -147.60 REMARK 500 ARG L 211 ASN L 212 147.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG L 50 0.09 SIDE CHAIN REMARK 500 ARG L 155 0.10 SIDE CHAIN REMARK 500 ARG L 188 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9I6Q H 12 288 PDB 9I6Q 9I6Q 12 288 DBREF 9I6Q L 1 214 PDB 9I6Q 9I6Q 1 214 SEQRES 1 H 277 GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 277 PRO GLY GLY SER MET LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 277 PHE THR PHE SER ASP ALA TRP MET ASP TRP VAL ARG GLN SEQRES 4 H 277 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLU ILE GLY SEQRES 5 H 277 ASN TYR ALA ILE ASN HIS ALA THR TYR TYR ALA GLU SER SEQRES 6 H 277 VAL LYS GLY ARG PHE ALA ILE SER ARG ASP ASP SER LYS SEQRES 7 H 277 SER SER VAL TYR LEU GLN MET ASN SER LEU ARG PRO GLU SEQRES 8 H 277 ASP THR GLY ILE TYR PHE CYS THR VAL ARG PHE ALA TYR SEQRES 9 H 277 TRP GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS SEQRES 10 H 277 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER SEQRES 11 H 277 ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU SEQRES 12 H 277 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP SEQRES 13 H 277 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 H 277 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 H 277 VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL SEQRES 16 H 277 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 H 277 ASP LYS LYS ILE VAL PRO ARG ASP CYS SER LEU SER SER SEQRES 18 H 277 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU SEQRES 19 H 277 TYR THR LEU SER SER SER VAL THR VAL PRO SER SER PRO SEQRES 20 H 277 ARG PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO SEQRES 21 H 277 ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG SEQRES 22 H 277 ASP CYS GLY CYS SEQRES 1 L 214 ASP ILE LYS MET THR GLN SER PRO SER SER MET TYR ALA SEQRES 2 L 214 SER LEU GLY GLU ARG VAL THR PHE THR CYS ARG ALA SER SEQRES 3 L 214 GLN ASP ILE ASN SER TYR LEU SER TRP PHE GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS SER PRO LYS THR LEU ILE TYR ARG ALA ASN SEQRES 5 L 214 ARG LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY GLN ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 L 214 GLU TYR GLU ASP MET GLY ILE TYR PHE CYS LEU GLN TYR SEQRES 8 L 214 ASP GLU PHE PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS HET PEG H 301 17 HET PGE H 302 24 HET PEG H 303 17 HET PEG H 304 13 HET PEG H 305 13 HET PEG H 306 13 HET PEG H 307 13 HET PEG H 308 13 HET PEG H 309 13 HET PEG H 310 13 HET PEG H 311 13 HET PEG H 312 17 HET PEG H 313 17 HET PEG H 314 17 HET PEG L 301 13 HET PEG L 302 17 HET PEG L 303 17 HET PEG L 304 17 HET PEG L 305 13 HET PEG L 306 13 HET PEG L 307 13 HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM PGE TRIETHYLENE GLYCOL FORMUL 3 PEG 20(C4 H10 O3) FORMUL 4 PGE C6 H14 O4 FORMUL 24 HOH *202(H2 O) HELIX 1 AA1 THR H 39 ALA H 43 5 5 HELIX 2 AA2 ASN H 64 ASN H 68 5 5 HELIX 3 AA3 GLU H 75 LYS H 78 5 4 HELIX 4 AA4 ASP H 87 LYS H 89 5 3 HELIX 5 AA5 ARG H 100 THR H 104 5 5 HELIX 6 AA6 SER H 169 SER H 171 5 3 HELIX 7 AA7 SER H 199 TRP H 201 5 3 HELIX 8 AA8 PRO H 213 SER H 216 5 4 HELIX 9 AA9 GLU L 79 MET L 83 5 5 HELIX 10 AB1 SER L 121 THR L 126 1 6 HELIX 11 AB2 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 LYS H 14 SER H 18 0 SHEET 2 AA1 4 MET H 29 SER H 36 -1 O SER H 32 N SER H 18 SHEET 3 AA1 4 SER H 91 MET H 96 -1 O MET H 96 N MET H 29 SHEET 4 AA1 4 PHE H 81 ASP H 86 -1 N SER H 84 O TYR H 93 SHEET 1 AA2 6 GLY H 21 VAL H 23 0 SHEET 2 AA2 6 THR H 120 VAL H 124 1 O THR H 123 N GLY H 21 SHEET 3 AA2 6 GLY H 105 VAL H 111 -1 N TYR H 107 O THR H 120 SHEET 4 AA2 6 MET H 45 SER H 51 -1 N VAL H 48 O PHE H 108 SHEET 5 AA2 6 GLY H 55 ILE H 62 -1 O GLU H 57 N ARG H 49 SHEET 6 AA2 6 THR H 71 TYR H 73 -1 O TYR H 72 N GLU H 61 SHEET 1 AA3 4 GLY H 21 VAL H 23 0 SHEET 2 AA3 4 THR H 120 VAL H 124 1 O THR H 123 N GLY H 21 SHEET 3 AA3 4 GLY H 105 VAL H 111 -1 N TYR H 107 O THR H 120 SHEET 4 AA3 4 TYR H 115 TRP H 116 -1 O TYR H 115 N VAL H 111 SHEET 1 AA4 4 SER H 133 LEU H 137 0 SHEET 2 AA4 4 MET H 148 TYR H 158 -1 O LYS H 156 N SER H 133 SHEET 3 AA4 4 LEU H 187 PRO H 197 -1 O TYR H 188 N TYR H 158 SHEET 4 AA4 4 VAL H 176 THR H 178 -1 N HIS H 177 O SER H 193 SHEET 1 AA5 4 SER H 133 LEU H 137 0 SHEET 2 AA5 4 MET H 148 TYR H 158 -1 O LYS H 156 N SER H 133 SHEET 3 AA5 4 LEU H 187 PRO H 197 -1 O TYR H 188 N TYR H 158 SHEET 4 AA5 4 VAL H 182 GLN H 184 -1 N GLN H 184 O LEU H 187 SHEET 1 AA6 3 THR H 164 TRP H 167 0 SHEET 2 AA6 3 THR H 207 HIS H 212 -1 O ASN H 209 N THR H 166 SHEET 3 AA6 3 THR H 217 LYS H 222 -1 O VAL H 219 N VAL H 210 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O LEU L 73 N PHE L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O LYS L 103 N MET L 11 SHEET 3 AA8 6 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N GLN L 38 O ILE L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA8 6 ARG L 53 LEU L 54 -1 O ARG L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O LYS L 103 N MET L 11 SHEET 3 AA9 4 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 THR L 114 PHE L 118 0 SHEET 2 AB1 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114 SHEET 3 AB1 4 TYR L 173 THR L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB1 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 AB2 4 SER L 153 ARG L 155 0 SHEET 2 AB2 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AB2 4 SER L 191 THR L 197 -1 O THR L 197 N ASN L 145 SHEET 4 AB2 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SSBOND 1 CYS H 33 CYS H 109 1555 1555 2.05 SSBOND 2 CYS H 153 CYS H 208 1555 1555 1.97 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.16 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.05 LINK O1 PEG H 301 C4 PEG L 301 1555 1555 1.45 LINK O1 PEG H 303 C4 PEG H 304 1555 1555 1.42 LINK O1 PEG H 304 C4 PEG H 305 1555 1555 1.45 LINK O1 PEG H 305 C4 PEG H 306 1555 1555 1.44 LINK O1 PEG H 306 C4 PEG H 307 1555 1555 1.46 LINK O1 PEG H 307 C4 PEG L 305 1555 1555 1.44 LINK C4 PEG H 308 O1 PEG H 309 1555 1555 1.47 LINK O1 PEG H 308 C4 PEG L 307 1555 1555 1.46 LINK C4 PEG H 309 O1 PEG H 310 1555 1555 1.42 LINK C4 PEG H 310 O1 PEG H 311 1555 1555 1.45 LINK C4 PEG H 311 O1 PEG H 312 1555 1555 1.42 LINK C4 PEG L 306 O1 PEG L 307 1555 1555 1.46 CISPEP 1 PHE H 159 PRO H 160 0 -6.02 CISPEP 2 GLU H 161 PRO H 162 0 -5.33 CISPEP 3 TRP H 201 PRO H 202 0 11.54 CISPEP 4 SER L 7 PRO L 8 0 -9.87 CISPEP 5 PHE L 94 PRO L 95 0 -6.38 CISPEP 6 TYR L 140 PRO L 141 0 -4.07 CRYST1 109.160 109.160 40.268 90.00 90.00 90.00 P 4 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 0.009161 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009161 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024834 0.00000