HEADER IMMUNE SYSTEM 21-SEP-22 8B50 TITLE CRYSTAL STRUCTURE OF A FAB FRAGMENT IN COMPLEX WITH L- TITLE 2 HYDROXYCOUMARYLALANINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB FRAGMENT K12F9-22 - HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB FRAGMENT K12F9-22 - LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, FLUORESCENT SIDE CHAIN, HAPTEN, NON-NATURAL AMINO ACID, KEYWDS 2 RECOMBINANT FAB, UMBELLIFERYLALANINE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR W.MEINING,A.EICHINGER,A.SKERRA REVDAT 1 04-OCT-23 8B50 0 JRNL AUTH M.RUBINI,W.MEINING,A.EICHINGER,M.MUELLER,K.KRAMER,A.SKERRA JRNL TITL PREPARATION AND CHARACTERIZATION OF MONOCLONAL ANTIBODIES JRNL TITL 2 AGAINST A NON NATURAL AMINO ACID CARRYING THE JRNL TITL 3 7-HYDROXYCOUMARIN SIDE CHAIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.67 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.60 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 3 NUMBER OF REFLECTIONS : 54280 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.192 REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2919 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) : 1.67 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.71 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2681 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.61 REMARK 3 BIN R VALUE (WORKING SET) : 0.3780 REMARK 3 BIN FREE R VALUE SET COUNT : 134 REMARK 3 BIN FREE R VALUE : 0.3920 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3320 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 24 REMARK 3 SOLVENT ATOMS : 261 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.66 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.20000 REMARK 3 B22 (A**2) : 1.20000 REMARK 3 B33 (A**2) : -3.89000 REMARK 3 B12 (A**2) : 0.60000 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): 0.099 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.796 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3477 ; 0.009 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3204 ; 0.001 ; 0.015 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4746 ; 1.591 ; 1.649 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7438 ; 1.303 ; 1.578 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 450 ; 7.572 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;32.530 ;22.671 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 565 ;12.218 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.493 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 461 ; 0.074 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3928 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 777 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 1 H 221 REMARK 3 ORIGIN FOR THE GROUP (A): 16.7720 -6.5410 2.8860 REMARK 3 T TENSOR REMARK 3 T11: 0.0435 T22: 0.0339 REMARK 3 T33: 0.3967 T12: 0.0327 REMARK 3 T13: 0.0316 T23: 0.0197 REMARK 3 L TENSOR REMARK 3 L11: 1.6188 L22: 0.7328 REMARK 3 L33: 1.3213 L12: 0.2625 REMARK 3 L13: 0.5871 L23: 0.5370 REMARK 3 S TENSOR REMARK 3 S11: -0.0078 S12: 0.0844 S13: 0.0354 REMARK 3 S21: 0.0454 S22: 0.0576 S23: 0.0384 REMARK 3 S31: -0.0974 S32: -0.0770 S33: -0.0498 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 : L 1 L 219 REMARK 3 ORIGIN FOR THE GROUP (A): 32.5160 -13.6080 -3.4700 REMARK 3 T TENSOR REMARK 3 T11: 0.0212 T22: 0.1380 REMARK 3 T33: 0.3442 T12: 0.0250 REMARK 3 T13: 0.0243 T23: -0.0026 REMARK 3 L TENSOR REMARK 3 L11: 3.7022 L22: 1.2495 REMARK 3 L33: 0.7673 L12: 1.0889 REMARK 3 L13: 0.9134 L23: 0.3658 REMARK 3 S TENSOR REMARK 3 S11: 0.0698 S12: 0.1375 S13: -0.2276 REMARK 3 S21: 0.1287 S22: -0.0018 S23: -0.0168 REMARK 3 S31: 0.0401 S32: 0.1443 S33: -0.0680 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.10 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 THE RIDING REMARK 3 POSITIONS U VALUES: WITH TLS ADDED REMARK 4 REMARK 4 8B50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-22. REMARK 100 THE DEPOSITION ID IS D_1292123576. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-MAY-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : BESSY REMARK 200 BEAMLINE : 14.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841 REMARK 200 MONOCHROMATOR : SI 111 DOUBLE-CRYSTAL REMARK 200 OPTICS : SI MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS DECEMBER 6, 2010 REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57236 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.670 REMARK 200 RESOLUTION RANGE LOW (A) : 61.413 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09500 REMARK 200 FOR THE DATA SET : 7.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.74800 REMARK 200 R SYM FOR SHELL (I) : 0.74800 REMARK 200 FOR SHELL : 1.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: BALBES 0.0.1.MAR_31_2008 REMARK 200 STARTING MODEL: 1JPT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.83 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 6000, MAGNESIUM REMARK 280 CHLORIDE, PH 6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.34767 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 60.69533 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: 3980 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19730 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL 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 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 133 REMARK 465 LYS H 134 REMARK 465 SER H 135 REMARK 465 THR H 136 REMARK 465 SER H 137 REMARK 465 GLY H 138 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 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 OG SER L 187 OD2 ASP L 190 2.12 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 O HOH H 497 O HOH L 408 2545 2.08 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 ASN H 77 32.65 73.26 REMARK 500 TYR H 104 -142.17 60.46 REMARK 500 ASP H 149 52.85 72.12 REMARK 500 LYS H 219 -78.24 -58.33 REMARK 500 VAL L 56 -46.66 81.67 REMARK 500 ASN L 143 66.27 60.22 REMARK 500 ASN L 157 -5.68 89.46 REMARK 500 SER L 161 140.69 -171.40 REMARK 500 LYS L 195 -66.03 -105.98 REMARK 500 REMARK 500 REMARK: NULL DBREF 8B50 H 1 227 PDB 8B50 8B50 1 227 DBREF 8B50 L 1 219 PDB 8B50 8B50 1 219 SEQRES 1 H 227 GLU VAL LYS LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 H 227 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 H 227 PHE ASN ILE LYS ASP THR TYR ILE HIS TRP VAL LYS GLN SEQRES 4 H 227 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ARG ILE ASN SEQRES 5 H 227 SER ALA THR GLY LEU VAL LYS TYR ASP PRO LYS PHE GLN SEQRES 6 H 227 GLY LYS ALA THR ILE THR VAL ASP MET TYR SER ASN ILE SEQRES 7 H 227 ALA TYR LEU ARG LEU THR SER LEU THR SER GLU ASP THR SEQRES 8 H 227 ALA VAL TYR TYR CYS GLY ARG TRP THR PHE PRO ARG TYR SEQRES 9 H 227 PHE ASP LEU TRP GLY ALA GLY THR THR VAL THR VAL SER SEQRES 10 H 227 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 227 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 227 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 227 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 227 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 227 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 227 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 227 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 H 227 HIS HIS HIS HIS HIS HIS SEQRES 1 L 219 ASP ILE GLU LEU THR GLN SER PRO SER SER VAL PRO VAL SEQRES 2 L 219 THR LEU GLY GLU SER VAL SER ILE SER CYS ARG SER SER SEQRES 3 L 219 THR SER LEU LEU HIS SER SER GLY LYS HIS ARG LEU TYR SEQRES 4 L 219 TRP PHE LEU GLN ARG PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 219 ILE TYR TYR VAL SER ASN LEU ALA SER GLY VAL SER ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 ARG ILE SER ARG VAL GLU ALA GLY ASP PHE GLY VAL TYR SEQRES 8 L 219 TYR CYS LEU GLN SER LEU GLU TYR PRO PHE THR PHE GLY SEQRES 9 L 219 SER GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET P0M H 301 18 HET GOL L 301 6 HETNAM P0M (2~{S})-2-AZANYL-3-(7-OXIDANYL-2-OXIDANYLIDENE-CHROMEN- HETNAM 2 P0M 4-YL)PROPANOIC ACID HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 P0M C12 H11 N O5 FORMUL 4 GOL C3 H8 O3 FORMUL 5 HOH *261(H2 O) HELIX 1 AA1 ASN H 28 ASP H 31 5 4 HELIX 2 AA2 PRO H 62 GLN H 65 5 4 HELIX 3 AA3 THR H 87 THR H 91 5 5 HELIX 4 AA4 SER H 161 ALA H 163 5 3 HELIX 5 AA5 SER H 192 LEU H 194 5 3 HELIX 6 AA6 LYS H 206 ASN H 209 5 4 HELIX 7 AA7 GLU L 84 PHE L 88 5 5 HELIX 8 AA8 SER L 126 LYS L 131 1 6 HELIX 9 AA9 LYS L 188 HIS L 194 1 7 SHEET 1 AA1 4 LYS H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA1 4 ILE H 78 LEU H 83 -1 O LEU H 81 N LEU H 20 SHEET 4 AA1 4 ALA H 68 ASP H 73 -1 N ASP H 73 O ILE H 78 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA2 6 ALA H 92 THR H 100 -1 N ALA H 92 O VAL H 114 SHEET 4 AA2 6 TYR H 33 GLN H 39 -1 N HIS H 35 O GLY H 97 SHEET 5 AA2 6 GLU H 46 ASN H 52 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 VAL H 58 TYR H 60 -1 O LYS H 59 N ARG H 50 SHEET 1 AA3 4 GLU H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA3 4 ALA H 92 THR H 100 -1 N ALA H 92 O VAL H 114 SHEET 4 AA3 4 TYR H 104 TRP H 108 -1 O TYR H 104 N THR H 100 SHEET 1 AA4 4 SER H 125 LEU H 129 0 SHEET 2 AA4 4 THR H 140 TYR H 150 -1 O LYS H 148 N SER H 125 SHEET 3 AA4 4 TYR H 181 PRO H 190 -1 O LEU H 183 N VAL H 147 SHEET 4 AA4 4 VAL H 168 THR H 170 -1 N HIS H 169 O VAL H 186 SHEET 1 AA5 4 SER H 125 LEU H 129 0 SHEET 2 AA5 4 THR H 140 TYR H 150 -1 O LYS H 148 N SER H 125 SHEET 3 AA5 4 TYR H 181 PRO H 190 -1 O LEU H 183 N VAL H 147 SHEET 4 AA5 4 VAL H 174 LEU H 175 -1 N VAL H 174 O SER H 182 SHEET 1 AA6 3 THR H 156 TRP H 159 0 SHEET 2 AA6 3 TYR H 199 HIS H 205 -1 O ASN H 202 N SER H 158 SHEET 3 AA6 3 THR H 210 VAL H 216 -1 O VAL H 216 N TYR H 199 SHEET 1 AA7 4 LEU L 4 THR L 5 0 SHEET 2 AA7 4 VAL L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 75 ILE L 80 -1 O PHE L 76 N CYS L 23 SHEET 4 AA7 4 PHE L 67 SER L 72 -1 N SER L 68 O ARG L 79 SHEET 1 AA8 6 SER L 10 THR L 14 0 SHEET 2 AA8 6 THR L 107 LYS L 112 1 O GLU L 110 N VAL L 11 SHEET 3 AA8 6 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AA8 6 LEU L 38 GLN L 43 -1 N PHE L 41 O TYR L 92 SHEET 5 AA8 6 GLN L 50 TYR L 54 -1 O LEU L 52 N TRP L 40 SHEET 6 AA8 6 ASN L 58 LEU L 59 -1 O ASN L 58 N TYR L 54 SHEET 1 AA9 4 SER L 10 THR L 14 0 SHEET 2 AA9 4 THR L 107 LYS L 112 1 O GLU L 110 N VAL L 11 SHEET 3 AA9 4 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AA9 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AB1 4 SER L 119 PHE L 123 0 SHEET 2 AB1 4 THR L 134 PHE L 144 -1 O ASN L 142 N SER L 119 SHEET 3 AB1 4 TYR L 178 SER L 187 -1 O LEU L 184 N VAL L 137 SHEET 4 AB1 4 SER L 164 VAL L 168 -1 N GLN L 165 O THR L 183 SHEET 1 AB2 4 ALA L 158 LEU L 159 0 SHEET 2 AB2 4 LYS L 150 VAL L 155 -1 N VAL L 155 O ALA L 158 SHEET 3 AB2 4 VAL L 196 THR L 202 -1 O GLU L 200 N GLN L 152 SHEET 4 AB2 4 VAL L 210 ASN L 215 -1 O VAL L 210 N VAL L 201 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.12 SSBOND 2 CYS H 145 CYS H 201 1555 1555 2.01 SSBOND 3 CYS H 221 CYS L 219 1555 1555 2.04 SSBOND 4 CYS L 23 CYS L 93 1555 1555 2.13 SSBOND 5 CYS L 139 CYS L 199 1555 1555 2.03 CISPEP 1 PHE H 151 PRO H 152 0 -0.58 CISPEP 2 GLU H 153 PRO H 154 0 -3.59 CISPEP 3 SER L 7 PRO L 8 0 -11.93 CISPEP 4 TYR L 99 PRO L 100 0 -4.79 CISPEP 5 TYR L 145 PRO L 146 0 -1.69 CRYST1 70.914 70.914 91.043 90.00 90.00 120.00 P 31 3 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 0.014102 0.008142 0.000000 0.00000 SCALE2 0.000000 0.016283 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010984 0.00000