HEADER IMMUNE SYSTEM 22-JAN-23 8FWH TITLE CRYSTAL STRUCTURE OF BIVALENT ANTIBODY FAB FRAGMENT OF ANTI-HUMAN LAG3 TITLE 2 (22D2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-HUMAN LAG3 (22D2) HEAVY CHAIN; COMPND 3 CHAIN: HHH; COMPND 4 FRAGMENT: FAB; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ANTI-HUMAN LAG3 (22D2) LIGHT CHAIN; COMPND 8 CHAIN: LLL; COMPND 9 FRAGMENT: FAB; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293 EXPI; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PCDNA 3.4 TOPO; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PLASMID; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_COMMON: MOUSE; SOURCE 14 ORGANISM_TAXID: 10090; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK 293 EXPI; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PCDNA 3.4 TOPO; SOURCE 20 EXPRESSION_SYSTEM_VECTOR: PLASMID KEYWDS FAB, INHIBITORY RECEPTORS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.K.MISHRA,P.AGNIHOTRI,R.A.MARIUZZA JRNL AUTH A.K.MISHRA,S.SHAHID,S.S.KARADE,P.AGNIHOTRI,A.KOLESNIKOV, JRNL AUTH 2 S.S.HASAN,R.A.MARIUZZA JRNL TITL CRYOEM STRUCTURE OF A THERAPEUTIC ANTIBODY (FAVEZELIMAB) JRNL TITL 2 BOUND TO HUMAN LAG3 DETERMINED USING A BIVALENT FAB AS JRNL TITL 3 FIDUCIAL MARKER. JRNL REF STRUCTURE 2023 JRNL REFN ISSN 0969-2126 JRNL PMID 37619561 JRNL DOI 10.1016/J.STR.2023.07.013 REMARK 2 REMARK 2 RESOLUTION. 2.83 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.83 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.75 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9 REMARK 3 NUMBER OF REFLECTIONS : 13587 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) : 0.216 REMARK 3 FREE R VALUE : 0.277 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.196 REMARK 3 FREE R VALUE TEST SET COUNT : 706 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) : 2.83 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.91 REMARK 3 REFLECTION IN BIN (WORKING SET) : 754 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.22 REMARK 3 BIN R VALUE (WORKING SET) : 0.3410 REMARK 3 BIN FREE R VALUE SET COUNT : 47 REMARK 3 BIN FREE R VALUE : 0.4670 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3145 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 4 REMARK 3 SOLVENT ATOMS : 27 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.32 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.80800 REMARK 3 B22 (A**2) : 10.89400 REMARK 3 B33 (A**2) : -5.23000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.69400 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 2.956 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.407 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.365 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.341 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3237 ; 0.007 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 2846 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4434 ; 1.397 ; 1.643 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6561 ; 1.279 ; 1.569 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 428 ; 7.019 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 133 ;38.039 ;23.459 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 447 ;17.024 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;18.474 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 445 ; 0.052 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3754 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 722 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 503 ; 0.236 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 83 ; 0.191 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1535 ; 0.163 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 66 ; 0.146 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.270 ; 0.200 REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1714 ; 6.035 ; 8.417 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1712 ; 6.034 ; 8.413 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2137 ; 9.182 ;12.619 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2137 ; 9.180 ;12.619 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1523 ; 6.332 ; 8.706 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1524 ; 6.330 ; 8.705 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2296 ; 9.767 ;12.911 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2297 ; 9.765 ;12.910 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 : NULL 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 8FWH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000271429. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-MAR-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13587 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.830 REMARK 200 RESOLUTION RANGE LOW (A) : 85.570 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 6WKM REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.26 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, PH 7.5, 0.2 M SODIUM REMARK 280 CHLORIDE, 10% W/V PEG8000, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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 X+1/2,Y+1/2,Z 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 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 1.000000 0.000000 0.000000 79.64350 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.19500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.64350 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.19500 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6920 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 38430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 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 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 GLY H 137 REMARK 465 GLY H 138 REMARK 465 CYS H 220 REMARK 465 ASP H 221 REMARK 465 LYS H 222 REMARK 465 THR H 223 REMARK 465 GLU L 217 REMARK 465 CYS L 218 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 GLU H 1 CG CD OE1 OE2 REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 LYS H 23 CG CD CE NZ REMARK 470 ASP H 31 CG OD1 OD2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 LYS H 63 CG CD CE NZ REMARK 470 LYS H 65 CG CD CE NZ REMARK 470 ASP H 73 CG OD1 OD2 REMARK 470 LYS H 74 CG CD CE NZ REMARK 470 LYS H 205 CG CD CE NZ REMARK 470 LYS H 210 CG CD CE NZ REMARK 470 LYS H 213 CG CD CE NZ REMARK 470 ARG H 214 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 216 CG CD OE1 OE2 REMARK 470 LYS H 218 CG CD CE NZ REMARK 470 THR L 76 O REMARK 470 GLU L 84 CG CD OE1 OE2 REMARK 470 ARG L 112 CG CD NE CZ NH1 NH2 REMARK 470 ASP L 126 CG OD1 OD2 REMARK 470 LYS L 130 CG CD CE NZ REMARK 470 GLU L 147 CG CD OE1 OE2 REMARK 470 LYS L 149 CG CD CE NZ REMARK 470 LYS L 153 CG CD CE NZ REMARK 470 GLN L 164 CG CD OE1 NE2 REMARK 470 GLU L 169 CG CD OE1 OE2 REMARK 470 LYS L 173 CG CD CE NZ REMARK 470 LYS L 187 CG CD CE NZ REMARK 470 GLU L 191 CG CD OE1 OE2 REMARK 470 LYS L 192 CG CD CE NZ REMARK 470 LYS L 194 CG CD CE NZ REMARK 470 ASN L 214 CG OD1 ND2 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 THRLL 76 O HOHLL 401 1.61 REMARK 500 ND2 ASNHH 33 NH1 ARGHH 101 2.04 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THRHH 16 -154.62 -106.48 REMARK 500 CYSHH 22 94.02 -166.07 REMARK 500 PHEHH 29 -63.71 76.70 REMARK 500 LYSHH 43 -166.52 -101.05 REMARK 500 ARGHH 101 -47.10 78.36 REMARK 500 ASPHH 148 70.26 62.48 REMARK 500 THRHH 164 -25.64 -140.28 REMARK 500 SERHH 181 116.91 -162.83 REMARK 500 THRHH 195 -77.62 -121.50 REMARK 500 HISHH 204 73.83 -150.32 REMARK 500 ASPLL 36 55.26 -95.06 REMARK 500 SERLL 56 -47.93 -173.95 REMARK 500 SERLL 69 -116.78 -170.45 REMARK 500 GLULL 85 0.52 -64.96 REMARK 500 ALALL 148 114.33 -165.58 REMARK 500 GLNLL 170 130.56 -38.82 REMARK 500 LYSLL 173 -73.48 -74.51 REMARK 500 SERLL 175 17.09 59.19 REMARK 500 LYSLL 194 -71.04 -116.59 REMARK 500 CYSLL 198 100.98 -170.78 REMARK 500 HISLL 202 145.60 -172.91 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 SERLL 69 GLYLL 70 -147.69 REMARK 500 REMARK 500 REMARK: NULL DBREF 8FWHHH 1 223 PDB 8FWH 8FWH 1 223 DBREF 8FWHLL 1 218 PDB 8FWH 8FWH 1 218 SEQRES 1HH 223 GLU VAL LEU LEU LEU GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2HH 223 PRO GLY THR SER VAL LYS ILE PRO CYS LYS ALA SER GLY SEQRES 3HH 223 TYR THR PHE THR ASP TYR ASN VAL ASP TRP VAL LYS GLN SEQRES 4HH 223 ARG HIS GLY LYS GLY LEU GLU TRP ILE GLY ASP ILE ASN SEQRES 5HH 223 PRO ASN ASN GLY GLY THR ILE TYR SER GLN LYS PHE LYS SEQRES 6HH 223 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7HH 223 ALA PHE MET GLU LEU ARG SER LEU THR SER GLU ASP THR SEQRES 8HH 223 ALA VAL TYR PHE CYS ALA ARG ASN TYR ARG TRP PHE GLY SEQRES 9HH 223 ALA MET ASP HIS TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10HH 223 SER SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11HH 223 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12HH 223 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13HH 223 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14HH 223 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15HH 223 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16HH 223 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17HH 223 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 18HH 223 LYS THR SEQRES 1LL 218 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2LL 218 SER PRO GLY GLN ARG ALA THR ILE SER CYS LYS ALA SER SEQRES 3LL 218 GLN SER LEU ASP TYR GLU GLY ASP SER ASP MET ASN TRP SEQRES 4LL 218 TYR GLN GLN LYS PRO GLY GLN PRO PRO ARG LEU LEU ILE SEQRES 5LL 218 SER GLY ALA SER ASN LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6LL 218 PHE SER GLY SER GLY SER GLY THR ASP PHE THR VAL ASN SEQRES 7LL 218 ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR SEQRES 8LL 218 CYS GLN GLN SER THR GLU ASP PRO ARG THR PHE GLY GLY SEQRES 9LL 218 GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10LL 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11LL 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12LL 218 TYR PRO ARG GLU ALA LYS TYR GLN TRP LYS VAL ASP ASN SEQRES 13LL 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14LL 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15LL 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16LL 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17LL 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET EDO LL 301 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 EDO C2 H6 O2 FORMUL 4 HOH *27(H2 O) HELIX 1 AA1 GLNHH 62 LYSHH 65 5 4 HELIX 2 AA2 THRHH 87 THRHH 91 5 5 HELIX 3 AA3 SERHH 160 ALAHH 162 5 3 HELIX 4 AA4 SERHH 191 THRHH 195 5 5 HELIX 5 AA5 LYSHH 205 ASNHH 208 5 4 HELIX 6 AA6 GLULL 83 ALALL 87 5 5 HELIX 7 AA7 SERLL 125 LYSLL 130 1 6 HELIX 8 AA8 LYSLL 187 LYSLL 192 1 6 SHEET 1 AA1 4 LEUHH 3 LEUHH 5 0 SHEET 2 AA1 4 VALHH 18 SERHH 25 -1 O LYSHH 23 N LEUHH 5 SHEET 3 AA1 4 THRHH 78 LEUHH 83 -1 O METHH 81 N ILEHH 20 SHEET 4 AA1 4 ALAHH 68 ASPHH 73 -1 N THRHH 71 O PHEHH 80 SHEET 1 AA2 6 GLUHH 10 VALHH 12 0 SHEET 2 AA2 6 THRHH 113 VALHH 117 1 O THRHH 116 N GLUHH 10 SHEET 3 AA2 6 ALAHH 92 ASNHH 99 -1 N ALAHH 92 O VALHH 115 SHEET 4 AA2 6 VALHH 34 GLNHH 39 -1 N VALHH 37 O PHEHH 95 SHEET 5 AA2 6 LEUHH 45 ILEHH 51 -1 O ILEHH 48 N TRPHH 36 SHEET 6 AA2 6 THRHH 58 TYRHH 60 -1 O ILEHH 59 N ASPHH 50 SHEET 1 AA3 4 GLUHH 10 VALHH 12 0 SHEET 2 AA3 4 THRHH 113 VALHH 117 1 O THRHH 116 N GLUHH 10 SHEET 3 AA3 4 ALAHH 92 ASNHH 99 -1 N ALAHH 92 O VALHH 115 SHEET 4 AA3 4 METHH 106 TRPHH 109 -1 O ASPHH 107 N ARGHH 98 SHEET 1 AA4 4 SERHH 124 LEUHH 128 0 SHEET 2 AA4 4 ALAHH 140 LYSHH 147 -1 O GLYHH 143 N LEUHH 128 SHEET 3 AA4 4 SERHH 183 VALHH 188 -1 O VALHH 186 N LEUHH 142 SHEET 4 AA4 4 VALHH 167 THRHH 169 -1 N HISHH 168 O VALHH 185 SHEET 1 AA5 3 THRHH 155 TRPHH 158 0 SHEET 2 AA5 3 TYRHH 198 HISHH 204 -1 O ASNHH 203 N THRHH 155 SHEET 3 AA5 3 THRHH 209 VALHH 215 -1 O VALHH 215 N TYRHH 198 SHEET 1 AA6 2 VALHH 173 LEUHH 174 0 SHEET 2 AA6 2 TYRHH 180 SERHH 181 -1 O SERHH 181 N VALHH 173 SHEET 1 AA7 3 LEULL 4 SERLL 7 0 SHEET 2 AA7 3 SERLL 22 ALALL 25 -1 O LYSLL 24 N THRLL 5 SHEET 3 AA7 3 ASPLL 74 PHELL 75 -1 O PHELL 75 N CYSLL 23 SHEET 1 AA8 6 SERLL 10 VALLL 13 0 SHEET 2 AA8 6 THRLL 106 ILELL 110 1 O GLULL 109 N LEULL 11 SHEET 3 AA8 6 ALALL 88 GLNLL 94 -1 N TYRLL 90 O THRLL 106 SHEET 4 AA8 6 METLL 37 GLNLL 42 -1 N ASNLL 38 O GLNLL 93 SHEET 5 AA8 6 ARGLL 49 SERLL 53 -1 O ARGLL 49 N GLNLL 41 SHEET 6 AA8 6 ASNLL 57 LEULL 58 -1 O ASNLL 57 N SERLL 53 SHEET 1 AA9 4 SERLL 10 VALLL 13 0 SHEET 2 AA9 4 THRLL 106 ILELL 110 1 O GLULL 109 N LEULL 11 SHEET 3 AA9 4 ALALL 88 GLNLL 94 -1 N TYRLL 90 O THRLL 106 SHEET 4 AA9 4 THRLL 101 PHELL 102 -1 O THRLL 101 N GLNLL 94 SHEET 1 AB1 3 ALALL 19 THRLL 20 0 SHEET 2 AB1 3 ASNLL 78 ILELL 79 -1 O ILELL 79 N ALALL 19 SHEET 3 AB1 3 PHELL 66 SERLL 67 -1 N SERLL 67 O ASNLL 78 SHEET 1 AB2 2 ASPLL 30 TYRLL 31 0 SHEET 2 AB2 2 ASPLL 34 SERLL 35 -1 O ASPLL 34 N TYRLL 31 SHEET 1 AB3 4 SERLL 118 PHELL 122 0 SHEET 2 AB3 4 THRLL 133 PHELL 143 -1 O LEULL 139 N PHELL 120 SHEET 3 AB3 4 TYRLL 177 SERLL 186 -1 O LEULL 179 N LEULL 140 SHEET 4 AB3 4 SERLL 163 VALLL 167 -1 N GLNLL 164 O THRLL 182 SHEET 1 AB4 3 TYRLL 150 VALLL 154 0 SHEET 2 AB4 3 TYRLL 196 VALLL 200 -1 O GLULL 199 N GLNLL 151 SHEET 3 AB4 3 VALLL 209 PHELL 213 -1 O VALLL 209 N VALLL 200 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.02 SSBOND 2 CYSHH 144 CYSHH 200 1555 1555 2.05 SSBOND 3 CYSLL 23 CYSLL 92 1555 1555 2.12 SSBOND 4 CYSLL 138 CYSLL 198 1555 1555 2.05 CISPEP 1 PHEHH 150 PROHH 151 0 -13.85 CISPEP 2 GLUHH 152 PROHH 153 0 -7.06 CISPEP 3 SERLL 7 PROLL 8 0 6.19 CISPEP 4 HISLL 80 PROLL 81 0 -2.72 CISPEP 5 ASPLL 98 PROLL 99 0 12.28 CISPEP 6 TYRLL 144 PROLL 145 0 9.37 CRYST1 159.287 44.390 89.084 90.00 106.14 90.00 C 1 2 1 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 0.006278 0.000000 0.001816 0.00000 SCALE2 0.000000 0.022528 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011686 0.00000