HEADER IMMUNE SYSTEM 09-MAY-23 8JBJ TITLE CRYSTAL STRUCTURE OF ANTI-PVRIG FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY HEAVY CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY LIGHT CHAIN; COMPND 7 CHAIN: B, D; 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 ANTIBODY, IMMUNOTHERAPY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.SUN,X.L.LI,J.SONG REVDAT 1 21-JUN-23 8JBJ 0 JRNL AUTH M.YI,J.SUN,H.SUN,Y.WANG,S.HOU,B.JIANG,Y.XIE,R.JI,L.XUE, JRNL AUTH 2 X.DING,X.SONG,A.XU,C.HUANG,Q.QUAN,J.SONG JRNL TITL IDENTIFICATION AND CHARACTERIZATION OF AN UNEXPECTED JRNL TITL 2 ISOMERIZATION MOTIF IN CDRH2 THAT AFFECTS ANTIBODY ACTIVITY. JRNL REF MABS V. 15 15364 2023 JRNL REFN ESSN 1942-0870 JRNL PMID 37229604 JRNL DOI 10.1080/19420862.2023.2215364 REMARK 2 REMARK 2 RESOLUTION. 1.61 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.17.1_3660: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.18 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.7 REMARK 3 NUMBER OF REFLECTIONS : 104034 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 5192 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 49.1800 - 5.0100 1.00 4193 222 0.1668 0.1741 REMARK 3 2 5.0100 - 3.9800 1.00 4028 185 0.1413 0.1901 REMARK 3 3 3.9800 - 3.4700 1.00 3982 200 0.1690 0.2238 REMARK 3 4 3.4700 - 3.1600 1.00 3962 205 0.1746 0.2108 REMARK 3 5 3.1600 - 2.9300 1.00 3872 218 0.1825 0.2328 REMARK 3 6 2.9300 - 2.7600 1.00 3943 209 0.1992 0.2231 REMARK 3 7 2.7600 - 2.6200 1.00 3915 185 0.1918 0.2549 REMARK 3 8 2.6200 - 2.5000 1.00 3903 220 0.1948 0.2425 REMARK 3 9 2.5000 - 2.4100 1.00 3867 216 0.1972 0.2648 REMARK 3 10 2.4100 - 2.3300 1.00 3884 191 0.2010 0.2416 REMARK 3 11 2.3300 - 2.2500 1.00 3889 214 0.2015 0.2573 REMARK 3 12 2.2500 - 2.1900 1.00 3867 230 0.1970 0.2462 REMARK 3 13 2.1900 - 2.1300 1.00 3859 199 0.2059 0.2430 REMARK 3 14 2.1300 - 2.0800 1.00 3858 205 0.2002 0.2491 REMARK 3 15 2.0800 - 2.0300 1.00 3881 211 0.2130 0.2458 REMARK 3 16 2.0300 - 1.9900 1.00 3848 218 0.2042 0.2348 REMARK 3 17 1.9900 - 1.9500 1.00 3866 200 0.2052 0.2228 REMARK 3 18 1.9500 - 1.9100 0.99 3812 215 0.2102 0.2478 REMARK 3 19 1.9100 - 1.8800 0.94 3629 187 0.2162 0.2544 REMARK 3 20 1.8800 - 1.8500 0.89 3429 164 0.2225 0.2687 REMARK 3 21 1.8500 - 1.8200 0.83 3213 162 0.2309 0.2570 REMARK 3 22 1.8200 - 1.7900 0.77 2960 155 0.2469 0.2902 REMARK 3 23 1.7900 - 1.7600 0.69 2676 159 0.2597 0.2916 REMARK 3 24 1.7600 - 1.7400 0.64 2444 130 0.2404 0.2757 REMARK 3 25 1.7400 - 1.7100 0.57 2205 116 0.2458 0.2528 REMARK 3 26 1.7100 - 1.6900 0.52 1963 100 0.2434 0.2705 REMARK 3 27 1.6900 - 1.6700 0.46 1776 100 0.2605 0.2730 REMARK 3 28 1.6700 - 1.6500 0.41 1581 72 0.2666 0.2890 REMARK 3 29 1.6500 - 1.6300 0.36 1404 53 0.2669 0.3067 REMARK 3 30 1.6300 - 1.6100 0.29 1133 51 0.2962 0.4225 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.770 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 6749 REMARK 3 ANGLE : 0.827 9192 REMARK 3 CHIRALITY : 0.056 1050 REMARK 3 PLANARITY : 0.005 1168 REMARK 3 DIHEDRAL : 10.316 927 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 18.7490 39.5259 71.9927 REMARK 3 T TENSOR REMARK 3 T11: 0.1977 T22: 0.1973 REMARK 3 T33: 0.1852 T12: 0.0636 REMARK 3 T13: -0.0361 T23: -0.0023 REMARK 3 L TENSOR REMARK 3 L11: 0.1428 L22: 0.1814 REMARK 3 L33: 0.0537 L12: 0.0541 REMARK 3 L13: 0.0100 L23: 0.0578 REMARK 3 S TENSOR REMARK 3 S11: 0.0077 S12: -0.0218 S13: -0.0230 REMARK 3 S21: -0.0436 S22: -0.0061 S23: 0.0311 REMARK 3 S31: -0.0097 S32: -0.0202 S33: -0.0000 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8JBJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 16-MAY-23. REMARK 100 THE DEPOSITION ID IS D_1300037565. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-APR-22 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : 7.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL45XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122876 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.6 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : 0.11700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.76700 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG3350, 0.4 M POTASSIUM FORMATE, REMARK 280 PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.13400 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.21200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.20400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.21200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.13400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.20400 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 3490 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 REMARK 350 BIOMOLECULE: 2 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: 3290 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 CYS A 225 REMARK 465 HIS A 226 REMARK 465 HIS A 227 REMARK 465 HIS A 228 REMARK 465 HIS A 229 REMARK 465 HIS A 230 REMARK 465 HIS A 231 REMARK 465 CYS B 213 REMARK 465 SER C 137 REMARK 465 LYS C 138 REMARK 465 SER C 139 REMARK 465 THR C 140 REMARK 465 LYS C 223 REMARK 465 SER C 224 REMARK 465 CYS C 225 REMARK 465 HIS C 226 REMARK 465 HIS C 227 REMARK 465 HIS C 228 REMARK 465 HIS C 229 REMARK 465 HIS C 230 REMARK 465 HIS C 231 REMARK 465 GLU D 212 REMARK 465 CYS D 213 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 ARG C 65 CG CD NE CZ NH1 NH2 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 NZ LYS A 223 O HOH A 301 1.93 REMARK 500 O PRO B 119 O HOH A 301 2.06 REMARK 500 O HOH A 510 O HOH A 560 2.12 REMARK 500 O HOH A 332 O HOH A 546 2.13 REMARK 500 O HOH D 301 O HOH D 323 2.17 REMARK 500 O HOH C 416 O HOH C 494 2.18 REMARK 500 O HOH B 348 O HOH B 538 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 NE2 GLN A 201 O HOH D 391 1655 2.14 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 CYS A 149 CA - CB - SG ANGL. DEV. = 7.8 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 THR B 50 -44.50 79.81 REMARK 500 SER B 76 67.51 39.20 REMARK 500 ALA B 83 -178.26 -176.93 REMARK 500 ARG C 65 61.54 32.41 REMARK 500 THR D 50 -46.34 74.11 REMARK 500 ALA D 83 -179.85 177.84 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 598 DISTANCE = 5.91 ANGSTROMS REMARK 525 HOH B 569 DISTANCE = 5.82 ANGSTROMS REMARK 525 HOH D 523 DISTANCE = 6.41 ANGSTROMS DBREF 8JBJ A 1 231 PDB 8JBJ 8JBJ 1 231 DBREF 8JBJ B 1 213 PDB 8JBJ 8JBJ 1 213 DBREF 8JBJ C 1 231 PDB 8JBJ 8JBJ 1 231 DBREF 8JBJ D 1 213 PDB 8JBJ 8JBJ 1 213 SEQRES 1 A 231 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 231 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 231 TYR THR PHE THR ASP TYR TRP ILE TYR TRP VAL ARG GLN SEQRES 4 A 231 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY THR ILE ASP SEQRES 5 A 231 THR SER ASP HIS LYS THR SER TYR ASN GLN LYS PHE ARG SEQRES 6 A 231 GLY ARG VAL THR MET THR ARG ASP THR SER THR SER THR SEQRES 7 A 231 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 A 231 ALA VAL TYR TYR CYS ALA ARG ASP PHE ILE ILE THR VAL SEQRES 9 A 231 ASN TYR PRO VAL VAL ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 A 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 A 231 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 A 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 A 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 A 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 A 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 A 231 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 A 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 A 231 PRO LYS SER CYS HIS HIS HIS HIS HIS HIS SEQRES 1 B 213 GLN ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 B 213 SER PRO GLY GLU ARG ALA THR LEU SER CYS SER ALA GLY SEQRES 3 B 213 SER SER VAL ASN TYR MET HIS TRP PHE GLN GLN LYS PRO SEQRES 4 B 213 GLY GLN ALA PRO ARG LEU LEU ILE TYR SER THR SER ASN SEQRES 5 B 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 B 213 SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU GLU SEQRES 7 B 213 PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SER SEQRES 8 B 213 SER LEU PRO PHE THR PHE GLY GLN GLY THR LYS LEU GLU SEQRES 9 B 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 B 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 B 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 B 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 B 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 B 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 B 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 B 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 B 213 ASN ARG GLY GLU CYS SEQRES 1 C 231 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 231 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 231 TYR THR PHE THR ASP TYR TRP ILE TYR TRP VAL ARG GLN SEQRES 4 C 231 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY THR ILE ASP SEQRES 5 C 231 THR SER ASP HIS LYS THR SER TYR ASN GLN LYS PHE ARG SEQRES 6 C 231 GLY ARG VAL THR MET THR ARG ASP THR SER THR SER THR SEQRES 7 C 231 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 C 231 ALA VAL TYR TYR CYS ALA ARG ASP PHE ILE ILE THR VAL SEQRES 9 C 231 ASN TYR PRO VAL VAL ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 C 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 231 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 231 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 C 231 PRO LYS SER CYS HIS HIS HIS HIS HIS HIS SEQRES 1 D 213 GLN ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 D 213 SER PRO GLY GLU ARG ALA THR LEU SER CYS SER ALA GLY SEQRES 3 D 213 SER SER VAL ASN TYR MET HIS TRP PHE GLN GLN LYS PRO SEQRES 4 D 213 GLY GLN ALA PRO ARG LEU LEU ILE TYR SER THR SER ASN SEQRES 5 D 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 D 213 SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU GLU SEQRES 7 D 213 PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SER SEQRES 8 D 213 SER LEU PRO PHE THR PHE GLY GLN GLY THR LYS LEU GLU SEQRES 9 D 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 D 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 D 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 D 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 D 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 D 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 D 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 D 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 D 213 ASN ARG GLY GLU CYS FORMUL 5 HOH *990(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 GLN A 62 ARG A 65 5 4 HELIX 3 AA3 ARG A 87 THR A 91 5 5 HELIX 4 AA4 SER A 165 ALA A 167 5 3 HELIX 5 AA5 SER A 196 LEU A 198 5 3 HELIX 6 AA6 LYS A 210 ASN A 213 5 4 HELIX 7 AA7 GLU B 78 PHE B 82 5 5 HELIX 8 AA8 SER B 120 SER B 126 1 7 HELIX 9 AA9 LYS B 182 LYS B 187 1 6 HELIX 10 AB1 THR C 28 TYR C 32 5 5 HELIX 11 AB2 GLN C 62 ARG C 65 5 4 HELIX 12 AB3 THR C 74 THR C 76 5 3 HELIX 13 AB4 ARG C 87 THR C 91 5 5 HELIX 14 AB5 SER C 196 LEU C 198 5 3 HELIX 15 AB6 LYS C 210 ASN C 213 5 4 HELIX 16 AB7 GLU D 78 PHE D 82 5 5 HELIX 17 AB8 SER D 120 LYS D 125 1 6 HELIX 18 AB9 LYS D 182 LYS D 187 1 6 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O MET A 81 N VAL A 20 SHEET 4 AA1 4 VAL A 68 ASP A 73 -1 N THR A 69 O GLU A 82 SHEET 1 AA2 6 GLU A 10 LYS A 12 0 SHEET 2 AA2 6 THR A 116 VAL A 120 1 O THR A 119 N LYS A 12 SHEET 3 AA2 6 ALA A 92 ARG A 98 -1 N TYR A 94 O THR A 116 SHEET 4 AA2 6 ILE A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 GLU A 46 ILE A 51 -1 O MET A 48 N TRP A 36 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O SER A 59 N THR A 50 SHEET 1 AA3 4 SER A 129 LEU A 133 0 SHEET 2 AA3 4 THR A 144 TYR A 154 -1 O LEU A 150 N PHE A 131 SHEET 3 AA3 4 TYR A 185 PRO A 194 -1 O LEU A 187 N VAL A 151 SHEET 4 AA3 4 VAL A 172 THR A 174 -1 N HIS A 173 O VAL A 190 SHEET 1 AA4 4 SER A 129 LEU A 133 0 SHEET 2 AA4 4 THR A 144 TYR A 154 -1 O LEU A 150 N PHE A 131 SHEET 3 AA4 4 TYR A 185 PRO A 194 -1 O LEU A 187 N VAL A 151 SHEET 4 AA4 4 VAL A 178 LEU A 179 -1 N VAL A 178 O SER A 186 SHEET 1 AA5 3 THR A 160 TRP A 163 0 SHEET 2 AA5 3 ILE A 204 HIS A 209 -1 O ASN A 206 N SER A 162 SHEET 3 AA5 3 THR A 214 LYS A 219 -1 O VAL A 216 N VAL A 207 SHEET 1 AA6 4 LEU B 4 SER B 7 0 SHEET 2 AA6 4 ALA B 19 ALA B 25 -1 O SER B 24 N THR B 5 SHEET 3 AA6 4 ASP B 69 ILE B 74 -1 O LEU B 72 N LEU B 21 SHEET 4 AA6 4 PHE B 61 SER B 66 -1 N SER B 62 O THR B 73 SHEET 1 AA7 6 THR B 10 LEU B 13 0 SHEET 2 AA7 6 THR B 101 ILE B 105 1 O LYS B 102 N LEU B 11 SHEET 3 AA7 6 ALA B 83 GLN B 89 -1 N ALA B 83 O LEU B 103 SHEET 4 AA7 6 HIS B 33 GLN B 37 -1 N PHE B 35 O TYR B 86 SHEET 5 AA7 6 ARG B 44 TYR B 48 -1 O LEU B 46 N TRP B 34 SHEET 6 AA7 6 ASN B 52 LEU B 53 -1 O ASN B 52 N TYR B 48 SHEET 1 AA8 4 THR B 10 LEU B 13 0 SHEET 2 AA8 4 THR B 101 ILE B 105 1 O LYS B 102 N LEU B 11 SHEET 3 AA8 4 ALA B 83 GLN B 89 -1 N ALA B 83 O LEU B 103 SHEET 4 AA8 4 THR B 96 PHE B 97 -1 O THR B 96 N GLN B 89 SHEET 1 AA9 4 SER B 113 PHE B 117 0 SHEET 2 AA9 4 THR B 128 PHE B 138 -1 O LEU B 134 N PHE B 115 SHEET 3 AA9 4 TYR B 172 SER B 181 -1 O LEU B 174 N LEU B 135 SHEET 4 AA9 4 SER B 158 VAL B 162 -1 N GLN B 159 O THR B 177 SHEET 1 AB1 4 ALA B 152 LEU B 153 0 SHEET 2 AB1 4 LYS B 144 VAL B 149 -1 N VAL B 149 O ALA B 152 SHEET 3 AB1 4 VAL B 190 THR B 196 -1 O GLU B 194 N GLN B 146 SHEET 4 AB1 4 VAL B 204 ASN B 209 -1 O VAL B 204 N VAL B 195 SHEET 1 AB2 4 GLN C 3 GLN C 6 0 SHEET 2 AB2 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AB2 4 THR C 78 LEU C 83 -1 O MET C 81 N VAL C 20 SHEET 4 AB2 4 VAL C 68 ASP C 73 -1 N THR C 69 O GLU C 82 SHEET 1 AB3 6 GLU C 10 LYS C 12 0 SHEET 2 AB3 6 THR C 116 VAL C 120 1 O THR C 119 N LYS C 12 SHEET 3 AB3 6 ALA C 92 ARG C 98 -1 N TYR C 94 O THR C 116 SHEET 4 AB3 6 ILE C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AB3 6 LEU C 45 ILE C 51 -1 O MET C 48 N TRP C 36 SHEET 6 AB3 6 THR C 58 TYR C 60 -1 O SER C 59 N THR C 50 SHEET 1 AB4 4 GLU C 10 LYS C 12 0 SHEET 2 AB4 4 THR C 116 VAL C 120 1 O THR C 119 N LYS C 12 SHEET 3 AB4 4 ALA C 92 ARG C 98 -1 N TYR C 94 O THR C 116 SHEET 4 AB4 4 TYR C 111 TRP C 112 -1 O TYR C 111 N ARG C 98 SHEET 1 AB5 4 SER C 129 LEU C 133 0 SHEET 2 AB5 4 THR C 144 TYR C 154 -1 O GLY C 148 N LEU C 133 SHEET 3 AB5 4 TYR C 185 PRO C 194 -1 O VAL C 193 N ALA C 145 SHEET 4 AB5 4 VAL C 172 THR C 174 -1 N HIS C 173 O VAL C 190 SHEET 1 AB6 4 SER C 129 LEU C 133 0 SHEET 2 AB6 4 THR C 144 TYR C 154 -1 O GLY C 148 N LEU C 133 SHEET 3 AB6 4 TYR C 185 PRO C 194 -1 O VAL C 193 N ALA C 145 SHEET 4 AB6 4 VAL C 178 LEU C 179 -1 N VAL C 178 O SER C 186 SHEET 1 AB7 3 THR C 160 TRP C 163 0 SHEET 2 AB7 3 ILE C 204 HIS C 209 -1 O ASN C 206 N SER C 162 SHEET 3 AB7 3 THR C 214 LYS C 219 -1 O VAL C 216 N VAL C 207 SHEET 1 AB8 4 LEU D 4 SER D 7 0 SHEET 2 AB8 4 ALA D 19 ALA D 25 -1 O SER D 24 N THR D 5 SHEET 3 AB8 4 ASP D 69 ILE D 74 -1 O LEU D 72 N LEU D 21 SHEET 4 AB8 4 PHE D 61 SER D 66 -1 N SER D 64 O THR D 71 SHEET 1 AB9 6 THR D 10 LEU D 13 0 SHEET 2 AB9 6 THR D 101 ILE D 105 1 O GLU D 104 N LEU D 11 SHEET 3 AB9 6 ALA D 83 GLN D 89 -1 N ALA D 83 O LEU D 103 SHEET 4 AB9 6 HIS D 33 GLN D 37 -1 N PHE D 35 O TYR D 86 SHEET 5 AB9 6 ARG D 44 TYR D 48 -1 O LEU D 46 N TRP D 34 SHEET 6 AB9 6 ASN D 52 LEU D 53 -1 O ASN D 52 N TYR D 48 SHEET 1 AC1 4 THR D 10 LEU D 13 0 SHEET 2 AC1 4 THR D 101 ILE D 105 1 O GLU D 104 N LEU D 11 SHEET 3 AC1 4 ALA D 83 GLN D 89 -1 N ALA D 83 O LEU D 103 SHEET 4 AC1 4 THR D 96 PHE D 97 -1 O THR D 96 N GLN D 89 SHEET 1 AC2 4 SER D 113 PHE D 117 0 SHEET 2 AC2 4 THR D 128 PHE D 138 -1 O LEU D 134 N PHE D 115 SHEET 3 AC2 4 TYR D 172 SER D 181 -1 O LEU D 180 N ALA D 129 SHEET 4 AC2 4 SER D 158 VAL D 162 -1 N GLN D 159 O THR D 177 SHEET 1 AC3 4 ALA D 152 LEU D 153 0 SHEET 2 AC3 4 LYS D 144 VAL D 149 -1 N VAL D 149 O ALA D 152 SHEET 3 AC3 4 VAL D 190 THR D 196 -1 O GLU D 194 N GLN D 146 SHEET 4 AC3 4 VAL D 204 ASN D 209 -1 O VAL D 204 N VAL D 195 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS A 149 CYS A 205 1555 1555 2.07 SSBOND 3 CYS B 23 CYS B 87 1555 1555 2.05 SSBOND 4 CYS B 133 CYS B 193 1555 1555 2.05 SSBOND 5 CYS C 22 CYS C 96 1555 1555 2.05 SSBOND 6 CYS C 149 CYS C 205 1555 1555 2.04 SSBOND 7 CYS D 23 CYS D 87 1555 1555 2.07 SSBOND 8 CYS D 133 CYS D 193 1555 1555 2.06 CISPEP 1 PHE A 155 PRO A 156 0 -7.13 CISPEP 2 GLU A 157 PRO A 158 0 -0.59 CISPEP 3 SER B 7 PRO B 8 0 -7.13 CISPEP 4 LEU B 93 PRO B 94 0 -3.44 CISPEP 5 TYR B 139 PRO B 140 0 3.37 CISPEP 6 PHE C 155 PRO C 156 0 -8.53 CISPEP 7 GLU C 157 PRO C 158 0 0.56 CISPEP 8 SER D 7 PRO D 8 0 -4.64 CISPEP 9 LEU D 93 PRO D 94 0 -5.30 CISPEP 10 TYR D 139 PRO D 140 0 3.89 CRYST1 64.268 76.408 192.424 90.00 90.00 90.00 P 21 21 21 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 0.015560 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013088 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005197 0.00000