HEADER VIRAL PROTEIN 07-FEB-21 7NFQ TITLE FUJIAN CAPMIDLINK DOMAIN IN COMPLEX WITH NB8193 COMPND MOL_ID: 1; COMPND 2 MOLECULE: POLYMERASE BASIC PROTEIN 2; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: RNA-DIRECTED RNA POLYMERASE SUBUNIT P3; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NB8193; COMPND 8 CHAIN: C, D; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/DUCK/FUJIAN/13/2002(H5N1) SOURCE 3 ); SOURCE 4 ORGANISM_TAXID: 274828; SOURCE 5 GENE: PB2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: CAMELIDAE MIXED LIBRARY; SOURCE 10 ORGANISM_TAXID: 1579311; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS INFLUENZA POLYMERASE, CAP-BINDING DOMAIN, NANOBODY, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.R.KEOWN,J.M.GRIMES,E.FODOR REVDAT 1 01-DEC-21 7NFQ 0 JRNL AUTH J.R.KEOWN,J.M.GRIMES,E.FODOR JRNL TITL FUJIAN CAPMIDLINK DOMAIN IN COMPLEX WITH NB8193 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.18RC2_3794 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.31 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 70.3 REMARK 3 NUMBER OF REFLECTIONS : 69134 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.169 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 3442 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 44.3100 - 4.9200 1.00 3794 225 0.1645 0.1982 REMARK 3 2 4.9200 - 3.9000 1.00 3731 207 0.1248 0.1478 REMARK 3 3 3.9000 - 3.4100 1.00 3774 201 0.1484 0.1778 REMARK 3 4 3.4100 - 3.1000 1.00 3734 191 0.1706 0.2355 REMARK 3 5 3.1000 - 2.8800 1.00 3739 204 0.1832 0.2341 REMARK 3 6 2.8800 - 2.7100 1.00 3766 183 0.1905 0.2144 REMARK 3 7 2.7100 - 2.5700 1.00 3752 199 0.1799 0.2181 REMARK 3 8 2.5700 - 2.4600 1.00 3691 204 0.1805 0.2153 REMARK 3 9 2.4600 - 2.3700 1.00 3718 188 0.1753 0.2454 REMARK 3 10 2.3700 - 2.2800 1.00 3794 190 0.1739 0.2580 REMARK 3 11 2.2800 - 2.2100 1.00 3736 186 0.1758 0.2114 REMARK 3 12 2.2100 - 2.1500 0.98 3673 169 0.1740 0.2170 REMARK 3 13 2.1500 - 2.0900 0.91 3407 168 0.1836 0.2371 REMARK 3 14 2.0900 - 2.0400 0.81 3013 153 0.1890 0.2071 REMARK 3 15 2.0400 - 2.0000 0.71 2698 142 0.1942 0.2438 REMARK 3 16 2.0000 - 1.9500 0.64 2384 122 0.1979 0.2107 REMARK 3 17 1.9500 - 1.9100 0.55 2047 95 0.2018 0.2447 REMARK 3 18 1.9100 - 1.8800 0.47 1771 91 0.2278 0.2672 REMARK 3 19 1.8800 - 1.8400 0.39 1446 82 0.2321 0.2587 REMARK 3 20 1.8400 - 1.8100 0.33 1255 67 0.2433 0.3331 REMARK 3 21 1.8100 - 1.7800 0.27 999 57 0.2654 0.3240 REMARK 3 22 1.7800 - 1.7600 0.20 744 51 0.2964 0.3905 REMARK 3 23 1.7600 - 1.7300 0.15 546 37 0.3328 0.3049 REMARK 3 24 1.7300 - 1.7100 0.09 331 17 0.3774 0.4175 REMARK 3 25 1.7100 - 1.6800 0.04 149 13 0.3249 0.4557 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) : 0.173 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.966 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.16 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.39 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 : 0.013 6326 REMARK 3 ANGLE : 1.209 8522 REMARK 3 CHIRALITY : 0.064 966 REMARK 3 PLANARITY : 0.008 1105 REMARK 3 DIHEDRAL : 21.900 895 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): 4.5888 10.3510 18.7829 REMARK 3 T TENSOR REMARK 3 T11: 0.2107 T22: 0.1975 REMARK 3 T33: 0.2768 T12: 0.0057 REMARK 3 T13: -0.0096 T23: 0.0018 REMARK 3 L TENSOR REMARK 3 L11: 0.0417 L22: 0.0123 REMARK 3 L33: 0.6820 L12: 0.0223 REMARK 3 L13: -0.0987 L23: -0.1092 REMARK 3 S TENSOR REMARK 3 S11: 0.0006 S12: -0.0191 S13: 0.0100 REMARK 3 S21: 0.0292 S22: -0.0038 S23: -0.0240 REMARK 3 S31: -0.0431 S32: 0.0537 S33: 0.0046 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 7NFQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-21. REMARK 100 THE DEPOSITION ID IS D_1292113865. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-MAY-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69149 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680 REMARK 200 RESOLUTION RANGE LOW (A) : 44.310 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 70.3 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.1700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74 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: 6S5V REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3350 AND 0.2 M (NH4)2 REMARK 280 CITRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 53.27150 REMARK 290 SMTRY3 2 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 APPLY THE FOLLOWING TO CHAINS: A, C 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 APPLY THE FOLLOWING TO CHAINS: B, 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 HIS A 233 REMARK 465 HIS A 234 REMARK 465 HIS A 235 REMARK 465 HIS A 236 REMARK 465 HIS A 237 REMARK 465 HIS A 238 REMARK 465 GLY A 239 REMARK 465 GLU A 240 REMARK 465 ASN A 241 REMARK 465 LEU A 242 REMARK 465 TYR A 243 REMARK 465 PHE A 244 REMARK 465 GLN A 245 REMARK 465 GLY A 246 REMARK 465 GLY A 247 REMARK 465 GLY A 248 REMARK 465 GLU A 249 REMARK 465 VAL A 250 REMARK 465 ARG A 251 REMARK 465 TYR A 488 REMARK 465 SER A 489 REMARK 465 SER A 533 REMARK 465 SER A 534 REMARK 465 MET A 535 REMARK 465 MET A 536 REMARK 465 SER C 117 REMARK 465 HIS C 118 REMARK 465 HIS C 119 REMARK 465 HIS C 120 REMARK 465 HIS C 121 REMARK 465 HIS C 122 REMARK 465 HIS C 123 REMARK 465 GLU C 124 REMARK 465 PRO C 125 REMARK 465 GLU C 126 REMARK 465 ALA C 127 REMARK 465 HIS B 233 REMARK 465 HIS B 234 REMARK 465 HIS B 235 REMARK 465 HIS B 236 REMARK 465 HIS B 237 REMARK 465 HIS B 238 REMARK 465 GLY B 239 REMARK 465 GLU B 240 REMARK 465 ASN B 241 REMARK 465 LEU B 242 REMARK 465 TYR B 243 REMARK 465 PHE B 244 REMARK 465 GLN B 245 REMARK 465 GLY B 246 REMARK 465 GLY B 247 REMARK 465 GLY B 248 REMARK 465 GLU B 249 REMARK 465 VAL B 250 REMARK 465 SER B 533 REMARK 465 SER B 534 REMARK 465 MET B 535 REMARK 465 MET B 536 REMARK 465 SER D 117 REMARK 465 HIS D 118 REMARK 465 HIS D 119 REMARK 465 HIS D 120 REMARK 465 HIS D 121 REMARK 465 HIS D 122 REMARK 465 HIS D 123 REMARK 465 GLU D 124 REMARK 465 PRO D 125 REMARK 465 GLU D 126 REMARK 465 ALA D 127 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 O LEU B 418 HH22 ARG B 427 1.59 REMARK 500 O HOH C 252 O HOH B 873 2.11 REMARK 500 O HOH D 480 O HOH D 482 2.16 REMARK 500 O HOH A 783 O HOH A 832 2.18 REMARK 500 O HOH D 468 O HOH D 475 2.18 REMARK 500 O HOH B 925 O HOH B 937 2.19 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 CYS C 96 CB CYS C 96 SG -0.113 REMARK 500 CYS D 96 CB CYS D 96 SG -0.131 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 MET A 431 CG - SD - CE ANGL. DEV. = 15.8 DEGREES REMARK 500 ASP A 499 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES REMARK 500 MET C 83 CG - SD - CE ANGL. DEV. = 12.8 DEGREES REMARK 500 ASP B 506 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES REMARK 500 CYS D 96 CA - CB - SG ANGL. DEV. = 7.4 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 ALA A 377 -168.72 -126.55 REMARK 500 ALA C 92 162.45 175.72 REMARK 500 ALA B 377 -167.35 -126.36 REMARK 500 REMARK 500 REMARK: NULL DBREF 7NFQ A 247 536 UNP Q6E3N3 Q6E3N3_9INFA 247 536 DBREF 7NFQ C 1 127 PDB 7NFQ 7NFQ 1 127 DBREF 7NFQ B 247 536 UNP Q6E3N3 Q6E3N3_9INFA 247 536 DBREF 7NFQ D 1 127 PDB 7NFQ 7NFQ 1 127 SEQADV 7NFQ HIS A 233 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS A 234 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS A 235 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS A 236 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS A 237 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS A 238 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ GLY A 239 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ GLU A 240 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ ASN A 241 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ LEU A 242 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ TYR A 243 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ PHE A 244 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ GLN A 245 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ GLY A 246 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS B 233 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS B 234 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS B 235 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS B 236 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS B 237 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ HIS B 238 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ GLY B 239 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ GLU B 240 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ ASN B 241 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ LEU B 242 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ TYR B 243 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ PHE B 244 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ GLN B 245 UNP Q6E3N3 EXPRESSION TAG SEQADV 7NFQ GLY B 246 UNP Q6E3N3 EXPRESSION TAG SEQRES 1 A 304 HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE GLN SEQRES 2 A 304 GLY GLY GLY GLU VAL ARG ASN ASP ASP VAL ASP GLN SER SEQRES 3 A 304 LEU ILE ILE ALA ALA ARG ASN ILE VAL ARG ARG ALA THR SEQRES 4 A 304 VAL SER THR ASP PRO LEU ALA SER LEU LEU GLU MET CYS SEQRES 5 A 304 HIS SER THR GLN ILE GLY GLY ILE ARG MET VAL ASP ILE SEQRES 6 A 304 LEU ARG GLN ASN PRO THR GLU GLU GLN ALA VAL ASP ILE SEQRES 7 A 304 CYS LYS ALA ALA MET GLY LEU ARG ILE SER SER SER PHE SEQRES 8 A 304 SER PHE GLY GLY PHE THR PHE LYS ARG THR SER GLY SER SEQRES 9 A 304 SER VAL LYS LYS GLU GLU GLU VAL LEU THR GLY ASN LEU SEQRES 10 A 304 GLN THR LEU LYS ILE ARG VAL HIS GLU GLY TYR GLU GLU SEQRES 11 A 304 PHE THR MET VAL GLY ARG ARG ALA THR ALA ILE LEU ARG SEQRES 12 A 304 LYS ALA THR ARG ARG LEU ILE GLN LEU ILE VAL SER GLY SEQRES 13 A 304 ARG ASP GLU GLN SER ILE ALA GLU ALA ILE ILE VAL ALA SEQRES 14 A 304 MET VAL PHE SER GLN GLU ASP CYS MET ILE LYS ALA VAL SEQRES 15 A 304 ARG GLY ASP LEU ASN PHE VAL ASN ARG ALA ASN GLN ARG SEQRES 16 A 304 LEU ASN PRO MET HIS GLN LEU LEU ARG HIS PHE GLN LYS SEQRES 17 A 304 ASP ALA LYS VAL LEU PHE GLN ASN TRP GLY ILE GLU PRO SEQRES 18 A 304 ILE ASP ASN VAL MET GLY MET ILE GLY ILE LEU PRO ASP SEQRES 19 A 304 MET THR PRO SER THR GLU MET SER LEU ARG GLY VAL ARG SEQRES 20 A 304 VAL SER LYS MET GLY VAL ASP GLU TYR SER SER THR GLU SEQRES 21 A 304 ARG VAL VAL VAL SER ILE ASP ARG PHE LEU ARG VAL ARG SEQRES 22 A 304 ASP GLN ARG GLY ASN VAL LEU LEU SER PRO GLU GLU VAL SEQRES 23 A 304 SER GLU THR GLN GLY THR GLU ARG LEU THR ILE THR TYR SEQRES 24 A 304 SER SER SER MET MET SEQRES 1 C 127 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 127 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 127 PHE THR PHE LYS MET TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 C 127 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE ASN SEQRES 5 C 127 SER ALA GLY GLY SER THR SER TYR VAL ASP SER VAL LYS SEQRES 6 C 127 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 C 127 LEU TYR LEU GLN MET ASN SER LEU LYS PRO ASP ASP THR SEQRES 8 C 127 ALA VAL TYR TYR CYS VAL GLN GLY ARG ASN TRP PRO TYR SEQRES 9 C 127 ASP TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 10 C 127 HIS HIS HIS HIS HIS HIS GLU PRO GLU ALA SEQRES 1 B 304 HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE GLN SEQRES 2 B 304 GLY GLY GLY GLU VAL ARG ASN ASP ASP VAL ASP GLN SER SEQRES 3 B 304 LEU ILE ILE ALA ALA ARG ASN ILE VAL ARG ARG ALA THR SEQRES 4 B 304 VAL SER THR ASP PRO LEU ALA SER LEU LEU GLU MET CYS SEQRES 5 B 304 HIS SER THR GLN ILE GLY GLY ILE ARG MET VAL ASP ILE SEQRES 6 B 304 LEU ARG GLN ASN PRO THR GLU GLU GLN ALA VAL ASP ILE SEQRES 7 B 304 CYS LYS ALA ALA MET GLY LEU ARG ILE SER SER SER PHE SEQRES 8 B 304 SER PHE GLY GLY PHE THR PHE LYS ARG THR SER GLY SER SEQRES 9 B 304 SER VAL LYS LYS GLU GLU GLU VAL LEU THR GLY ASN LEU SEQRES 10 B 304 GLN THR LEU LYS ILE ARG VAL HIS GLU GLY TYR GLU GLU SEQRES 11 B 304 PHE THR MET VAL GLY ARG ARG ALA THR ALA ILE LEU ARG SEQRES 12 B 304 LYS ALA THR ARG ARG LEU ILE GLN LEU ILE VAL SER GLY SEQRES 13 B 304 ARG ASP GLU GLN SER ILE ALA GLU ALA ILE ILE VAL ALA SEQRES 14 B 304 MET VAL PHE SER GLN GLU ASP CYS MET ILE LYS ALA VAL SEQRES 15 B 304 ARG GLY ASP LEU ASN PHE VAL ASN ARG ALA ASN GLN ARG SEQRES 16 B 304 LEU ASN PRO MET HIS GLN LEU LEU ARG HIS PHE GLN LYS SEQRES 17 B 304 ASP ALA LYS VAL LEU PHE GLN ASN TRP GLY ILE GLU PRO SEQRES 18 B 304 ILE ASP ASN VAL MET GLY MET ILE GLY ILE LEU PRO ASP SEQRES 19 B 304 MET THR PRO SER THR GLU MET SER LEU ARG GLY VAL ARG SEQRES 20 B 304 VAL SER LYS MET GLY VAL ASP GLU TYR SER SER THR GLU SEQRES 21 B 304 ARG VAL VAL VAL SER ILE ASP ARG PHE LEU ARG VAL ARG SEQRES 22 B 304 ASP GLN ARG GLY ASN VAL LEU LEU SER PRO GLU GLU VAL SEQRES 23 B 304 SER GLU THR GLN GLY THR GLU ARG LEU THR ILE THR TYR SEQRES 24 B 304 SER SER SER MET MET SEQRES 1 D 127 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 127 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 127 PHE THR PHE LYS MET TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 D 127 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE ASN SEQRES 5 D 127 SER ALA GLY GLY SER THR SER TYR VAL ASP SER VAL LYS SEQRES 6 D 127 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 127 LEU TYR LEU GLN MET ASN SER LEU LYS PRO ASP ASP THR SEQRES 8 D 127 ALA VAL TYR TYR CYS VAL GLN GLY ARG ASN TRP PRO TYR SEQRES 9 D 127 ASP TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 10 D 127 HIS HIS HIS HIS HIS HIS GLU PRO GLU ALA HET GOL A 601 14 HET GOL B 701 14 HET GOL B 702 14 HET GOL B 703 14 HET PEG B 704 17 HET GOL D 301 14 HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 GOL 5(C3 H8 O3) FORMUL 9 PEG C4 H10 O3 FORMUL 11 HOH *453(H2 O) HELIX 1 AA1 ASN A 252 VAL A 272 1 21 HELIX 2 AA2 ASP A 275 THR A 287 1 13 HELIX 3 AA3 MET A 294 ASN A 301 1 8 HELIX 4 AA4 GLU A 305 MET A 315 1 11 HELIX 5 AA5 ASP A 390 GLN A 406 1 17 HELIX 6 AA6 GLU A 407 ALA A 413 1 7 HELIX 7 AA7 ASN A 429 ASP A 441 1 13 HELIX 8 AA8 ALA A 442 GLY A 450 1 9 HELIX 9 AA9 SER A 514 VAL A 518 5 5 HELIX 10 AB1 THR C 28 TYR C 32 5 5 HELIX 11 AB2 ASP C 62 LYS C 65 5 4 HELIX 12 AB3 LYS C 87 THR C 91 5 5 HELIX 13 AB4 ASN B 252 VAL B 272 1 21 HELIX 14 AB5 ASP B 275 SER B 286 1 12 HELIX 15 AB6 MET B 294 ASN B 301 1 8 HELIX 16 AB7 GLU B 305 MET B 315 1 11 HELIX 17 AB8 ASP B 390 GLN B 406 1 17 HELIX 18 AB9 GLU B 407 LYS B 412 1 6 HELIX 19 AC1 ASN B 429 ASP B 441 1 13 HELIX 20 AC2 ALA B 442 GLY B 450 1 9 HELIX 21 AC3 SER B 514 VAL B 518 5 5 HELIX 22 AC4 THR D 28 TYR D 32 5 5 HELIX 23 AC5 ASP D 62 LYS D 65 5 4 HELIX 24 AC6 LYS D 87 THR D 91 5 5 SHEET 1 AA1 3 ILE A 292 ARG A 293 0 SHEET 2 AA1 3 GLN A 288 ILE A 289 -1 N ILE A 289 O ILE A 292 SHEET 3 AA1 3 ILE A 529 THR A 530 -1 O THR A 530 N GLN A 288 SHEET 1 AA2 2 ILE A 319 SER A 320 0 SHEET 2 AA2 2 ARG A 493 VAL A 494 -1 O VAL A 494 N ILE A 319 SHEET 1 AA3 8 PHE A 323 PHE A 325 0 SHEET 2 AA3 8 PHE A 328 SER A 334 -1 O PHE A 330 N PHE A 323 SHEET 3 AA3 8 GLU A 361 VAL A 366 -1 O GLU A 362 N THR A 333 SHEET 4 AA3 8 ALA A 370 ALA A 377 -1 O ALA A 372 N MET A 365 SHEET 5 AA3 8 ARG A 380 GLY A 388 -1 O GLN A 383 N ARG A 375 SHEET 6 AA3 8 VAL A 478 SER A 481 1 O SER A 481 N VAL A 386 SHEET 7 AA3 8 MET A 460 ILE A 463 -1 N ILE A 461 O VAL A 480 SHEET 8 AA3 8 PRO A 469 SER A 470 -1 O SER A 470 N GLY A 462 SHEET 1 AA4 2 LYS A 339 LEU A 345 0 SHEET 2 AA4 2 THR A 351 HIS A 357 -1 O LEU A 352 N VAL A 344 SHEET 1 AA5 2 ILE A 451 PRO A 453 0 SHEET 2 AA5 2 MET A 473 LEU A 475 -1 O SER A 474 N GLU A 452 SHEET 1 AA6 3 SER A 497 ILE A 498 0 SHEET 2 AA6 3 VAL A 504 ARG A 505 -1 O ARG A 505 N SER A 497 SHEET 3 AA6 3 VAL A 511 LEU A 513 -1 O LEU A 512 N VAL A 504 SHEET 1 AA7 4 GLN C 3 SER C 7 0 SHEET 2 AA7 4 LEU C 18 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AA7 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA7 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AA8 6 GLY C 10 VAL C 12 0 SHEET 2 AA8 6 THR C 111 VAL C 115 1 O THR C 114 N GLY C 10 SHEET 3 AA8 6 ALA C 92 GLN C 98 -1 N TYR C 94 O THR C 111 SHEET 4 AA8 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AA8 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AA8 6 THR C 58 TYR C 60 -1 O SER C 59 N SER C 50 SHEET 1 AA9 3 ILE B 292 ARG B 293 0 SHEET 2 AA9 3 GLN B 288 ILE B 289 -1 N ILE B 289 O ILE B 292 SHEET 3 AA9 3 ILE B 529 THR B 530 -1 O THR B 530 N GLN B 288 SHEET 1 AB1 2 ILE B 319 SER B 320 0 SHEET 2 AB1 2 ARG B 493 VAL B 494 -1 O VAL B 494 N ILE B 319 SHEET 1 AB2 8 PHE B 323 PHE B 325 0 SHEET 2 AB2 8 PHE B 328 SER B 334 -1 O PHE B 330 N PHE B 323 SHEET 3 AB2 8 GLU B 361 VAL B 366 -1 O GLU B 362 N THR B 333 SHEET 4 AB2 8 ALA B 370 ALA B 377 -1 O ALA B 372 N MET B 365 SHEET 5 AB2 8 ARG B 380 GLY B 388 -1 O GLN B 383 N ARG B 375 SHEET 6 AB2 8 VAL B 478 SER B 481 1 O SER B 481 N VAL B 386 SHEET 7 AB2 8 MET B 460 ILE B 463 -1 N ILE B 461 O VAL B 480 SHEET 8 AB2 8 PRO B 469 SER B 470 -1 O SER B 470 N GLY B 462 SHEET 1 AB3 2 LYS B 340 LEU B 345 0 SHEET 2 AB3 2 THR B 351 VAL B 356 -1 O VAL B 356 N LYS B 340 SHEET 1 AB4 2 ILE B 451 PRO B 453 0 SHEET 2 AB4 2 MET B 473 LEU B 475 -1 O SER B 474 N GLU B 452 SHEET 1 AB5 3 VAL B 496 ILE B 498 0 SHEET 2 AB5 3 VAL B 504 ASP B 506 -1 O ARG B 505 N SER B 497 SHEET 3 AB5 3 VAL B 511 LEU B 513 -1 O LEU B 512 N VAL B 504 SHEET 1 AB6 4 GLN D 3 SER D 7 0 SHEET 2 AB6 4 LEU D 18 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 3 AB6 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AB6 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AB7 6 GLY D 10 VAL D 12 0 SHEET 2 AB7 6 THR D 111 VAL D 115 1 O THR D 114 N GLY D 10 SHEET 3 AB7 6 ALA D 92 GLN D 98 -1 N ALA D 92 O VAL D 113 SHEET 4 AB7 6 MET D 34 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AB7 6 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AB7 6 THR D 58 TYR D 60 -1 O SER D 59 N SER D 50 SSBOND 1 CYS C 22 CYS C 96 1555 1555 2.01 SSBOND 2 CYS D 22 CYS D 96 1555 1555 2.04 CISPEP 1 TRP C 102 PRO C 103 0 1.78 CISPEP 2 TRP D 102 PRO D 103 0 -5.55 CRYST1 42.583 106.543 98.405 90.00 98.01 90.00 P 1 21 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 0.023484 0.000000 0.003303 0.00000 SCALE2 0.000000 0.009386 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010262 0.00000