HEADER RNA BINDING PROTEIN/RNA 12-JUL-24 9CM4 TITLE HCV2 FAB BOUND TO SELECTED RNA LOOP COMPND MOL_ID: 1; COMPND 2 MOLECULE: HCV2 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HCV2 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HCV2 RNA LOOP; COMPND 11 CHAIN: G, J; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 16 ORGANISM_TAXID: 32630 KEYWDS FAB, RNA, EPITOPE, LOOP, RNA BINDING PROTEIN-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.T.DISARE,A.LEWICKA,J.A.PICCIRILLI REVDAT 1 14-JAN-26 9CM4 0 JRNL AUTH M.T.DISARE,A.LEWICKA,D.KROCHMAL,D.KOIRALA,J.A.PICCIRILLI JRNL TITL A SUITE OF PORTABLE RNA EPITOPES AS STRUCTURAL BIOLOGY TOOLS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.82 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 1.82 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.67 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 107470 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.161 REMARK 3 R VALUE (WORKING SET) : 0.160 REMARK 3 FREE R VALUE : 0.198 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.850 REMARK 3 FREE R VALUE TEST SET COUNT : 1986 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 54.6700 - 4.3900 0.98 7792 146 0.1457 0.1665 REMARK 3 2 4.3900 - 3.4800 0.99 7633 140 0.1261 0.1710 REMARK 3 3 3.4800 - 3.0400 0.99 7682 144 0.1420 0.1652 REMARK 3 4 3.0400 - 2.7600 0.98 7485 143 0.1624 0.1898 REMARK 3 5 2.7600 - 2.5700 0.99 7584 141 0.1678 0.2227 REMARK 3 6 2.5700 - 2.4100 0.99 7590 146 0.1667 0.2158 REMARK 3 7 2.4100 - 2.2900 0.99 7531 145 0.1690 0.2257 REMARK 3 8 2.2900 - 2.1900 0.99 7516 150 0.1751 0.2152 REMARK 3 9 2.1900 - 2.1100 0.99 7577 135 0.1788 0.2384 REMARK 3 10 2.1100 - 2.0400 0.96 7254 144 0.1787 0.2192 REMARK 3 11 2.0400 - 1.9700 0.98 7519 118 0.1757 0.2223 REMARK 3 12 1.9700 - 1.9200 0.98 7445 145 0.1918 0.2719 REMARK 3 13 1.9200 - 1.8700 0.98 7405 163 0.2389 0.2703 REMARK 3 14 1.8700 - 1.8200 0.98 7471 126 0.3033 0.3506 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) : 0.230 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.910 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.11 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 : 0.016 7770 REMARK 3 ANGLE : 1.395 10754 REMARK 3 CHIRALITY : 0.099 1234 REMARK 3 PLANARITY : 0.011 1216 REMARK 3 DIHEDRAL : 19.327 2898 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): -72.7936 21.7438 28.1846 REMARK 3 T TENSOR REMARK 3 T11: 0.2009 T22: 0.1634 REMARK 3 T33: 0.1996 T12: -0.0099 REMARK 3 T13: 0.0100 T23: 0.0234 REMARK 3 L TENSOR REMARK 3 L11: 0.1407 L22: 0.1266 REMARK 3 L33: 0.2503 L12: -0.0464 REMARK 3 L13: -0.0970 L23: 0.1071 REMARK 3 S TENSOR REMARK 3 S11: 0.0269 S12: 0.0028 S13: 0.0248 REMARK 3 S21: 0.0145 S22: -0.0004 S23: 0.0002 REMARK 3 S31: -0.0246 S32: -0.0007 S33: -0.0247 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 9CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000285863. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-OCT-22 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 : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107770 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820 REMARK 200 RESOLUTION RANGE LOW (A) : 54.670 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : 0.36510 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.3900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7 REMARK 200 DATA REDUNDANCY IN SHELL : 5.40 REMARK 200 R MERGE FOR SHELL (I) : 1.19900 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 (%): 55.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M BIS-TRIS REMARK 280 PH 5.5, 25% W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, REMARK 280 HANGING DROP, 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 107.61600 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.10500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.61600 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.10500 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5750 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22110 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, J 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5940 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22520 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G 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 GLU H 1 REMARK 465 ILE H 2 REMARK 465 SER H 227 REMARK 465 CYS H 228 REMARK 465 ASP H 229 REMARK 465 LYS H 230 REMARK 465 THR H 231 REMARK 465 HIS H 232 REMARK 465 THR H 233 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 GLU A 1 REMARK 465 ILE A 2 REMARK 465 SER A 227 REMARK 465 CYS A 228 REMARK 465 ASP A 229 REMARK 465 LYS A 230 REMARK 465 THR A 231 REMARK 465 HIS A 232 REMARK 465 THR A 233 REMARK 465 GLU B 214 REMARK 465 CYS B 215 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 HOH H 421 O HOH H 492 1.85 REMARK 500 O HOH A 347 O HOH A 506 1.88 REMARK 500 O HOH B 596 O HOH B 655 1.88 REMARK 500 O HOH B 689 O HOH B 722 1.89 REMARK 500 O HOH A 485 O HOH A 504 1.90 REMARK 500 O HOH J 141 O HOH J 149 1.94 REMARK 500 O HOH B 446 O HOH B 685 1.98 REMARK 500 O HOH L 585 O HOH L 635 1.99 REMARK 500 O HOH H 401 O HOH L 560 1.99 REMARK 500 O HOH G 147 O HOH G 157 2.04 REMARK 500 O HOH A 432 O HOH A 511 2.04 REMARK 500 O HOH L 501 O HOH L 624 2.04 REMARK 500 O HOH H 362 O HOH H 479 2.08 REMARK 500 O HOH B 740 O HOH G 160 2.08 REMARK 500 O HOH A 326 O HOH A 531 2.08 REMARK 500 O HOH A 422 O HOH A 502 2.09 REMARK 500 O HOH A 498 O HOH B 452 2.10 REMARK 500 O HOH G 150 O HOH G 158 2.10 REMARK 500 O HOH B 481 O HOH B 582 2.11 REMARK 500 O HOH B 617 O HOH B 652 2.11 REMARK 500 O HOH A 527 O HOH B 723 2.13 REMARK 500 O HOH B 568 O HOH B 642 2.13 REMARK 500 O HOH B 476 O HOH B 673 2.14 REMARK 500 O HOH J 142 O HOH J 154 2.14 REMARK 500 O HOH A 474 O HOH A 478 2.15 REMARK 500 O HOH J 119 O HOH J 151 2.15 REMARK 500 O HOH B 702 O HOH B 709 2.15 REMARK 500 O HOH G 163 O HOH G 168 2.15 REMARK 500 O HOH L 597 O HOH L 631 2.16 REMARK 500 O HOH B 638 O HOH B 665 2.16 REMARK 500 O HOH A 499 O HOH A 535 2.16 REMARK 500 O HOH L 414 O HOH L 571 2.17 REMARK 500 O HOH B 487 O HOH B 558 2.17 REMARK 500 O HOH H 480 O HOH H 514 2.18 REMARK 500 O HOH A 384 O HOH B 497 2.18 REMARK 500 O HOH L 552 O HOH L 665 2.18 REMARK 500 O HOH B 542 O HOH B 584 2.18 REMARK 500 O HOH A 407 O HOH A 485 2.19 REMARK 500 O HOH B 526 O HOH B 712 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 O4 SO4 B 302 O HOH A 496 4446 2.18 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 B 195 CB CYS B 195 SG -0.126 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 LEU H 190 CA - CB - CG ANGL. DEV. = 14.9 DEGREES REMARK 500 LEU A 190 CA - CB - CG ANGL. DEV. = 14.4 DEGREES REMARK 500 U G 6 O5' - P - OP1 ANGL. DEV. = -6.9 DEGREES REMARK 500 A G 10 O5' - P - OP2 ANGL. DEV. = -6.2 DEGREES REMARK 500 C J 3 O5' - P - OP2 ANGL. DEV. = -6.8 DEGREES REMARK 500 U J 6 C2 - N3 - C4 ANGL. DEV. = -5.4 DEGREES REMARK 500 U J 6 N3 - C4 - C5 ANGL. DEV. = 4.7 DEGREES REMARK 500 U J 6 C5 - C6 - N1 ANGL. DEV. = -3.7 DEGREES REMARK 500 U J 6 N3 - C4 - O4 ANGL. DEV. = -4.2 DEGREES REMARK 500 A J 10 N1 - C6 - N6 ANGL. DEV. = 4.4 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 ARG H 104 142.82 91.33 REMARK 500 ASP H 156 62.55 65.11 REMARK 500 ALA L 52 -40.70 73.08 REMARK 500 ALA L 85 -178.30 -171.01 REMARK 500 TYR L 95 -77.22 -129.77 REMARK 500 GLU A 4 -167.37 -115.65 REMARK 500 ARG A 104 143.80 85.48 REMARK 500 ASP A 156 62.44 67.47 REMARK 500 ALA B 52 -45.19 77.50 REMARK 500 ALA B 85 -177.90 -173.06 REMARK 500 TYR B 95 -79.48 -123.25 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 H 574 DISTANCE = 5.94 ANGSTROMS REMARK 525 HOH H 575 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH H 576 DISTANCE = 6.89 ANGSTROMS REMARK 525 HOH H 577 DISTANCE = 7.83 ANGSTROMS REMARK 525 HOH L 693 DISTANCE = 6.49 ANGSTROMS REMARK 525 HOH A 587 DISTANCE = 5.84 ANGSTROMS REMARK 525 HOH A 588 DISTANCE = 6.00 ANGSTROMS REMARK 525 HOH A 589 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH A 590 DISTANCE = 6.39 ANGSTROMS REMARK 525 HOH A 591 DISTANCE = 6.49 ANGSTROMS REMARK 525 HOH A 592 DISTANCE = 6.51 ANGSTROMS REMARK 525 HOH A 593 DISTANCE = 6.75 ANGSTROMS REMARK 525 HOH A 594 DISTANCE = 7.50 ANGSTROMS REMARK 525 HOH B 741 DISTANCE = 5.88 ANGSTROMS REMARK 525 HOH B 742 DISTANCE = 6.52 ANGSTROMS REMARK 525 HOH B 743 DISTANCE = 6.53 ANGSTROMS REMARK 525 HOH G 169 DISTANCE = 6.90 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG L 301 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH L 499 O REMARK 620 2 HOH L 660 O 89.5 REMARK 620 3 HOH L 675 O 93.2 154.4 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B 301 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH B 416 O REMARK 620 2 HOH B 687 O 90.4 REMARK 620 3 HOH B 713 O 119.0 144.1 REMARK 620 N 1 2 DBREF 9CM4 H 1 233 PDB 9CM4 9CM4 1 233 DBREF 9CM4 L 1 215 PDB 9CM4 9CM4 1 215 DBREF 9CM4 A 1 233 PDB 9CM4 9CM4 1 233 DBREF 9CM4 B 1 215 PDB 9CM4 9CM4 1 215 DBREF 9CM4 G 1 20 PDB 9CM4 9CM4 1 20 DBREF 9CM4 J 1 20 PDB 9CM4 9CM4 1 20 SEQRES 1 H 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 233 ALA SER GLY PHE TYR ILE SER SER TYR SER ILE HIS TRP SEQRES 4 H 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 233 SER ILE TYR PRO SER TYR GLY TYR THR SER TYR ALA ASP SEQRES 6 H 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG ARG TYR ARG SEQRES 9 H 233 SER TYR TYR SER ARG TYR GLY PHE ASP TYR TRP GLY GLN SEQRES 10 H 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 L 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 215 SER SER TYR TYR PRO SER THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 A 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 A 233 ALA SER GLY PHE TYR ILE SER SER TYR SER ILE HIS TRP SEQRES 4 A 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 A 233 SER ILE TYR PRO SER TYR GLY TYR THR SER TYR ALA ASP SEQRES 6 A 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 A 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 A 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG ARG TYR ARG SEQRES 9 A 233 SER TYR TYR SER ARG TYR GLY PHE ASP TYR TRP GLY GLN SEQRES 10 A 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 B 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 B 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 B 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 B 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 B 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 B 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 B 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 B 215 SER SER TYR TYR PRO SER THR PHE GLY GLN GLY THR LYS SEQRES 9 B 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 20 G G C G A U A G U A U C U SEQRES 2 G 20 C A A C G C C SEQRES 1 J 20 G G C G A U A G U A U C U SEQRES 2 J 20 C A A C G C C HET MG L 301 1 HET SO4 L 302 5 HET SO4 L 303 5 HET MG B 301 1 HET SO4 B 302 5 HET SO4 B 303 5 HET SO4 B 304 5 HETNAM MG MAGNESIUM ION HETNAM SO4 SULFATE ION FORMUL 7 MG 2(MG 2+) FORMUL 8 SO4 5(O4 S 2-) FORMUL 14 HOH *1333(H2 O) HELIX 1 AA1 TYR H 31 SER H 33 5 3 HELIX 2 AA2 ASP H 65 LYS H 68 5 4 HELIX 3 AA3 THR H 77 LYS H 79 5 3 HELIX 4 AA4 ARG H 90 THR H 94 5 5 HELIX 5 AA5 SER H 168 ALA H 170 5 3 HELIX 6 AA6 SER H 199 GLY H 202 5 4 HELIX 7 AA7 LYS H 213 ASN H 216 5 4 HELIX 8 AA8 GLN L 80 PHE L 84 5 5 HELIX 9 AA9 SER L 122 LYS L 127 1 6 HELIX 10 AB1 LYS L 184 HIS L 190 1 7 HELIX 11 AB2 TYR A 31 SER A 33 5 3 HELIX 12 AB3 THR A 77 LYS A 79 5 3 HELIX 13 AB4 ARG A 90 THR A 94 5 5 HELIX 14 AB5 SER A 168 ALA A 170 5 3 HELIX 15 AB6 SER A 199 LEU A 201 5 3 HELIX 16 AB7 LYS A 213 ASN A 216 5 4 HELIX 17 AB8 GLN B 80 PHE B 84 5 5 HELIX 18 AB9 SER B 122 LYS B 127 1 6 HELIX 19 AC1 LYS B 184 HIS B 190 1 7 SHEET 1 AA1 4 GLN H 6 SER H 10 0 SHEET 2 AA1 4 LEU H 21 SER H 28 -1 O ALA H 26 N VAL H 8 SHEET 3 AA1 4 THR H 81 MET H 86 -1 O MET H 86 N LEU H 21 SHEET 4 AA1 4 PHE H 71 ASP H 76 -1 N THR H 72 O GLN H 85 SHEET 1 AA2 6 GLY H 13 VAL H 15 0 SHEET 2 AA2 6 THR H 119 VAL H 123 1 O THR H 122 N GLY H 13 SHEET 3 AA2 6 ALA H 95 TYR H 103 -1 N TYR H 97 O THR H 119 SHEET 4 AA2 6 TYR H 35 GLN H 42 -1 N VAL H 40 O TYR H 98 SHEET 5 AA2 6 LEU H 48 ILE H 54 -1 O GLU H 49 N ARG H 41 SHEET 6 AA2 6 THR H 61 TYR H 63 -1 O SER H 62 N SER H 53 SHEET 1 AA3 4 GLY H 13 VAL H 15 0 SHEET 2 AA3 4 THR H 119 VAL H 123 1 O THR H 122 N GLY H 13 SHEET 3 AA3 4 ALA H 95 TYR H 103 -1 N TYR H 97 O THR H 119 SHEET 4 AA3 4 PHE H 112 TRP H 115 -1 O TYR H 114 N ARG H 101 SHEET 1 AA4 4 SER H 132 LEU H 136 0 SHEET 2 AA4 4 THR H 147 TYR H 157 -1 O LEU H 153 N PHE H 134 SHEET 3 AA4 4 TYR H 188 PRO H 197 -1 O LEU H 190 N VAL H 154 SHEET 4 AA4 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193 SHEET 1 AA5 4 SER H 132 LEU H 136 0 SHEET 2 AA5 4 THR H 147 TYR H 157 -1 O LEU H 153 N PHE H 134 SHEET 3 AA5 4 TYR H 188 PRO H 197 -1 O LEU H 190 N VAL H 154 SHEET 4 AA5 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189 SHEET 1 AA6 3 THR H 163 TRP H 166 0 SHEET 2 AA6 3 ILE H 207 HIS H 212 -1 O ASN H 209 N SER H 165 SHEET 3 AA6 3 THR H 217 LYS H 222 -1 O VAL H 219 N VAL H 210 SHEET 1 AA7 4 MET L 5 SER L 8 0 SHEET 2 AA7 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA7 4 PHE L 63 SER L 68 -1 N SER L 66 O THR L 73 SHEET 1 AA8 6 SER L 11 ALA L 14 0 SHEET 2 AA8 6 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 12 SHEET 3 AA8 6 THR L 86 SER L 92 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 6 VAL L 34 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AA8 6 LYS L 46 TYR L 50 -1 O LEU L 48 N TRP L 36 SHEET 6 AA8 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AA9 4 SER L 11 ALA L 14 0 SHEET 2 AA9 4 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 12 SHEET 3 AA9 4 THR L 86 SER L 92 -1 N TYR L 87 O THR L 103 SHEET 4 AA9 4 SER L 97 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AB1 4 TYR L 174 SER L 183 -1 O LEU L 176 N LEU L 137 SHEET 4 AB1 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AB2 4 ALA L 154 LEU L 155 0 SHEET 2 AB2 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB2 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AB2 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AB3 4 GLN A 6 SER A 10 0 SHEET 2 AB3 4 LEU A 21 SER A 28 -1 O ALA A 26 N VAL A 8 SHEET 3 AB3 4 THR A 81 MET A 86 -1 O MET A 86 N LEU A 21 SHEET 4 AB3 4 PHE A 71 ASP A 76 -1 N THR A 72 O GLN A 85 SHEET 1 AB4 6 GLY A 13 VAL A 15 0 SHEET 2 AB4 6 THR A 119 VAL A 123 1 O THR A 122 N VAL A 15 SHEET 3 AB4 6 ALA A 95 TYR A 103 -1 N TYR A 97 O THR A 119 SHEET 4 AB4 6 TYR A 35 GLN A 42 -1 N VAL A 40 O TYR A 98 SHEET 5 AB4 6 LEU A 48 ILE A 54 -1 O VAL A 51 N TRP A 39 SHEET 6 AB4 6 THR A 61 TYR A 63 -1 O SER A 62 N SER A 53 SHEET 1 AB5 4 GLY A 13 VAL A 15 0 SHEET 2 AB5 4 THR A 119 VAL A 123 1 O THR A 122 N VAL A 15 SHEET 3 AB5 4 ALA A 95 TYR A 103 -1 N TYR A 97 O THR A 119 SHEET 4 AB5 4 TYR A 114 TRP A 115 -1 O TYR A 114 N ARG A 101 SHEET 1 AB6 4 SER A 132 LEU A 136 0 SHEET 2 AB6 4 THR A 147 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AB6 4 TYR A 188 PRO A 197 -1 O LEU A 190 N VAL A 154 SHEET 4 AB6 4 VAL A 175 THR A 177 -1 N HIS A 176 O VAL A 193 SHEET 1 AB7 4 SER A 132 LEU A 136 0 SHEET 2 AB7 4 THR A 147 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AB7 4 TYR A 188 PRO A 197 -1 O LEU A 190 N VAL A 154 SHEET 4 AB7 4 VAL A 181 LEU A 182 -1 N VAL A 181 O SER A 189 SHEET 1 AB8 3 THR A 163 TRP A 166 0 SHEET 2 AB8 3 ILE A 207 HIS A 212 -1 O ASN A 209 N SER A 165 SHEET 3 AB8 3 THR A 217 LYS A 222 -1 O VAL A 219 N VAL A 210 SHEET 1 AB9 4 MET B 5 SER B 8 0 SHEET 2 AB9 4 VAL B 20 ALA B 26 -1 O ARG B 25 N THR B 6 SHEET 3 AB9 4 ASP B 71 ILE B 76 -1 O PHE B 72 N CYS B 24 SHEET 4 AB9 4 PHE B 63 SER B 68 -1 N SER B 64 O THR B 75 SHEET 1 AC1 6 SER B 11 ALA B 14 0 SHEET 2 AC1 6 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 12 SHEET 3 AC1 6 THR B 86 SER B 92 -1 N TYR B 87 O THR B 103 SHEET 4 AC1 6 VAL B 34 GLN B 39 -1 N GLN B 39 O THR B 86 SHEET 5 AC1 6 LYS B 46 TYR B 50 -1 O LEU B 48 N TRP B 36 SHEET 6 AC1 6 SER B 54 LEU B 55 -1 O SER B 54 N TYR B 50 SHEET 1 AC2 4 SER B 11 ALA B 14 0 SHEET 2 AC2 4 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 12 SHEET 3 AC2 4 THR B 86 SER B 92 -1 N TYR B 87 O THR B 103 SHEET 4 AC2 4 SER B 97 PHE B 99 -1 O THR B 98 N GLN B 91 SHEET 1 AC3 4 SER B 115 PHE B 119 0 SHEET 2 AC3 4 THR B 130 PHE B 140 -1 O LEU B 136 N PHE B 117 SHEET 3 AC3 4 TYR B 174 SER B 183 -1 O LEU B 180 N VAL B 133 SHEET 4 AC3 4 SER B 160 VAL B 164 -1 N GLN B 161 O THR B 179 SHEET 1 AC4 4 ALA B 154 LEU B 155 0 SHEET 2 AC4 4 LYS B 146 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AC4 4 VAL B 192 THR B 198 -1 O GLU B 196 N GLN B 148 SHEET 4 AC4 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SSBOND 1 CYS H 25 CYS H 99 1555 1555 2.15 SSBOND 2 CYS H 152 CYS H 208 1555 1555 2.05 SSBOND 3 CYS L 24 CYS L 89 1555 1555 2.06 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.09 SSBOND 5 CYS A 25 CYS A 99 1555 1555 2.15 SSBOND 6 CYS A 152 CYS A 208 1555 1555 2.08 SSBOND 7 CYS B 24 CYS B 89 1555 1555 2.10 SSBOND 8 CYS B 135 CYS B 195 1555 1555 2.08 LINK MG MG L 301 O HOH L 499 1555 1555 2.05 LINK MG MG L 301 O HOH L 660 1555 1555 1.88 LINK MG MG L 301 O HOH L 675 1555 1555 2.46 LINK MG MG B 301 O HOH B 416 1555 1555 2.48 LINK MG MG B 301 O HOH B 687 1555 1555 2.28 LINK MG MG B 301 O HOH B 713 1555 1555 2.37 CISPEP 1 PHE H 158 PRO H 159 0 -3.57 CISPEP 2 GLU H 160 PRO H 161 0 -0.32 CISPEP 3 SER L 8 PRO L 9 0 -5.29 CISPEP 4 TYR L 141 PRO L 142 0 7.90 CISPEP 5 PHE A 158 PRO A 159 0 -3.70 CISPEP 6 GLU A 160 PRO A 161 0 -1.44 CISPEP 7 SER B 8 PRO B 9 0 1.49 CISPEP 8 TYR B 141 PRO B 142 0 6.65 CRYST1 215.232 52.210 133.338 90.00 124.92 90.00 C 1 2 1 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 0.004646 0.000000 0.003244 0.00000 SCALE2 0.000000 0.019153 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009147 0.00000