HEADER PROTEIN BINDING 26-MAR-24 9ETJ TITLE MOUSE CNPASE CATALYTIC DOMAIN WITH NANOBODY 10E COMPND MOL_ID: 1; COMPND 2 MOLECULE: 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; COMPND 3 CHAIN: A, B, E, G; COMPND 4 SYNONYM: CNP,CNPASE; COMPND 5 EC: 3.1.4.37; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: MOUSE CNPASE CATALYTIC DOMAIN; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: CHAINS: C,D,F,H; COMPND 10 CHAIN: C, D, F, H; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: ANTI-CNPASE NANOBODY 10E SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: CNP, CNP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_TAXID: 30538; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CNPASE, MYELIN, NANOBODY, SINGLE-DOMAIN ANTIBODY, COMPLEX, PROTEIN KEYWDS 2 BINDING EXPDTA X-RAY DIFFRACTION AUTHOR S.MARKUSSON,A.RAASAKKA,F.OPAZO,P.KURSULA REVDAT 1 11-DEC-24 9ETJ 0 JRNL AUTH S.MARKUSSON,A.RAASAKKA,F.OPAZO,P.KURSULA JRNL TITL MOUSE CNPASE CATALYTIC DOMAIN WITH NANOBODY 10E JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 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) : 2.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.95 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 48602 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.254 REMARK 3 R VALUE (WORKING SET) : 0.252 REMARK 3 FREE R VALUE : 0.304 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.120 REMARK 3 FREE R VALUE TEST SET COUNT : 2002 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 47.9500 - 6.1400 0.99 3530 158 0.2010 0.2533 REMARK 3 2 6.1400 - 4.8800 1.00 3403 146 0.2203 0.2749 REMARK 3 3 4.8800 - 4.2600 1.00 3375 142 0.1918 0.2361 REMARK 3 4 4.2600 - 3.8700 1.00 3341 147 0.2364 0.2685 REMARK 3 5 3.8700 - 3.5900 0.99 3322 140 0.2750 0.3297 REMARK 3 6 3.5900 - 3.3800 1.00 3316 141 0.2773 0.3782 REMARK 3 7 3.3800 - 3.2100 1.00 3329 143 0.3201 0.3503 REMARK 3 8 3.2100 - 3.0700 1.00 3309 141 0.3201 0.3555 REMARK 3 9 3.0700 - 2.9500 1.00 3291 139 0.3184 0.3668 REMARK 3 10 2.9500 - 2.8500 1.00 3304 139 0.3625 0.3793 REMARK 3 11 2.8500 - 2.7600 1.00 3291 144 0.4105 0.5172 REMARK 3 12 2.7600 - 2.6800 1.00 3272 144 0.4268 0.5306 REMARK 3 13 2.6800 - 2.6100 0.99 3267 139 0.4262 0.4935 REMARK 3 14 2.6100 - 2.5500 0.99 3250 139 0.4299 0.4653 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.562 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.225 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 78.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 102.0 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 : 0.020 10744 REMARK 3 ANGLE : 1.612 14530 REMARK 3 CHIRALITY : 0.075 1529 REMARK 3 PLANARITY : 0.013 1872 REMARK 3 DIHEDRAL : 14.758 3899 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 161 THROUGH 378) REMARK 3 ORIGIN FOR THE GROUP (A): -20.0795 -6.4538 22.1940 REMARK 3 T TENSOR REMARK 3 T11: 0.7623 T22: 0.6390 REMARK 3 T33: 0.6368 T12: 0.1434 REMARK 3 T13: -0.0241 T23: -0.0700 REMARK 3 L TENSOR REMARK 3 L11: 4.5721 L22: 2.6191 REMARK 3 L33: 3.4161 L12: 0.4101 REMARK 3 L13: 1.7337 L23: 1.0000 REMARK 3 S TENSOR REMARK 3 S11: -0.1562 S12: -0.7049 S13: 0.8129 REMARK 3 S21: 0.2184 S22: -0.0109 S23: 0.2511 REMARK 3 S31: -0.6481 S32: -0.4155 S33: 0.1812 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 2 THROUGH 128) REMARK 3 ORIGIN FOR THE GROUP (A): -7.4593 -32.0493 25.8460 REMARK 3 T TENSOR REMARK 3 T11: 0.5703 T22: 0.5470 REMARK 3 T33: 0.6410 T12: 0.1381 REMARK 3 T13: 0.0624 T23: 0.0039 REMARK 3 L TENSOR REMARK 3 L11: 4.7811 L22: 4.0127 REMARK 3 L33: 9.4876 L12: -0.8104 REMARK 3 L13: 2.6284 L23: -3.9307 REMARK 3 S TENSOR REMARK 3 S11: 0.1174 S12: -0.0593 S13: -0.4574 REMARK 3 S21: -0.0526 S22: -0.0327 S23: -0.1511 REMARK 3 S31: 1.2143 S32: 0.6484 S33: -0.1248 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 162 THROUGH 378) REMARK 3 ORIGIN FOR THE GROUP (A): 37.3189 -7.9976 39.0043 REMARK 3 T TENSOR REMARK 3 T11: 1.3700 T22: 0.7638 REMARK 3 T33: 0.6423 T12: -0.2250 REMARK 3 T13: 0.0808 T23: 0.0445 REMARK 3 L TENSOR REMARK 3 L11: 3.1813 L22: 3.1756 REMARK 3 L33: 5.5024 L12: 0.3691 REMARK 3 L13: -0.3526 L23: 0.4820 REMARK 3 S TENSOR REMARK 3 S11: 0.0431 S12: 0.6216 S13: 0.5947 REMARK 3 S21: -0.7900 S22: 0.0430 S23: -0.1889 REMARK 3 S31: -2.0329 S32: 0.3794 S33: -0.0526 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 2 THROUGH 128) REMARK 3 ORIGIN FOR THE GROUP (A): 26.5374 -34.5386 35.0238 REMARK 3 T TENSOR REMARK 3 T11: 0.4681 T22: 0.4525 REMARK 3 T33: 0.6516 T12: -0.0780 REMARK 3 T13: 0.1304 T23: -0.0745 REMARK 3 L TENSOR REMARK 3 L11: 7.6786 L22: 3.2012 REMARK 3 L33: 9.1920 L12: 2.1079 REMARK 3 L13: 3.6625 L23: 1.9381 REMARK 3 S TENSOR REMARK 3 S11: 0.0929 S12: 0.3471 S13: -0.2760 REMARK 3 S21: -0.0480 S22: -0.0421 S23: 0.0978 REMARK 3 S31: 0.7541 S32: -0.5075 S33: -0.0920 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'E' AND RESID 161 THROUGH 378) REMARK 3 ORIGIN FOR THE GROUP (A): 20.5394 -25.4420 0.1570 REMARK 3 T TENSOR REMARK 3 T11: 0.6829 T22: 0.8330 REMARK 3 T33: 0.6865 T12: 0.1954 REMARK 3 T13: 0.0730 T23: 0.0782 REMARK 3 L TENSOR REMARK 3 L11: 2.3281 L22: 3.1064 REMARK 3 L33: 6.6778 L12: -0.1809 REMARK 3 L13: 0.0487 L23: 1.6955 REMARK 3 S TENSOR REMARK 3 S11: 0.0668 S12: -0.0245 S13: 0.2203 REMARK 3 S21: 0.0446 S22: -0.1652 S23: 0.6406 REMARK 3 S31: -0.7462 S32: -1.0607 S33: 0.1467 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'F' AND RESID 2 THROUGH 128) REMARK 3 ORIGIN FOR THE GROUP (A): 40.6488 -43.3632 9.9835 REMARK 3 T TENSOR REMARK 3 T11: 0.7012 T22: 0.5704 REMARK 3 T33: 0.6510 T12: 0.1347 REMARK 3 T13: -0.0269 T23: -0.0371 REMARK 3 L TENSOR REMARK 3 L11: 3.8955 L22: 4.9986 REMARK 3 L33: 9.0524 L12: -0.2225 REMARK 3 L13: -0.9022 L23: -2.8027 REMARK 3 S TENSOR REMARK 3 S11: -0.1218 S12: -0.2024 S13: -0.2193 REMARK 3 S21: 0.3891 S22: -0.0922 S23: -0.5262 REMARK 3 S31: 1.0345 S32: 1.2715 S33: 0.2919 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN 'G' AND RESID 161 THROUGH 378) REMARK 3 ORIGIN FOR THE GROUP (A): -0.9110 -23.9689 62.0017 REMARK 3 T TENSOR REMARK 3 T11: 0.6427 T22: 0.9076 REMARK 3 T33: 0.7697 T12: -0.2017 REMARK 3 T13: 0.0611 T23: -0.0923 REMARK 3 L TENSOR REMARK 3 L11: 3.1108 L22: 1.3630 REMARK 3 L33: 6.5035 L12: 0.3449 REMARK 3 L13: -0.5643 L23: 0.1807 REMARK 3 S TENSOR REMARK 3 S11: 0.0710 S12: 0.1205 S13: 0.5272 REMARK 3 S21: -0.4436 S22: 0.2230 S23: -0.5508 REMARK 3 S31: -0.9131 S32: 1.5195 S33: -0.2582 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 128) REMARK 3 ORIGIN FOR THE GROUP (A): -21.7023 -40.5316 51.2487 REMARK 3 T TENSOR REMARK 3 T11: 0.5704 T22: 0.5413 REMARK 3 T33: 0.6904 T12: -0.0098 REMARK 3 T13: -0.1198 T23: 0.0106 REMARK 3 L TENSOR REMARK 3 L11: 4.7954 L22: 5.4150 REMARK 3 L33: 5.9860 L12: -0.3325 REMARK 3 L13: -0.0171 L23: 1.5759 REMARK 3 S TENSOR REMARK 3 S11: 0.3567 S12: 0.4248 S13: -0.1222 REMARK 3 S21: -0.8173 S22: -0.1646 S23: 0.4642 REMARK 3 S31: -0.0716 S32: -0.8433 S33: -0.1434 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and resid 162 through 378) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid 162 through 207 or REMARK 3 resid 216 through 290 or resid 297 REMARK 3 through 378)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 162 through 207 or REMARK 3 resid 216 through 291 or resid 298 REMARK 3 through 378)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "G" and (resid 162 through 207 or REMARK 3 resid 216 through 291 or resid 298 REMARK 3 through 378)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "C" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "D" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "F" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and resid 2 through 128) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9ETJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1292137548. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-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 : PETRA III, DESY REMARK 200 BEAMLINE : P11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48792 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 7.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62 REMARK 200 COMPLETENESS FOR SHELL (%) : 1.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.500 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 (%): 48.43 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA MALONATE, 20% PEG3350, PH REMARK 280 7.5, VAPOR DIFFUSION, SITTING 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 50.86500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.22500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.12500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.22500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.86500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.12500 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, 3, 4 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 GLY A 159 REMARK 465 LEU A 160 REMARK 465 GLY A 208 REMARK 465 ASP A 209 REMARK 465 GLU A 210 REMARK 465 PRO A 211 REMARK 465 LYS A 212 REMARK 465 GLU A 213 REMARK 465 LYS A 214 REMARK 465 LEU A 215 REMARK 465 SER A 291 REMARK 465 ASP A 292 REMARK 465 LEU A 293 REMARK 465 ASP A 294 REMARK 465 LYS A 295 REMARK 465 PRO A 296 REMARK 465 GLU C 1 REMARK 465 GLY B 159 REMARK 465 LEU B 160 REMARK 465 GLU B 161 REMARK 465 GLY B 208 REMARK 465 ASP B 209 REMARK 465 GLU B 210 REMARK 465 PRO B 211 REMARK 465 LYS B 212 REMARK 465 GLU B 213 REMARK 465 LYS B 214 REMARK 465 SER B 291 REMARK 465 ASP B 292 REMARK 465 LEU B 293 REMARK 465 ASP B 294 REMARK 465 LYS B 295 REMARK 465 GLU D 1 REMARK 465 GLY E 159 REMARK 465 LEU E 160 REMARK 465 GLY E 208 REMARK 465 ASP E 209 REMARK 465 GLU E 210 REMARK 465 PRO E 211 REMARK 465 LYS E 212 REMARK 465 GLU E 213 REMARK 465 LYS E 214 REMARK 465 GLU F 1 REMARK 465 GLY G 159 REMARK 465 LEU G 160 REMARK 465 GLY G 208 REMARK 465 ASP G 209 REMARK 465 GLU G 210 REMARK 465 PRO G 211 REMARK 465 LYS G 212 REMARK 465 GLU G 213 REMARK 465 LYS G 214 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 HH21 ARG H 67 OD2 ASP H 87 1.37 REMARK 500 OD2 ASP C 96 HH12 ARG C 102 1.39 REMARK 500 O GLY B 355 H GLY B 357 1.49 REMARK 500 O GLU B 300 HE22 GLN B 332 1.53 REMARK 500 HH TYR G 220 O PRO G 272 1.53 REMARK 500 HH TYR B 238 OD1 ASP D 98 1.54 REMARK 500 O GLU D 6 HG SER D 7 1.55 REMARK 500 HH12 ARG D 102 OG SER D 107 1.56 REMARK 500 HG1 THR E 274 OD2 ASP E 326 1.59 REMARK 500 O GLY A 355 H GLY A 357 1.59 REMARK 500 HH TYR E 238 OD1 ASP F 98 1.60 REMARK 500 OD2 ASP C 96 NH1 ARG C 102 2.11 REMARK 500 O GLU B 300 NE2 GLN B 332 2.16 REMARK 500 O GLY B 355 N GLY B 357 2.17 REMARK 500 O GLY A 355 N GLY A 357 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 GLU A 161 CD GLU A 161 OE2 0.076 REMARK 500 TYR A 247 CE1 TYR A 247 CZ 0.080 REMARK 500 CYS C 22 CB CYS C 22 SG -0.098 REMARK 500 CYS C 50 CB CYS C 50 SG -0.099 REMARK 500 SER C 52 CB SER C 52 OG -0.103 REMARK 500 TYR C 59 CD1 TYR C 59 CE1 -0.098 REMARK 500 GLU D 46 CD GLU D 46 OE2 0.068 REMARK 500 CYS D 50 CB CYS D 50 SG -0.103 REMARK 500 CYS D 93 CB CYS D 93 SG -0.108 REMARK 500 GLU E 179 CB GLU E 179 CG -0.142 REMARK 500 GLU E 179 CD GLU E 179 OE2 0.084 REMARK 500 CYS F 50 CB CYS F 50 SG -0.098 REMARK 500 TRP F 109 CE3 TRP F 109 CZ3 0.123 REMARK 500 CYS H 50 CB CYS H 50 SG -0.114 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 ARG C 102 CG - CD - NE ANGL. DEV. = -13.2 DEGREES REMARK 500 ASP C 116 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 ARG E 182 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 LEU F 99 CB - CG - CD2 ANGL. DEV. = 12.7 DEGREES REMARK 500 ASP F 116 CB - CG - OD1 ANGL. DEV. = 6.6 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 HIS A 204 32.66 -89.14 REMARK 500 THR A 233 -67.23 -105.28 REMARK 500 ASP A 237 53.78 37.58 REMARK 500 SER A 338 28.58 -76.77 REMARK 500 GLU A 341 172.82 -56.09 REMARK 500 LYS A 356 66.37 -56.28 REMARK 500 SER C 7 163.02 179.00 REMARK 500 TYR C 55 -24.03 56.41 REMARK 500 HIS C 57 73.05 -116.77 REMARK 500 ASN C 77 59.71 34.15 REMARK 500 SER C 127 173.21 -51.10 REMARK 500 GLU B 201 71.63 -100.39 REMARK 500 HIS B 204 39.32 -91.27 REMARK 500 PHE B 205 -33.87 -133.23 REMARK 500 PHE B 221 54.99 -92.33 REMARK 500 THR B 233 -66.45 -108.00 REMARK 500 ASP B 237 51.17 38.34 REMARK 500 SER B 338 32.65 -74.62 REMARK 500 GLU B 341 170.94 -59.87 REMARK 500 LYS B 356 60.03 -62.67 REMARK 500 SER D 7 162.17 176.67 REMARK 500 TYR D 55 -21.96 69.18 REMARK 500 HIS D 57 73.07 -116.14 REMARK 500 LYS D 65 -96.60 -21.39 REMARK 500 ASN D 77 64.27 36.19 REMARK 500 SER D 127 171.87 -55.83 REMARK 500 GLU E 201 65.22 -101.35 REMARK 500 HIS E 204 30.39 -85.55 REMARK 500 PHE E 205 -32.40 -142.40 REMARK 500 PHE E 221 55.53 -95.14 REMARK 500 THR E 233 -70.15 -111.18 REMARK 500 SER E 291 -62.82 -134.77 REMARK 500 ASP E 292 -88.54 41.87 REMARK 500 ASP E 294 -77.61 -45.14 REMARK 500 PRO E 296 -179.83 -47.50 REMARK 500 SER E 338 27.44 -75.31 REMARK 500 LYS E 356 58.71 -65.68 REMARK 500 LYS F 43 -174.41 -68.12 REMARK 500 TYR F 55 -133.20 -75.86 REMARK 500 GLU F 56 39.38 -66.31 REMARK 500 ALA F 64 43.64 -98.20 REMARK 500 ASN F 77 63.56 35.76 REMARK 500 LYS G 162 -54.43 -135.18 REMARK 500 GLU G 201 69.68 -105.04 REMARK 500 HIS G 204 37.74 -92.03 REMARK 500 PHE G 205 -30.13 -135.86 REMARK 500 THR G 233 -73.63 -105.43 REMARK 500 LYS G 356 75.69 -47.41 REMARK 500 VAL H 2 96.50 162.68 REMARK 500 SER H 7 163.65 175.38 REMARK 500 REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL 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 CA F 201 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PRO A 226 O REMARK 620 2 ASN F 97 O 135.1 REMARK 620 3 ASN F 97 OD1 136.3 1.5 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 201 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 237 OD1 REMARK 620 2 ASP C 96 OD1 150.0 REMARK 620 3 ASP C 98 OD2 97.3 85.7 REMARK 620 4 PRO C 114 O 92.1 79.8 164.1 REMARK 620 5 ASP C 116 OD1 137.5 68.7 105.0 75.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 202 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 31 O REMARK 620 2 ASN C 97 O 102.2 REMARK 620 3 ASN C 97 OD1 71.3 65.2 REMARK 620 4 PRO E 226 O 53.3 143.3 118.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA H 201 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PRO B 226 O REMARK 620 2 ASP H 31 O 136.3 REMARK 620 3 ASN H 97 O 136.4 1.5 REMARK 620 4 ASN H 97 OD1 137.7 2.7 1.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 201 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 237 OD1 REMARK 620 2 ASP D 98 OD2 111.8 REMARK 620 3 PRO D 114 O 104.6 132.2 REMARK 620 4 ASP D 116 OD1 156.2 88.3 67.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 202 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN D 97 O REMARK 620 2 ASP D 101 OD2 98.8 REMARK 620 3 PRO G 226 O 123.7 114.2 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA H 202 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 96 OD1 REMARK 620 2 ASP H 98 OD2 85.1 REMARK 620 3 PRO H 114 O 83.4 157.1 REMARK 620 4 ASP H 116 OD1 82.4 122.9 75.0 REMARK 620 N 1 2 3 DBREF 9ETJ A 159 378 UNP P16330 CN37_MOUSE 179 398 DBREF 9ETJ C 1 128 PDB 9ETJ 9ETJ 1 128 DBREF 9ETJ B 159 378 UNP P16330 CN37_MOUSE 179 398 DBREF 9ETJ D 1 128 PDB 9ETJ 9ETJ 1 128 DBREF 9ETJ E 159 378 UNP P16330 CN37_MOUSE 179 398 DBREF 9ETJ F 1 128 PDB 9ETJ 9ETJ 1 128 DBREF 9ETJ G 159 378 UNP P16330 CN37_MOUSE 179 398 DBREF 9ETJ H 1 128 PDB 9ETJ 9ETJ 1 128 SEQRES 1 A 220 GLY LEU GLU LYS ASP PHE LEU PRO LEU TYR PHE GLY TRP SEQRES 2 A 220 PHE LEU THR LYS LYS SER SER GLU THR LEU ARG LYS ALA SEQRES 3 A 220 GLY GLN VAL PHE LEU GLU GLU LEU GLY ASN HIS LYS ALA SEQRES 4 A 220 PHE LYS LYS GLU LEU ARG HIS PHE ILE SER GLY ASP GLU SEQRES 5 A 220 PRO LYS GLU LYS LEU GLU LEU VAL SER TYR PHE GLY LYS SEQRES 6 A 220 ARG PRO PRO GLY VAL LEU HIS CYS THR THR LYS PHE CYS SEQRES 7 A 220 ASP TYR GLY LYS ALA ALA GLY ALA GLU GLU TYR ALA GLN SEQRES 8 A 220 GLN GLU VAL VAL LYS ARG SER TYR GLY LYS ALA PHE LYS SEQRES 9 A 220 LEU SER ILE SER ALA LEU PHE VAL THR PRO LYS THR ALA SEQRES 10 A 220 GLY ALA GLN VAL VAL LEU THR ASP GLN GLU LEU GLN LEU SEQRES 11 A 220 TRP PRO SER ASP LEU ASP LYS PRO SER ALA SER GLU GLY SEQRES 12 A 220 LEU PRO PRO GLY SER ARG ALA HIS VAL THR LEU GLY CYS SEQRES 13 A 220 ALA ALA ASP VAL GLN PRO VAL GLN THR GLY LEU ASP LEU SEQRES 14 A 220 LEU ASP ILE LEU GLN GLN VAL LYS GLY GLY SER GLN GLY SEQRES 15 A 220 GLU ALA VAL GLY GLU LEU PRO ARG GLY LYS LEU TYR SER SEQRES 16 A 220 LEU GLY LYS GLY ARG TRP MET LEU SER LEU THR LYS LYS SEQRES 17 A 220 MET GLU VAL LYS ALA ILE PHE THR GLY TYR TYR GLY SEQRES 1 C 131 GLU VAL GLN LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 131 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 C 131 ILE THR LEU ASP ASP PHE GLY ILE GLY TRP PHE ARG GLN SEQRES 4 C 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA CYS ILE SER SEQRES 5 C 131 PRO GLY TYR GLU HIS ILE TYR TYR ALA ASP SER ALA LYS SEQRES 6 C 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 C 131 VAL TYR LEU GLN MET ASN ASN LEU LYS PRO TRP ASP THR SEQRES 8 C 131 GLY VAL TYR TYR CYS ALA ALA ASP ASN ASP LEU PRO ASP SEQRES 9 C 131 ARG LEU TRP GLY GLY SER ASP TRP SER ASP PRO SER PRO SEQRES 10 C 131 TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 11 C 131 SER SEQRES 1 B 220 GLY LEU GLU LYS ASP PHE LEU PRO LEU TYR PHE GLY TRP SEQRES 2 B 220 PHE LEU THR LYS LYS SER SER GLU THR LEU ARG LYS ALA SEQRES 3 B 220 GLY GLN VAL PHE LEU GLU GLU LEU GLY ASN HIS LYS ALA SEQRES 4 B 220 PHE LYS LYS GLU LEU ARG HIS PHE ILE SER GLY ASP GLU SEQRES 5 B 220 PRO LYS GLU LYS LEU GLU LEU VAL SER TYR PHE GLY LYS SEQRES 6 B 220 ARG PRO PRO GLY VAL LEU HIS CYS THR THR LYS PHE CYS SEQRES 7 B 220 ASP TYR GLY LYS ALA ALA GLY ALA GLU GLU TYR ALA GLN SEQRES 8 B 220 GLN GLU VAL VAL LYS ARG SER TYR GLY LYS ALA PHE LYS SEQRES 9 B 220 LEU SER ILE SER ALA LEU PHE VAL THR PRO LYS THR ALA SEQRES 10 B 220 GLY ALA GLN VAL VAL LEU THR ASP GLN GLU LEU GLN LEU SEQRES 11 B 220 TRP PRO SER ASP LEU ASP LYS PRO SER ALA SER GLU GLY SEQRES 12 B 220 LEU PRO PRO GLY SER ARG ALA HIS VAL THR LEU GLY CYS SEQRES 13 B 220 ALA ALA ASP VAL GLN PRO VAL GLN THR GLY LEU ASP LEU SEQRES 14 B 220 LEU ASP ILE LEU GLN GLN VAL LYS GLY GLY SER GLN GLY SEQRES 15 B 220 GLU ALA VAL GLY GLU LEU PRO ARG GLY LYS LEU TYR SER SEQRES 16 B 220 LEU GLY LYS GLY ARG TRP MET LEU SER LEU THR LYS LYS SEQRES 17 B 220 MET GLU VAL LYS ALA ILE PHE THR GLY TYR TYR GLY SEQRES 1 D 131 GLU VAL GLN LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 131 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 D 131 ILE THR LEU ASP ASP PHE GLY ILE GLY TRP PHE ARG GLN SEQRES 4 D 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA CYS ILE SER SEQRES 5 D 131 PRO GLY TYR GLU HIS ILE TYR TYR ALA ASP SER ALA LYS SEQRES 6 D 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 131 VAL TYR LEU GLN MET ASN ASN LEU LYS PRO TRP ASP THR SEQRES 8 D 131 GLY VAL TYR TYR CYS ALA ALA ASP ASN ASP LEU PRO ASP SEQRES 9 D 131 ARG LEU TRP GLY GLY SER ASP TRP SER ASP PRO SER PRO SEQRES 10 D 131 TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 11 D 131 SER SEQRES 1 E 220 GLY LEU GLU LYS ASP PHE LEU PRO LEU TYR PHE GLY TRP SEQRES 2 E 220 PHE LEU THR LYS LYS SER SER GLU THR LEU ARG LYS ALA SEQRES 3 E 220 GLY GLN VAL PHE LEU GLU GLU LEU GLY ASN HIS LYS ALA SEQRES 4 E 220 PHE LYS LYS GLU LEU ARG HIS PHE ILE SER GLY ASP GLU SEQRES 5 E 220 PRO LYS GLU LYS LEU GLU LEU VAL SER TYR PHE GLY LYS SEQRES 6 E 220 ARG PRO PRO GLY VAL LEU HIS CYS THR THR LYS PHE CYS SEQRES 7 E 220 ASP TYR GLY LYS ALA ALA GLY ALA GLU GLU TYR ALA GLN SEQRES 8 E 220 GLN GLU VAL VAL LYS ARG SER TYR GLY LYS ALA PHE LYS SEQRES 9 E 220 LEU SER ILE SER ALA LEU PHE VAL THR PRO LYS THR ALA SEQRES 10 E 220 GLY ALA GLN VAL VAL LEU THR ASP GLN GLU LEU GLN LEU SEQRES 11 E 220 TRP PRO SER ASP LEU ASP LYS PRO SER ALA SER GLU GLY SEQRES 12 E 220 LEU PRO PRO GLY SER ARG ALA HIS VAL THR LEU GLY CYS SEQRES 13 E 220 ALA ALA ASP VAL GLN PRO VAL GLN THR GLY LEU ASP LEU SEQRES 14 E 220 LEU ASP ILE LEU GLN GLN VAL LYS GLY GLY SER GLN GLY SEQRES 15 E 220 GLU ALA VAL GLY GLU LEU PRO ARG GLY LYS LEU TYR SER SEQRES 16 E 220 LEU GLY LYS GLY ARG TRP MET LEU SER LEU THR LYS LYS SEQRES 17 E 220 MET GLU VAL LYS ALA ILE PHE THR GLY TYR TYR GLY SEQRES 1 F 131 GLU VAL GLN LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 131 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 F 131 ILE THR LEU ASP ASP PHE GLY ILE GLY TRP PHE ARG GLN SEQRES 4 F 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA CYS ILE SER SEQRES 5 F 131 PRO GLY TYR GLU HIS ILE TYR TYR ALA ASP SER ALA LYS SEQRES 6 F 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 F 131 VAL TYR LEU GLN MET ASN ASN LEU LYS PRO TRP ASP THR SEQRES 8 F 131 GLY VAL TYR TYR CYS ALA ALA ASP ASN ASP LEU PRO ASP SEQRES 9 F 131 ARG LEU TRP GLY GLY SER ASP TRP SER ASP PRO SER PRO SEQRES 10 F 131 TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 11 F 131 SER SEQRES 1 G 220 GLY LEU GLU LYS ASP PHE LEU PRO LEU TYR PHE GLY TRP SEQRES 2 G 220 PHE LEU THR LYS LYS SER SER GLU THR LEU ARG LYS ALA SEQRES 3 G 220 GLY GLN VAL PHE LEU GLU GLU LEU GLY ASN HIS LYS ALA SEQRES 4 G 220 PHE LYS LYS GLU LEU ARG HIS PHE ILE SER GLY ASP GLU SEQRES 5 G 220 PRO LYS GLU LYS LEU GLU LEU VAL SER TYR PHE GLY LYS SEQRES 6 G 220 ARG PRO PRO GLY VAL LEU HIS CYS THR THR LYS PHE CYS SEQRES 7 G 220 ASP TYR GLY LYS ALA ALA GLY ALA GLU GLU TYR ALA GLN SEQRES 8 G 220 GLN GLU VAL VAL LYS ARG SER TYR GLY LYS ALA PHE LYS SEQRES 9 G 220 LEU SER ILE SER ALA LEU PHE VAL THR PRO LYS THR ALA SEQRES 10 G 220 GLY ALA GLN VAL VAL LEU THR ASP GLN GLU LEU GLN LEU SEQRES 11 G 220 TRP PRO SER ASP LEU ASP LYS PRO SER ALA SER GLU GLY SEQRES 12 G 220 LEU PRO PRO GLY SER ARG ALA HIS VAL THR LEU GLY CYS SEQRES 13 G 220 ALA ALA ASP VAL GLN PRO VAL GLN THR GLY LEU ASP LEU SEQRES 14 G 220 LEU ASP ILE LEU GLN GLN VAL LYS GLY GLY SER GLN GLY SEQRES 15 G 220 GLU ALA VAL GLY GLU LEU PRO ARG GLY LYS LEU TYR SER SEQRES 16 G 220 LEU GLY LYS GLY ARG TRP MET LEU SER LEU THR LYS LYS SEQRES 17 G 220 MET GLU VAL LYS ALA ILE PHE THR GLY TYR TYR GLY SEQRES 1 H 131 GLU VAL GLN LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 131 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 H 131 ILE THR LEU ASP ASP PHE GLY ILE GLY TRP PHE ARG GLN SEQRES 4 H 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA CYS ILE SER SEQRES 5 H 131 PRO GLY TYR GLU HIS ILE TYR TYR ALA ASP SER ALA LYS SEQRES 6 H 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 H 131 VAL TYR LEU GLN MET ASN ASN LEU LYS PRO TRP ASP THR SEQRES 8 H 131 GLY VAL TYR TYR CYS ALA ALA ASP ASN ASP LEU PRO ASP SEQRES 9 H 131 ARG LEU TRP GLY GLY SER ASP TRP SER ASP PRO SER PRO SEQRES 10 H 131 TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 11 H 131 SER HET CA C 201 1 HET CA C 202 1 HET CA D 201 1 HET CA D 202 1 HET CA F 201 1 HET CA H 201 1 HET CA H 202 1 HETNAM CA CALCIUM ION FORMUL 9 CA 7(CA 2+) HELIX 1 AA1 GLU A 161 LEU A 165 5 5 HELIX 2 AA2 THR A 174 ASN A 194 1 21 HELIX 3 AA3 HIS A 195 LYS A 200 1 6 HELIX 4 AA4 LEU A 217 PHE A 221 1 5 HELIX 5 AA5 GLY A 243 GLN A 249 1 7 HELIX 6 AA6 GLN A 250 TYR A 257 1 8 HELIX 7 AA7 THR A 282 GLN A 287 1 6 HELIX 8 AA8 VAL A 321 LYS A 335 1 15 HELIX 9 AA9 ASP C 62 LYS C 65 5 4 HELIX 10 AB1 LYS C 84 THR C 88 5 5 HELIX 11 AB2 PRO C 100 GLY C 106 5 7 HELIX 12 AB3 THR B 174 ASN B 194 1 21 HELIX 13 AB4 HIS B 195 GLU B 201 1 7 HELIX 14 AB5 GLU B 216 PHE B 221 1 6 HELIX 15 AB6 ASP B 237 LYS B 240 5 4 HELIX 16 AB7 GLY B 243 GLN B 249 1 7 HELIX 17 AB8 GLN B 250 TYR B 257 1 8 HELIX 18 AB9 GLN B 284 TRP B 289 5 6 HELIX 19 AC1 VAL B 321 GLY B 337 1 17 HELIX 20 AC2 ASN D 74 LYS D 76 5 3 HELIX 21 AC3 LYS D 84 THR D 88 5 5 HELIX 22 AC4 PRO D 100 GLY D 105 1 6 HELIX 23 AC5 GLU E 161 LEU E 165 5 5 HELIX 24 AC6 THR E 174 HIS E 195 1 22 HELIX 25 AC7 HIS E 195 GLU E 201 1 7 HELIX 26 AC8 GLU E 216 PHE E 221 1 6 HELIX 27 AC9 ASP E 237 LYS E 240 5 4 HELIX 28 AD1 GLY E 243 GLN E 249 1 7 HELIX 29 AD2 GLN E 250 TYR E 257 1 8 HELIX 30 AD3 GLN E 284 TRP E 289 5 6 HELIX 31 AD4 VAL E 321 GLY E 337 1 17 HELIX 32 AD5 ASP F 62 LYS F 65 5 4 HELIX 33 AD6 LYS F 84 THR F 88 5 5 HELIX 34 AD7 ASP F 101 GLY F 105 5 5 HELIX 35 AD8 THR G 174 HIS G 195 1 22 HELIX 36 AD9 HIS G 195 GLU G 201 1 7 HELIX 37 AE1 GLU G 216 PHE G 221 1 6 HELIX 38 AE2 ASP G 237 LYS G 240 5 4 HELIX 39 AE3 GLY G 243 GLN G 249 1 7 HELIX 40 AE4 GLN G 250 SER G 256 1 7 HELIX 41 AE5 THR G 282 GLN G 287 1 6 HELIX 42 AE6 VAL G 321 GLY G 337 1 17 HELIX 43 AE7 LYS H 84 THR H 88 5 5 HELIX 44 AE8 PRO H 100 GLY H 105 5 6 SHEET 1 AA1 6 HIS A 230 PHE A 235 0 SHEET 2 AA1 6 TYR A 168 LEU A 173 -1 N TRP A 171 O CYS A 231 SHEET 3 AA1 6 TRP A 359 TYR A 376 -1 O ILE A 372 N PHE A 172 SHEET 4 AA1 6 ALA A 260 VAL A 270 -1 N PHE A 261 O ALA A 371 SHEET 5 AA1 6 THR A 274 VAL A 280 -1 O GLN A 278 N SER A 266 SHEET 6 AA1 6 HIS A 309 CYS A 314 -1 O LEU A 312 N ALA A 275 SHEET 1 AA2 5 HIS A 230 PHE A 235 0 SHEET 2 AA2 5 TYR A 168 LEU A 173 -1 N TRP A 171 O CYS A 231 SHEET 3 AA2 5 TRP A 359 TYR A 376 -1 O ILE A 372 N PHE A 172 SHEET 4 AA2 5 GLY A 349 SER A 353 -1 N TYR A 352 O MET A 360 SHEET 5 AA2 5 GLY A 344 GLU A 345 -1 N GLY A 344 O LEU A 351 SHEET 1 AA3 4 GLN C 3 SER C 7 0 SHEET 2 AA3 4 LEU C 18 SER C 25 -1 O ALA C 23 N GLU C 5 SHEET 3 AA3 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA3 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AA4 6 LEU C 11 VAL C 12 0 SHEET 2 AA4 6 THR C 122 VAL C 126 1 O THR C 125 N VAL C 12 SHEET 3 AA4 6 GLY C 89 ASP C 96 -1 N GLY C 89 O VAL C 124 SHEET 4 AA4 6 GLY C 33 GLN C 39 -1 N GLN C 39 O VAL C 90 SHEET 5 AA4 6 GLU C 46 ILE C 51 -1 O ALA C 49 N TRP C 36 SHEET 6 AA4 6 ILE C 58 TYR C 60 -1 O TYR C 59 N CYS C 50 SHEET 1 AA5 4 LEU C 11 VAL C 12 0 SHEET 2 AA5 4 THR C 122 VAL C 126 1 O THR C 125 N VAL C 12 SHEET 3 AA5 4 GLY C 89 ASP C 96 -1 N GLY C 89 O VAL C 124 SHEET 4 AA5 4 TYR C 117 TRP C 118 -1 O TYR C 117 N ALA C 95 SHEET 1 AA6 6 HIS B 230 PHE B 235 0 SHEET 2 AA6 6 TYR B 168 LEU B 173 -1 N TRP B 171 O CYS B 231 SHEET 3 AA6 6 TRP B 359 TYR B 376 -1 O ILE B 372 N PHE B 172 SHEET 4 AA6 6 ALA B 260 VAL B 270 -1 N PHE B 261 O ALA B 371 SHEET 5 AA6 6 THR B 274 VAL B 280 -1 O GLY B 276 N PHE B 269 SHEET 6 AA6 6 HIS B 309 CYS B 314 -1 O LEU B 312 N ALA B 275 SHEET 1 AA7 5 HIS B 230 PHE B 235 0 SHEET 2 AA7 5 TYR B 168 LEU B 173 -1 N TRP B 171 O CYS B 231 SHEET 3 AA7 5 TRP B 359 TYR B 376 -1 O ILE B 372 N PHE B 172 SHEET 4 AA7 5 GLY B 349 SER B 353 -1 N TYR B 352 O MET B 360 SHEET 5 AA7 5 ALA B 342 LEU B 346 -1 N GLY B 344 O LEU B 351 SHEET 1 AA8 4 GLN D 3 GLU D 5 0 SHEET 2 AA8 4 LEU D 18 SER D 25 -1 O ALA D 23 N GLU D 5 SHEET 3 AA8 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AA8 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AA9 6 LEU D 11 VAL D 12 0 SHEET 2 AA9 6 THR D 122 VAL D 126 1 O THR D 125 N VAL D 12 SHEET 3 AA9 6 GLY D 89 ASP D 96 -1 N GLY D 89 O VAL D 124 SHEET 4 AA9 6 GLY D 33 GLN D 39 -1 N GLY D 35 O ALA D 94 SHEET 5 AA9 6 GLU D 46 ILE D 51 -1 O ALA D 49 N TRP D 36 SHEET 6 AA9 6 ILE D 58 TYR D 60 -1 O TYR D 59 N CYS D 50 SHEET 1 AB1 4 LEU D 11 VAL D 12 0 SHEET 2 AB1 4 THR D 122 VAL D 126 1 O THR D 125 N VAL D 12 SHEET 3 AB1 4 GLY D 89 ASP D 96 -1 N GLY D 89 O VAL D 124 SHEET 4 AB1 4 TYR D 117 TRP D 118 -1 O TYR D 117 N ALA D 95 SHEET 1 AB2 6 HIS E 230 PHE E 235 0 SHEET 2 AB2 6 TYR E 168 LEU E 173 -1 N PHE E 169 O THR E 233 SHEET 3 AB2 6 TRP E 359 TYR E 376 -1 O ILE E 372 N PHE E 172 SHEET 4 AB2 6 ALA E 260 VAL E 270 -1 N PHE E 261 O ALA E 371 SHEET 5 AB2 6 THR E 274 VAL E 280 -1 O VAL E 280 N SER E 264 SHEET 6 AB2 6 HIS E 309 CYS E 314 -1 O GLY E 313 N ALA E 275 SHEET 1 AB3 5 HIS E 230 PHE E 235 0 SHEET 2 AB3 5 TYR E 168 LEU E 173 -1 N PHE E 169 O THR E 233 SHEET 3 AB3 5 TRP E 359 TYR E 376 -1 O ILE E 372 N PHE E 172 SHEET 4 AB3 5 GLY E 349 SER E 353 -1 N TYR E 352 O MET E 360 SHEET 5 AB3 5 GLY E 344 GLU E 345 -1 N GLY E 344 O LEU E 351 SHEET 1 AB4 4 GLN F 3 SER F 7 0 SHEET 2 AB4 4 LEU F 18 SER F 25 -1 O SER F 21 N SER F 7 SHEET 3 AB4 4 THR F 78 MET F 83 -1 O MET F 83 N LEU F 18 SHEET 4 AB4 4 PHE F 68 ARG F 72 -1 N SER F 71 O TYR F 80 SHEET 1 AB5 6 GLY F 10 VAL F 12 0 SHEET 2 AB5 6 THR F 122 VAL F 126 1 O THR F 125 N VAL F 12 SHEET 3 AB5 6 GLY F 89 ASP F 96 -1 N TYR F 91 O THR F 122 SHEET 4 AB5 6 GLY F 33 GLN F 39 -1 N PHE F 37 O TYR F 92 SHEET 5 AB5 6 GLU F 46 ILE F 51 -1 O ALA F 49 N TRP F 36 SHEET 6 AB5 6 ILE F 58 TYR F 60 -1 O TYR F 59 N CYS F 50 SHEET 1 AB6 4 GLY F 10 VAL F 12 0 SHEET 2 AB6 4 THR F 122 VAL F 126 1 O THR F 125 N VAL F 12 SHEET 3 AB6 4 GLY F 89 ASP F 96 -1 N TYR F 91 O THR F 122 SHEET 4 AB6 4 TYR F 117 TRP F 118 -1 O TYR F 117 N ALA F 95 SHEET 1 AB7 6 HIS G 230 PHE G 235 0 SHEET 2 AB7 6 TYR G 168 LEU G 173 -1 N PHE G 169 O THR G 233 SHEET 3 AB7 6 ARG G 358 TYR G 376 -1 O ILE G 372 N PHE G 172 SHEET 4 AB7 6 ALA G 260 VAL G 270 -1 N PHE G 261 O ALA G 371 SHEET 5 AB7 6 THR G 274 VAL G 280 -1 O VAL G 280 N SER G 264 SHEET 6 AB7 6 HIS G 309 CYS G 314 -1 O LEU G 312 N ALA G 275 SHEET 1 AB8 5 HIS G 230 PHE G 235 0 SHEET 2 AB8 5 TYR G 168 LEU G 173 -1 N PHE G 169 O THR G 233 SHEET 3 AB8 5 ARG G 358 TYR G 376 -1 O ILE G 372 N PHE G 172 SHEET 4 AB8 5 LYS G 350 GLY G 355 -1 N TYR G 352 O MET G 360 SHEET 5 AB8 5 ALA G 342 GLU G 345 -1 N GLY G 344 O LEU G 351 SHEET 1 AB9 4 GLN H 3 SER H 7 0 SHEET 2 AB9 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB9 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB9 4 THR H 69 ARG H 72 -1 N SER H 71 O TYR H 80 SHEET 1 AC1 6 GLY H 10 VAL H 12 0 SHEET 2 AC1 6 THR H 122 VAL H 126 1 O THR H 125 N GLY H 10 SHEET 3 AC1 6 GLY H 89 ASP H 96 -1 N GLY H 89 O VAL H 124 SHEET 4 AC1 6 GLY H 33 GLN H 39 -1 N PHE H 37 O TYR H 92 SHEET 5 AC1 6 GLU H 46 ILE H 51 -1 O ILE H 51 N ILE H 34 SHEET 6 AC1 6 ILE H 58 TYR H 60 -1 O TYR H 59 N CYS H 50 SHEET 1 AC2 4 GLY H 10 VAL H 12 0 SHEET 2 AC2 4 THR H 122 VAL H 126 1 O THR H 125 N GLY H 10 SHEET 3 AC2 4 GLY H 89 ASP H 96 -1 N GLY H 89 O VAL H 124 SHEET 4 AC2 4 TYR H 117 TRP H 118 -1 O TYR H 117 N ALA H 95 LINK O PRO A 226 CA CA F 201 1555 4445 2.50 LINK OD1 ASP A 237 CA CA C 201 1555 1555 2.86 LINK O ASP C 31 CA CA C 202 1555 1555 2.62 LINK OD1 ASP C 96 CA CA C 201 1555 1555 2.75 LINK O ASN C 97 CA CA C 202 1555 1555 2.45 LINK OD1 ASN C 97 CA CA C 202 1555 1555 2.29 LINK OD2 ASP C 98 CA CA C 201 1555 1555 2.56 LINK O PRO C 114 CA CA C 201 1555 1555 2.45 LINK OD1 ASP C 116 CA CA C 201 1555 1555 2.57 LINK CA CA C 202 O PRO E 226 4545 1555 2.25 LINK O PRO B 226 CA CA H 201 1555 4546 2.27 LINK OD1 ASP B 237 CA CA D 201 1555 1555 2.56 LINK O ASN D 97 CA CA D 202 1555 1555 2.55 LINK OD2 ASP D 98 CA CA D 201 1555 1555 2.68 LINK OD2 ASP D 101 CA CA D 202 1555 1555 2.56 LINK O PRO D 114 CA CA D 201 1555 1555 2.49 LINK OD1 ASP D 116 CA CA D 201 1555 1555 2.79 LINK CA CA D 202 O PRO G 226 4446 1555 2.29 LINK O ASN F 97 CA CA F 201 1555 1555 2.43 LINK OD1 ASN F 97 CA CA F 201 1555 1555 2.62 LINK O ASP H 31 CA CA H 201 1555 1555 3.09 LINK OD1 ASP H 96 CA CA H 202 1555 1555 2.78 LINK O ASN H 97 CA CA H 201 1555 1555 2.68 LINK OD1 ASN H 97 CA CA H 201 1555 1555 2.35 LINK OD2 ASP H 98 CA CA H 202 1555 1555 2.37 LINK O PRO H 114 CA CA H 202 1555 1555 2.75 LINK OD1 ASP H 116 CA CA H 202 1555 1555 2.58 CISPEP 1 LEU C 99 PRO C 100 0 0.02 CISPEP 2 LEU D 99 PRO D 100 0 0.49 CISPEP 3 LEU F 99 PRO F 100 0 1.25 CISPEP 4 LEU H 99 PRO H 100 0 0.43 CRYST1 101.730 118.250 122.450 90.00 90.00 90.00 P 21 21 21 16 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 0.009830 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008457 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008167 0.00000 MTRIX1 1 -0.997719 -0.066990 -0.008327 17.25823 1 MTRIX2 1 -0.067248 0.997082 0.036116 -3.82566 1 MTRIX3 1 0.005883 0.036593 -0.999313 61.56891 1 MTRIX1 2 0.841360 -0.404431 -0.358536 42.80214 1 MTRIX2 2 0.407064 0.910566 -0.071887 -9.55805 1 MTRIX3 2 0.355544 -0.085464 0.930744 -14.26566 1 MTRIX1 3 -0.802159 0.466015 0.373325 -22.30916 1 MTRIX2 3 0.476241 0.876462 -0.070780 -6.99961 1 MTRIX3 3 -0.360190 0.121016 -0.924997 76.44267 1 MTRIX1 4 -0.997688 -0.058601 -0.034413 18.10422 1 MTRIX2 4 -0.059057 0.998178 0.012379 -3.30722 1 MTRIX3 4 0.033625 0.014383 -0.999331 61.56318 1 MTRIX1 5 0.818783 -0.455529 -0.349410 41.18536 1 MTRIX2 5 0.454682 0.886118 -0.089770 -9.24941 1 MTRIX3 5 0.350511 -0.085368 0.932660 -14.24381 1 MTRIX1 6 -0.777396 0.507643 0.371421 -20.80332 1 MTRIX2 6 0.511627 0.853816 -0.096110 -6.71344 1 MTRIX3 6 -0.365915 0.115314 -0.923477 75.96448 1