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HEADER OXYGEN STORAGE/TRANSPORT 28-APR-06 2GTL TITLE LUMBRICUS ERYTHROCRUORIN AT 3.5A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: EXTRACELLULAR GLOBIN 4; COMPND 3 CHAIN: A, E, I; COMPND 4 SYNONYM: GLOBIN IV, ERYTHROCRUORIN, GLOBIN A; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: EXTRACELLULAR GLOBIN 2; COMPND 7 CHAIN: B, F, J; COMPND 8 SYNONYM: GLOBIN II, ERYTHROCRUORIN, GLOBIN AIII, GLOBIN B; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: EXTRACELLULAR GLOBIN-3; COMPND 11 CHAIN: C, G, K; COMPND 12 SYNONYM: EXTRACELLULAR GLOBIN III, ERYTHROCRUORIN, GLOBIN COMPND 13 C; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: HEMOGLOBIN CHAIN D1; COMPND 16 CHAIN: D, H, L; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: HEMOGLOBIN LINKER CHAIN L1; COMPND 19 CHAIN: M; COMPND 20 MOL_ID: 6; COMPND 21 MOLECULE: EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT; COMPND 22 CHAIN: N; COMPND 23 MOL_ID: 7; COMPND 24 MOLECULE: EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT; COMPND 25 CHAIN: O SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 3 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 6 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 9 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 10 MOL_ID: 4; SOURCE 11 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 12 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 13 MOL_ID: 5; SOURCE 14 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 15 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 16 MOL_ID: 6; SOURCE 17 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 18 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 19 MOL_ID: 7; SOURCE 20 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 21 ORGANISM_COMMON: COMMON EARTHWORM KEYWDS ANNELID ERYTHROCRUORINS, RESPIRATORY PROTEIN, HEXAGONAL KEYWDS 2 BILAYER, DIHEDRAL D6 SYMMETRY, TRIPLE STRANDED HELICAL COILS EXPDTA X-RAY DIFFRACTION AUTHOR W.E.ROYER JR.,H.SHARMA,K.STRAND,J.E.KNAPP,B.BHYRAVBHATLA REVDAT 2 01-AUG-06 2GTL 1 JRNL REVDAT 1 18-JUL-06 2GTL 0 JRNL AUTH W.E.ROYER JR.,H.SHARMA,K.STRAND,J.E.KNAPP, JRNL AUTH 2 B.BHYRAVBHATLA JRNL TITL LUMBRICUS ERYTHROCRUORIN AT 3.5 A RESOLUTION: JRNL TITL 2 ARCHITECTURE OF A MEGADALTON RESPIRATORY COMPLEX. JRNL REF STRUCTURE V. 14 1167 2006 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 775689 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM IN RESOLUTION SHELLS REMARK 3 R VALUE (WORKING SET) : 0.288 REMARK 3 FREE R VALUE : 0.297 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 38554 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 50 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.52 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10785 REMARK 3 BIN R VALUE (WORKING SET) : 0.4280 REMARK 3 BIN FREE R VALUE : 0.4170 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 560 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 19103 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 545 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.78 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 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2GTL COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-18) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB037533. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 14-BM-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 890862 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 100.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.3 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 74.9 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: CNS REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 6% (W/W) PEG 8000, 10MM CACL2, 3% REMARK 280 ISOPROPANOL, 60MM HEPES, PH 7.5, VAPOR DIFFUSION, TEMPERATURE REMARK 280 298.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE UNIQUE NON-CRYSTALLOGRAPHIC REPEAT REMARK 300 UNIT, WHICH CONSISTS OF 15 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR REMARK 300 DCOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = D6). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 0.987212 0.158328 0.018543 0.16036 REMARK 350 BIOMT2 2 -0.064738 0.504495 -0.860984 -0.36070 REMARK 350 BIOMT3 2 -0.145673 0.848774 0.508293 0.96356 REMARK 350 BIOMT1 3 0.961637 0.251919 -0.108587 0.27942 REMARK 350 BIOMT2 3 0.028852 -0.486516 -0.873195 -1.38266 REMARK 350 BIOMT3 3 -0.272803 0.836564 -0.475121 1.12382 REMARK 350 BIOMT1 4 0.948849 0.187181 -0.254260 0.23813 REMARK 350 BIOMT2 4 0.187181 -0.982022 -0.024421 -2.04392 REMARK 350 BIOMT3 4 -0.254260 -0.024421 -0.966828 0.32052 REMARK 350 BIOMT1 5 0.961637 0.028852 -0.272803 0.07777 REMARK 350 BIOMT2 5 0.251919 -0.486516 0.836564 -1.68322 REMARK 350 BIOMT3 5 -0.108587 -0.873195 -0.475121 -0.64304 REMARK 350 BIOMT1 6 0.987212 -0.064738 -0.145673 -0.04129 REMARK 350 BIOMT2 6 0.158328 0.504495 0.848774 -0.66126 REMARK 350 BIOMT3 6 0.018543 -0.860984 0.508293 -0.80330 REMARK 350 BIOMT1 7 -0.996434 -0.078644 -0.030564 -0.71655 REMARK 350 BIOMT2 7 -0.078644 0.734460 0.674079 -0.45444 REMARK 350 BIOMT3 7 -0.030564 0.674079 -0.738026 1.08571 REMARK 350 BIOMT1 8 -0.974148 -0.223382 0.033699 -0.87742 REMARK 350 BIOMT2 8 -0.223382 0.930221 -0.291187 -0.08245 REMARK 350 BIOMT3 8 0.033699 -0.291187 -0.956072 0.12654 REMARK 350 BIOMT1 9 -0.952139 -0.238328 0.191393 -0.92059 REMARK 350 BIOMT2 9 -0.238328 0.186771 -0.953056 -0.73438 REMARK 350 BIOMT3 9 0.191393 -0.953056 -0.234632 -0.68426 REMARK 350 BIOMT1 10 -0.952415 -0.108536 0.284824 -0.80288 REMARK 350 BIOMT2 10 -0.108536 -0.752438 -0.649659 -1.75829 REMARK 350 BIOMT3 10 0.284824 -0.649659 0.704854 -0.53589 REMARK 350 BIOMT1 11 -0.974701 0.036201 0.220561 -0.64202 REMARK 350 BIOMT2 11 0.036201 -0.948199 0.315608 -2.13028 REMARK 350 BIOMT3 11 0.220561 0.315608 0.922900 0.42329 REMARK 350 BIOMT1 12 -0.996710 0.051147 0.062867 -0.59885 REMARK 350 BIOMT2 12 0.051147 -0.204749 0.977477 -1.47835 REMARK 350 BIOMT3 12 0.062867 0.977477 0.201460 1.23408 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 ALA A 1 REMARK 465 ASP A 2 REMARK 465 ASP A 3 REMARK 465 GLU A 4 REMARK 465 ASP C 1 REMARK 465 GLU C 2 REMARK 465 ASN C 152 REMARK 465 ALA C 153 REMARK 465 ALA E 1 REMARK 465 ASP E 2 REMARK 465 ASP E 3 REMARK 465 GLU E 4 REMARK 465 ASP G 1 REMARK 465 GLU G 2 REMARK 465 ASN G 152 REMARK 465 ALA G 153 REMARK 465 ALA I 1 REMARK 465 ASP I 2 REMARK 465 ASP I 3 REMARK 465 GLU I 4 REMARK 465 ASP K 1 REMARK 465 GLU K 2 REMARK 465 ASN K 152 REMARK 465 ALA K 153 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 HIS C 3 CG ND1 CD2 CE1 NE2 REMARK 470 HIS G 3 CG ND1 CD2 CE1 NE2 REMARK 470 HIS K 3 CG ND1 CD2 CE1 NE2 REMARK 470 LEU M 13 CG CD1 CD2 REMARK 470 LYS M 15 CG CD CE NZ REMARK 470 ASP M 22 CG OD1 OD2 REMARK 470 LYS M 26 CG CD CE NZ REMARK 470 LYS M 27 CG CD CE NZ REMARK 470 ASP M 30 CG OD1 OD2 REMARK 470 LYS M 37 CG CD CE NZ REMARK 470 ASP M 43 CG OD1 OD2 REMARK 470 LYS M 44 CG CD CE NZ REMARK 470 LYS M 45 CG CD CE NZ REMARK 470 GLU M 59 CG CD OE1 OE2 REMARK 470 GLU M 64 CG CD OE1 OE2 REMARK 470 SER M 187 CB OG REMARK 470 PHE N 19 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG N 23 CG CD NE CZ NH1 NH2 REMARK 470 ARG N 26 CG CD NE CZ NH1 NH2 REMARK 470 GLU N 39 CG CD OE1 OE2 REMARK 470 ASP N 186 CB CG OD1 OD2 REMARK 470 HIS N 228 CG ND1 CD2 CE1 NE2 REMARK 470 ASP N 229 CG OD1 OD2 REMARK 470 GLN O 8 CG CD OE1 NE2 REMARK 470 SER O 9 OG REMARK 470 HIS O 10 CG ND1 CD2 CE1 NE2 REMARK 470 ASP O 11 CG OD1 OD2 REMARK 470 GLU O 12 CG CD OE1 OE2 REMARK 470 ILE O 13 CG1 CG2 CD1 REMARK 470 ILE O 14 CG1 CG2 CD1 REMARK 470 ASP O 15 CG OD1 OD2 REMARK 470 LYS O 16 CG CD CE NZ REMARK 470 LEU O 17 CG CD1 CD2 REMARK 470 ILE O 18 CG1 CG2 CD1 REMARK 470 GLU O 19 CG CD OE1 OE2 REMARK 470 LYS O 23 CG CD CE NZ REMARK 470 LYS O 221 CG CD CE NZ REMARK 470 LYS O 222 CG CD CE NZ 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 THR A 48 N THR A 48 CA -0.066 REMARK 500 MET D 83 SD MET D 83 CE -0.065 REMARK 500 GLN D 141 CA GLN D 141 C 0.053 REMARK 500 MET O 125 SD MET O 125 CE 0.072 REMARK 500 ILE O 204 CA ILE O 204 CB -0.057 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLY A 64 N - CA - C ANGL. DEV. = -7.6 DEGREES REMARK 500 GLU A 65 N - CA - C ANGL. DEV. = -8.5 DEGREES REMARK 500 LEU A 150 N - CA - C ANGL. DEV. = 11.0 DEGREES REMARK 500 ARG B 123 N - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 ARG C 13 N - CA - C ANGL. DEV. = -7.1 DEGREES REMARK 500 CYS D 138 N - CA - C ANGL. DEV. = 9.3 DEGREES REMARK 500 GLY E 64 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 GLU E 65 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 LEU E 150 N - CA - C ANGL. DEV. = 11.2 DEGREES REMARK 500 ARG F 123 N - CA - C ANGL. DEV. = 7.9 DEGREES REMARK 500 CYS H 138 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 GLY I 64 N - CA - C ANGL. DEV. = -7.9 DEGREES REMARK 500 GLU I 65 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 THR I 87 N - CA - C ANGL. DEV. = 7.1 DEGREES REMARK 500 LEU I 150 N - CA - C ANGL. DEV. = 11.3 DEGREES REMARK 500 ARG J 123 N - CA - C ANGL. DEV. = 7.6 DEGREES REMARK 500 ARG K 13 N - CA - C ANGL. DEV. = -7.5 DEGREES REMARK 500 CYS L 138 N - CA - C ANGL. DEV. = 8.7 DEGREES REMARK 500 HIS M 61 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 THR M 116 N - CA - C ANGL. DEV. = -7.4 DEGREES REMARK 500 SER M 119 N - CA - C ANGL. DEV. = 11.4 DEGREES REMARK 500 CYS M 120 N - CA - C ANGL. DEV. = 7.6 DEGREES REMARK 500 HIS M 160 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 THR M 161 N - CA - C ANGL. DEV. = -7.3 DEGREES REMARK 500 VAL M 210 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 VAL M 216 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 ALA M 222 N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 CYS N 76 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 CYS N 83 CA - CB - SG ANGL. DEV. = -8.4 DEGREES REMARK 500 ASP N 84 N - CA - C ANGL. DEV. = 7.6 DEGREES REMARK 500 ASP N 101 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 GLY N 119 N - CA - C ANGL. DEV. = 11.0 DEGREES REMARK 500 LEU N 179 N - CA - C ANGL. DEV. = -7.9 DEGREES REMARK 500 ARG N 209 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 CYS O 69 CA - CB - SG ANGL. DEV. = -9.2 DEGREES REMARK 500 PRO O 140 N - CA - C ANGL. DEV. = 7.7 DEGREES REMARK 500 HIS O 145 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 GLU O 160 N - CA - C ANGL. DEV. = -7.1 DEGREES REMARK 500 GLY O 194 N - CA - C ANGL. DEV. = -7.6 DEGREES REMARK 500 HIS O 206 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHORS STATE THAT THE CONFLICTS AT RESIDUE 78 FOR REMARK 999 CHAINS A,E,I AND RESIDUE 66 FOR CHAINS B,F,J ARE REMARK 999 POSSIBLY DUE TO AN ERROR WITH THE SEQUENCING, REMARK 999 HOWEVER THEY CAN NOT DISTINGUISH IT AT THE CURRENT REMARK 999 RESOLUTION. DBREF 2GTL A 1 151 UNP P13579 GLB4_LUMTE 1 151 DBREF 2GTL E 1 151 UNP P13579 GLB4_LUMTE 1 151 DBREF 2GTL I 1 151 UNP P13579 GLB4_LUMTE 1 151 DBREF 2GTL B 1 145 UNP P02218 GLB2_LUMTE 1 145 DBREF 2GTL F 1 145 UNP P02218 GLB2_LUMTE 1 145 DBREF 2GTL J 1 145 UNP P02218 GLB2_LUMTE 1 145 DBREF 2GTL C 1 153 UNP P11069 GLB3_LUMTE 18 170 DBREF 2GTL G 1 153 UNP P11069 GLB3_LUMTE 18 170 DBREF 2GTL K 1 153 UNP P11069 GLB3_LUMTE 18 170 DBREF 2GTL D 8 147 UNP O61233 O61233_LUMTE 19 158 DBREF 2GTL H 8 147 UNP O61233 O61233_LUMTE 19 158 DBREF 2GTL L 8 147 UNP O61233 O61233_LUMTE 19 158 DBREF 2GTL M 9 225 UNP Q9GV76 Q9GV76_LUMTE 24 240 DBREF 2GTL N 10 229 UNP Q2I743 Q2I743_LUMTE 47 266 DBREF 2GTL O 8 222 UNP Q2I742 Q2I742_LUMTE 26 240 SEQADV 2GTL LYS A 78 UNP P13579 ASP 78 CONFLICT SEQADV 2GTL LYS E 78 UNP P13579 ASP 78 CONFLICT SEQADV 2GTL LYS I 78 UNP P13579 ASP 78 CONFLICT SEQADV 2GTL ASP B 66 UNP P02218 GLU 66 CONFLICT SEQADV 2GTL ASP F 66 UNP P02218 GLU 66 CONFLICT SEQADV 2GTL ASP J 66 UNP P02218 GLU 66 CONFLICT SEQADV 2GTL GLU C 49 UNP P11069 ASP 66 CONFLICT SEQADV 2GTL GLU G 49 UNP P11069 ASP 66 CONFLICT SEQADV 2GTL GLU K 49 UNP P11069 ASP 66 CONFLICT SEQADV 2GTL CYS O 113 UNP Q2I742 VAL 131 CONFLICT SEQRES 1 A 151 ALA ASP ASP GLU ASP CYS CYS SER TYR GLU ASP ARG ARG SEQRES 2 A 151 GLU ILE ARG HIS ILE TRP ASP ASP VAL TRP SER SER SER SEQRES 3 A 151 PHE THR ASP ARG ARG VAL ALA ILE VAL ARG ALA VAL PHE SEQRES 4 A 151 ASP ASP LEU PHE LYS HIS TYR PRO THR SER LYS ALA LEU SEQRES 5 A 151 PHE GLU ARG VAL LYS ILE ASP GLU PRO GLU SER GLY GLU SEQRES 6 A 151 PHE LYS SER HIS LEU VAL ARG VAL ALA ASN GLY LEU LYS SEQRES 7 A 151 LEU LEU ILE ASN LEU LEU ASP ASP THR LEU VAL LEU GLN SEQRES 8 A 151 SER HIS LEU GLY HIS LEU ALA ASP GLN HIS ILE GLN ARG SEQRES 9 A 151 LYS GLY VAL THR LYS GLU TYR PHE ARG GLY ILE GLY GLU SEQRES 10 A 151 ALA PHE ALA ARG VAL LEU PRO GLN VAL LEU SER CYS PHE SEQRES 11 A 151 ASN VAL ASP ALA TRP ASN ARG CYS PHE HIS ARG LEU VAL SEQRES 12 A 151 ALA ARG ILE ALA LYS ASP LEU PRO SEQRES 1 B 145 LYS LYS GLN CYS GLY VAL LEU GLU GLY LEU LYS VAL LYS SEQRES 2 B 145 SER GLU TRP GLY ARG ALA TYR GLY SER GLY HIS ASP ARG SEQRES 3 B 145 GLU ALA PHE SER GLN ALA ILE TRP ARG ALA THR PHE ALA SEQRES 4 B 145 GLN VAL PRO GLU SER ARG SER LEU PHE LYS ARG VAL HIS SEQRES 5 B 145 GLY ASP ASP THR SER HIS PRO ALA PHE ILE ALA HIS ALA SEQRES 6 B 145 ASP ARG VAL LEU GLY GLY LEU ASP ILE ALA ILE SER THR SEQRES 7 B 145 LEU ASP GLN PRO ALA THR LEU LYS GLU GLU LEU ASP HIS SEQRES 8 B 145 LEU GLN VAL GLN HIS GLU GLY ARG LYS ILE PRO ASP ASN SEQRES 9 B 145 TYR PHE ASP ALA PHE LYS THR ALA ILE LEU HIS VAL VAL SEQRES 10 B 145 ALA ALA GLN LEU GLY ARG CYS TYR ASP ARG GLU ALA TRP SEQRES 11 B 145 ASP ALA CYS ILE ASP HIS ILE GLU ASP GLY ILE LYS GLY SEQRES 12 B 145 HIS HIS SEQRES 1 C 153 ASP GLU HIS GLU HIS CYS CYS SER GLU GLU ASP HIS ARG SEQRES 2 C 153 ILE VAL GLN LYS GLN TRP ASP ILE LEU TRP ARG ASP THR SEQRES 3 C 153 GLU SER SER LYS ILE LYS ILE GLY PHE GLY ARG LEU LEU SEQRES 4 C 153 LEU THR LYS LEU ALA LYS ASP ILE PRO GLU VAL ASN ASP SEQRES 5 C 153 LEU PHE LYS ARG VAL ASP ILE GLU HIS ALA GLU GLY PRO SEQRES 6 C 153 LYS PHE SER ALA HIS ALA LEU ARG ILE LEU ASN GLY LEU SEQRES 7 C 153 ASP LEU ALA ILE ASN LEU LEU ASP ASP PRO PRO ALA LEU SEQRES 8 C 153 ASP ALA ALA LEU ASP HIS LEU ALA HIS GLN HIS GLU VAL SEQRES 9 C 153 ARG GLU GLY VAL GLN LYS ALA HIS PHE LYS LYS PHE GLY SEQRES 10 C 153 GLU ILE LEU ALA THR GLY LEU PRO GLN VAL LEU ASP ASP SEQRES 11 C 153 TYR ASP ALA LEU ALA TRP LYS SER CYS LEU LYS GLY ILE SEQRES 12 C 153 LEU THR LYS ILE SER SER ARG LEU ASN ALA SEQRES 1 D 140 GLU CYS LEU VAL THR GLU SER LEU LYS VAL LYS LEU GLN SEQRES 2 D 140 TRP ALA SER ALA PHE GLY HIS ALA HIS GLU ARG VAL ALA SEQRES 3 D 140 PHE GLY LEU GLU LEU TRP ARG ASP ILE ILE ASP ASP HIS SEQRES 4 D 140 PRO GLU ILE LYS ALA PRO PHE SER ARG VAL ARG GLY ASP SEQRES 5 D 140 ASN ILE TYR SER PRO GLU PHE GLY ALA HIS SER GLN ARG SEQRES 6 D 140 VAL LEU SER GLY LEU ASP ILE THR ILE SER MET LEU ASP SEQRES 7 D 140 THR PRO ASP MET LEU ALA ALA GLN LEU ALA HIS LEU LYS SEQRES 8 D 140 VAL GLN HIS VAL GLU ARG ASN LEU LYS PRO GLU PHE PHE SEQRES 9 D 140 ASP ILE PHE LEU LYS HIS LEU LEU HIS VAL LEU GLY ASP SEQRES 10 D 140 ARG LEU GLY THR HIS PHE ASP PHE GLY ALA TRP HIS ASP SEQRES 11 D 140 CYS VAL ASP GLN ILE ILE ASP GLY ILE LYS SEQRES 1 E 151 ALA ASP ASP GLU ASP CYS CYS SER TYR GLU ASP ARG ARG SEQRES 2 E 151 GLU ILE ARG HIS ILE TRP ASP ASP VAL TRP SER SER SER SEQRES 3 E 151 PHE THR ASP ARG ARG VAL ALA ILE VAL ARG ALA VAL PHE SEQRES 4 E 151 ASP ASP LEU PHE LYS HIS TYR PRO THR SER LYS ALA LEU SEQRES 5 E 151 PHE GLU ARG VAL LYS ILE ASP GLU PRO GLU SER GLY GLU SEQRES 6 E 151 PHE LYS SER HIS LEU VAL ARG VAL ALA ASN GLY LEU LYS SEQRES 7 E 151 LEU LEU ILE ASN LEU LEU ASP ASP THR LEU VAL LEU GLN SEQRES 8 E 151 SER HIS LEU GLY HIS LEU ALA ASP GLN HIS ILE GLN ARG SEQRES 9 E 151 LYS GLY VAL THR LYS GLU TYR PHE ARG GLY ILE GLY GLU SEQRES 10 E 151 ALA PHE ALA ARG VAL LEU PRO GLN VAL LEU SER CYS PHE SEQRES 11 E 151 ASN VAL ASP ALA TRP ASN ARG CYS PHE HIS ARG LEU VAL SEQRES 12 E 151 ALA ARG ILE ALA LYS ASP LEU PRO SEQRES 1 F 145 LYS LYS GLN CYS GLY VAL LEU GLU GLY LEU LYS VAL LYS SEQRES 2 F 145 SER GLU TRP GLY ARG ALA TYR GLY SER GLY HIS ASP ARG SEQRES 3 F 145 GLU ALA PHE SER GLN ALA ILE TRP ARG ALA THR PHE ALA SEQRES 4 F 145 GLN VAL PRO GLU SER ARG SER LEU PHE LYS ARG VAL HIS SEQRES 5 F 145 GLY ASP ASP THR SER HIS PRO ALA PHE ILE ALA HIS ALA SEQRES 6 F 145 ASP ARG VAL LEU GLY GLY LEU ASP ILE ALA ILE SER THR SEQRES 7 F 145 LEU ASP GLN PRO ALA THR LEU LYS GLU GLU LEU ASP HIS SEQRES 8 F 145 LEU GLN VAL GLN HIS GLU GLY ARG LYS ILE PRO ASP ASN SEQRES 9 F 145 TYR PHE ASP ALA PHE LYS THR ALA ILE LEU HIS VAL VAL SEQRES 10 F 145 ALA ALA GLN LEU GLY ARG CYS TYR ASP ARG GLU ALA TRP SEQRES 11 F 145 ASP ALA CYS ILE ASP HIS ILE GLU ASP GLY ILE LYS GLY SEQRES 12 F 145 HIS HIS SEQRES 1 G 153 ASP GLU HIS GLU HIS CYS CYS SER GLU GLU ASP HIS ARG SEQRES 2 G 153 ILE VAL GLN LYS GLN TRP ASP ILE LEU TRP ARG ASP THR SEQRES 3 G 153 GLU SER SER LYS ILE LYS ILE GLY PHE GLY ARG LEU LEU SEQRES 4 G 153 LEU THR LYS LEU ALA LYS ASP ILE PRO GLU VAL ASN ASP SEQRES 5 G 153 LEU PHE LYS ARG VAL ASP ILE GLU HIS ALA GLU GLY PRO SEQRES 6 G 153 LYS PHE SER ALA HIS ALA LEU ARG ILE LEU ASN GLY LEU SEQRES 7 G 153 ASP LEU ALA ILE ASN LEU LEU ASP ASP PRO PRO ALA LEU SEQRES 8 G 153 ASP ALA ALA LEU ASP HIS LEU ALA HIS GLN HIS GLU VAL SEQRES 9 G 153 ARG GLU GLY VAL GLN LYS ALA HIS PHE LYS LYS PHE GLY SEQRES 10 G 153 GLU ILE LEU ALA THR GLY LEU PRO GLN VAL LEU ASP ASP SEQRES 11 G 153 TYR ASP ALA LEU ALA TRP LYS SER CYS LEU LYS GLY ILE SEQRES 12 G 153 LEU THR LYS ILE SER SER ARG LEU ASN ALA SEQRES 1 H 140 GLU CYS LEU VAL THR GLU SER LEU LYS VAL LYS LEU GLN SEQRES 2 H 140 TRP ALA SER ALA PHE GLY HIS ALA HIS GLU ARG VAL ALA SEQRES 3 H 140 PHE GLY LEU GLU LEU TRP ARG ASP ILE ILE ASP ASP HIS SEQRES 4 H 140 PRO GLU ILE LYS ALA PRO PHE SER ARG VAL ARG GLY ASP SEQRES 5 H 140 ASN ILE TYR SER PRO GLU PHE GLY ALA HIS SER GLN ARG SEQRES 6 H 140 VAL LEU SER GLY LEU ASP ILE THR ILE SER MET LEU ASP SEQRES 7 H 140 THR PRO ASP MET LEU ALA ALA GLN LEU ALA HIS LEU LYS SEQRES 8 H 140 VAL GLN HIS VAL GLU ARG ASN LEU LYS PRO GLU PHE PHE SEQRES 9 H 140 ASP ILE PHE LEU LYS HIS LEU LEU HIS VAL LEU GLY ASP SEQRES 10 H 140 ARG LEU GLY THR HIS PHE ASP PHE GLY ALA TRP HIS ASP SEQRES 11 H 140 CYS VAL ASP GLN ILE ILE ASP GLY ILE LYS SEQRES 1 I 151 ALA ASP ASP GLU ASP CYS CYS SER TYR GLU ASP ARG ARG SEQRES 2 I 151 GLU ILE ARG HIS ILE TRP ASP ASP VAL TRP SER SER SER SEQRES 3 I 151 PHE THR ASP ARG ARG VAL ALA ILE VAL ARG ALA VAL PHE SEQRES 4 I 151 ASP ASP LEU PHE LYS HIS TYR PRO THR SER LYS ALA LEU SEQRES 5 I 151 PHE GLU ARG VAL LYS ILE ASP GLU PRO GLU SER GLY GLU SEQRES 6 I 151 PHE LYS SER HIS LEU VAL ARG VAL ALA ASN GLY LEU LYS SEQRES 7 I 151 LEU LEU ILE ASN LEU LEU ASP ASP THR LEU VAL LEU GLN SEQRES 8 I 151 SER HIS LEU GLY HIS LEU ALA ASP GLN HIS ILE GLN ARG SEQRES 9 I 151 LYS GLY VAL THR LYS GLU TYR PHE ARG GLY ILE GLY GLU SEQRES 10 I 151 ALA PHE ALA ARG VAL LEU PRO GLN VAL LEU SER CYS PHE SEQRES 11 I 151 ASN VAL ASP ALA TRP ASN ARG CYS PHE HIS ARG LEU VAL SEQRES 12 I 151 ALA ARG ILE ALA LYS ASP LEU PRO SEQRES 1 J 145 LYS LYS GLN CYS GLY VAL LEU GLU GLY LEU LYS VAL LYS SEQRES 2 J 145 SER GLU TRP GLY ARG ALA TYR GLY SER GLY HIS ASP ARG SEQRES 3 J 145 GLU ALA PHE SER GLN ALA ILE TRP ARG ALA THR PHE ALA SEQRES 4 J 145 GLN VAL PRO GLU SER ARG SER LEU PHE LYS ARG VAL HIS SEQRES 5 J 145 GLY ASP ASP THR SER HIS PRO ALA PHE ILE ALA HIS ALA SEQRES 6 J 145 ASP ARG VAL LEU GLY GLY LEU ASP ILE ALA ILE SER THR SEQRES 7 J 145 LEU ASP GLN PRO ALA THR LEU LYS GLU GLU LEU ASP HIS SEQRES 8 J 145 LEU GLN VAL GLN HIS GLU GLY ARG LYS ILE PRO ASP ASN SEQRES 9 J 145 TYR PHE ASP ALA PHE LYS THR ALA ILE LEU HIS VAL VAL SEQRES 10 J 145 ALA ALA GLN LEU GLY ARG CYS TYR ASP ARG GLU ALA TRP SEQRES 11 J 145 ASP ALA CYS ILE ASP HIS ILE GLU ASP GLY ILE LYS GLY SEQRES 12 J 145 HIS HIS SEQRES 1 K 153 ASP GLU HIS GLU HIS CYS CYS SER GLU GLU ASP HIS ARG SEQRES 2 K 153 ILE VAL GLN LYS GLN TRP ASP ILE LEU TRP ARG ASP THR SEQRES 3 K 153 GLU SER SER LYS ILE LYS ILE GLY PHE GLY ARG LEU LEU SEQRES 4 K 153 LEU THR LYS LEU ALA LYS ASP ILE PRO GLU VAL ASN ASP SEQRES 5 K 153 LEU PHE LYS ARG VAL ASP ILE GLU HIS ALA GLU GLY PRO SEQRES 6 K 153 LYS PHE SER ALA HIS ALA LEU ARG ILE LEU ASN GLY LEU SEQRES 7 K 153 ASP LEU ALA ILE ASN LEU LEU ASP ASP PRO PRO ALA LEU SEQRES 8 K 153 ASP ALA ALA LEU ASP HIS LEU ALA HIS GLN HIS GLU VAL SEQRES 9 K 153 ARG GLU GLY VAL GLN LYS ALA HIS PHE LYS LYS PHE GLY SEQRES 10 K 153 GLU ILE LEU ALA THR GLY LEU PRO GLN VAL LEU ASP ASP SEQRES 11 K 153 TYR ASP ALA LEU ALA TRP LYS SER CYS LEU LYS GLY ILE SEQRES 12 K 153 LEU THR LYS ILE SER SER ARG LEU ASN ALA SEQRES 1 L 140 GLU CYS LEU VAL THR GLU SER LEU LYS VAL LYS LEU GLN SEQRES 2 L 140 TRP ALA SER ALA PHE GLY HIS ALA HIS GLU ARG VAL ALA SEQRES 3 L 140 PHE GLY LEU GLU LEU TRP ARG ASP ILE ILE ASP ASP HIS SEQRES 4 L 140 PRO GLU ILE LYS ALA PRO PHE SER ARG VAL ARG GLY ASP SEQRES 5 L 140 ASN ILE TYR SER PRO GLU PHE GLY ALA HIS SER GLN ARG SEQRES 6 L 140 VAL LEU SER GLY LEU ASP ILE THR ILE SER MET LEU ASP SEQRES 7 L 140 THR PRO ASP MET LEU ALA ALA GLN LEU ALA HIS LEU LYS SEQRES 8 L 140 VAL GLN HIS VAL GLU ARG ASN LEU LYS PRO GLU PHE PHE SEQRES 9 L 140 ASP ILE PHE LEU LYS HIS LEU LEU HIS VAL LEU GLY ASP SEQRES 10 L 140 ARG LEU GLY THR HIS PHE ASP PHE GLY ALA TRP HIS ASP SEQRES 11 L 140 CYS VAL ASP GLN ILE ILE ASP GLY ILE LYS SEQRES 1 M 217 ARG PHE GLN TYR LEU VAL LYS ASN GLN ASN LEU HIS ILE SEQRES 2 M 217 ASP TYR LEU ALA LYS LYS LEU HIS ASP ILE GLU GLU GLU SEQRES 3 M 217 TYR ASN LYS LEU THR HIS ASP VAL ASP LYS LYS THR ILE SEQRES 4 M 217 ARG GLN LEU LYS ALA ARG ILE SER ASN LEU GLU GLU HIS SEQRES 5 M 217 HIS CYS ASP GLU HIS GLU SER GLU CYS ARG GLY ASP VAL SEQRES 6 M 217 PRO GLU CYS ILE HIS ASP LEU LEU PHE CYS ASP GLY GLU SEQRES 7 M 217 LYS ASP CYS ARG ASP GLY SER ASP GLU ASP PRO GLU THR SEQRES 8 M 217 CYS SER LEU ASN ILE THR HIS VAL GLY SER SER TYR THR SEQRES 9 M 217 GLY LEU ALA THR TRP THR SER CYS GLU ASP LEU ASN PRO SEQRES 10 M 217 ASP HIS ALA ILE VAL THR ILE THR ALA ALA HIS ARG LYS SEQRES 11 M 217 SER PHE PHE PRO ASN ARG VAL TRP LEU ARG ALA THR LEU SEQRES 12 M 217 SER TYR GLU LEU ASP GLU HIS ASP HIS THR VAL SER THR SEQRES 13 M 217 THR GLN LEU ARG GLY PHE TYR ASN PHE GLY LYS ARG GLU SEQRES 14 M 217 LEU LEU LEU ALA PRO LEU LYS GLY GLN SER GLU GLY TYR SEQRES 15 M 217 GLY VAL ILE CYS ASP PHE ASN LEU GLY ASP ASP ASP HIS SEQRES 16 M 217 ALA ASP CYS LYS ILE VAL VAL PRO SER SER LEU PHE VAL SEQRES 17 M 217 CYS ALA HIS PHE ASN ALA GLN ARG TYR SEQRES 1 N 220 LEU ASP PRO ARG LEU GLY ALA ASN ALA PHE LEU ILE ILE SEQRES 2 N 220 ARG LEU ASP ARG ILE ILE GLU LYS LEU ARG THR LYS LEU SEQRES 3 N 220 ASP GLU ALA GLU LYS ILE ASP PRO GLU HIS PHE VAL SER SEQRES 4 N 220 GLU ILE ASP ALA ARG VAL THR LYS ILE GLU GLY THR HIS SEQRES 5 N 220 CYS GLU LYS ARG THR PHE GLN CYS GLY GLY ASN GLU GLN SEQRES 6 N 220 GLU CYS ILE SER ASP LEU LEU VAL CYS ASP GLY HIS LYS SEQRES 7 N 220 ASP CYS HIS ASN ALA HIS ASP GLU ASP PRO ASP VAL CYS SEQRES 8 N 220 ASP THR SER VAL VAL LYS ALA GLY ASN VAL PHE SER GLY SEQRES 9 N 220 THR SER THR TRP HIS GLY CYS LEU ALA ARG GLU ASP HIS SEQRES 10 N 220 VAL THR ARG ILE THR ILE THR ALA SER LYS ARG ARG LYS SEQRES 11 N 220 PHE PHE THR ALA ARG ILE TRP LEU ARG ALA LEU VAL GLU SEQRES 12 N 220 SER GLU LEU GLU ARG HIS GLY GLU ASN VAL THR SER SER SEQRES 13 N 220 PHE ASN ALA LYS GLY TYR TYR ASN PHE ALA SER ARG ARG SEQRES 14 N 220 LEU ILE LEU LEU PRO THR ASP ASP HIS ASP ASP HIS LEU SEQRES 15 N 220 ALA VAL VAL CYS SER PHE ASN ARG GLY ASP ASN GLU ARG SEQRES 16 N 220 ALA GLU CYS HIS ARG VAL THR GLU ALA THR LEU HIS GLN SEQRES 17 N 220 CYS ALA ASP LEU PHE VAL THR LEU GLU GLU HIS ASP SEQRES 1 O 215 GLN SER HIS ASP GLU ILE ILE ASP LYS LEU ILE GLU ARG SEQRES 2 O 215 THR ASN LYS ILE THR THR SER ILE SER HIS VAL GLU SER SEQRES 3 O 215 LEU LEU ASP ASP ARG LEU ASP PRO LYS ARG ILE ARG LYS SEQRES 4 O 215 ALA GLY SER LEU ARG HIS ARG VAL GLU GLU LEU GLU ASP SEQRES 5 O 215 PRO SER CYS ASP GLU HIS GLU HIS GLN CYS GLY GLY ASP SEQRES 6 O 215 ASP PRO GLN CYS ILE SER LYS LEU PHE VAL CYS ASP GLY SEQRES 7 O 215 HIS ASN ASP CYS ARG ASN GLY GLU ASP GLU LYS ASP CYS SEQRES 8 O 215 THR LEU PRO THR LYS ALA GLY ASP LYS PHE ILE GLY ASP SEQRES 9 O 215 VAL CYS PHE ASP HIS CYS THR LYS ARG ARG PRO GLU HIS SEQRES 10 O 215 MET THR LEU ALA PHE GLU SER SER SER ILE ALA ALA PHE SEQRES 11 O 215 PHE THR PRO ILE ALA ASP LEU HIS VAL HIS ILE GLU ILE SEQRES 12 O 215 GLU SER GLU THR ASP GLU ASP GLU SER GLU VAL SER MET SEQRES 13 O 215 PRO ALA ASP GLY GLU TYR SER PHE ALA ASP HIS ARG LEU SEQRES 14 O 215 THR ILE HIS PRO PRO GLU GLU ASP GLY LEU GLY LEU VAL SEQRES 15 O 215 GLY GLU PHE ASP GLY TYR ASN PHE ASP ARG PHE VAL GLY SEQRES 16 O 215 HIS ILE VAL HIS GLU LEU SER GLU GLU VAL CYS ALA GLU SEQRES 17 O 215 PHE ILE PHE HIS ARG LYS LYS HET CA M 250 1 HET CA M 251 1 HET ZN M 252 1 HET CA N 250 1 HET CA O 250 1 HET CMO A 161 2 HET CMO B 161 2 HET CMO C 161 2 HET CMO D 161 2 HET CMO E 161 2 HET CMO F 161 2 HET CMO G 161 2 HET CMO H 161 2 HET CMO I 161 2 HET CMO J 161 2 HET CMO K 161 2 HET CMO L 161 2 HET HEM A 160 43 HET HEM B 160 43 HET HEM C 160 43 HET HEM D 160 43 HET HEM E 160 43 HET HEM F 160 43 HET HEM G 160 43 HET HEM H 160 43 HET HEM I 160 43 HET HEM J 160 43 HET HEM K 160 43 HET HEM L 160 43 HETNAM CA CALCIUM ION HETNAM ZN ZINC ION HETNAM CMO CARBON MONOXIDE HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 16 CA 4(CA 2+) FORMUL 18 ZN ZN 2+ FORMUL 21 CMO 12(C O) FORMUL 33 HEM 12(C34 H32 FE N4 O4) HELIX 1 1 SER A 8 TRP A 23 1 16 HELIX 2 2 PHE A 27 TYR A 46 1 20 HELIX 3 3 PRO A 47 LYS A 57 5 11 HELIX 4 4 GLY A 64 ASN A 82 1 19 HELIX 5 5 ASP A 86 GLN A 103 1 18 HELIX 6 6 THR A 108 LEU A 127 1 20 HELIX 7 7 ASN A 131 ALA A 147 1 17 HELIX 8 8 VAL B 6 GLY B 21 1 16 HELIX 9 9 SER B 22 VAL B 41 1 20 HELIX 10 10 PRO B 42 HIS B 52 5 11 HELIX 11 11 HIS B 58 SER B 77 1 20 HELIX 12 12 GLN B 81 GLU B 97 1 17 HELIX 13 13 PRO B 102 GLY B 122 1 21 HELIX 14 14 ASP B 126 GLY B 143 1 18 HELIX 15 15 SER C 8 ILE C 21 1 14 HELIX 16 16 LEU C 22 ASP C 25 5 4 HELIX 17 17 GLU C 27 ILE C 47 1 21 HELIX 18 18 PRO C 48 ASN C 51 5 4 HELIX 19 19 LEU C 53 ASP C 58 5 6 HELIX 20 20 GLY C 64 LEU C 84 1 21 HELIX 21 21 ASP C 87 VAL C 104 1 18 HELIX 22 22 GLN C 109 LEU C 128 1 20 HELIX 23 23 ASP C 132 SER C 149 1 18 HELIX 24 24 VAL D 11 GLY D 26 1 16 HELIX 25 25 ALA D 28 HIS D 46 1 19 HELIX 26 26 PRO D 47 ARG D 55 5 9 HELIX 27 27 SER D 63 SER D 82 1 20 HELIX 28 28 THR D 86 GLU D 103 1 18 HELIX 29 29 PRO D 108 GLY D 127 1 20 HELIX 30 30 ASP D 131 GLY D 145 1 15 HELIX 31 31 SER E 8 TRP E 23 1 16 HELIX 32 32 PHE E 27 TYR E 46 1 20 HELIX 33 33 PRO E 47 LYS E 57 5 11 HELIX 34 34 GLY E 64 ASN E 82 1 19 HELIX 35 35 ASP E 86 GLN E 103 1 18 HELIX 36 36 THR E 108 LEU E 127 1 20 HELIX 37 37 ASN E 131 ALA E 147 1 17 HELIX 38 38 VAL F 6 GLY F 21 1 16 HELIX 39 39 SER F 22 VAL F 41 1 20 HELIX 40 40 PRO F 42 HIS F 52 5 11 HELIX 41 41 HIS F 58 SER F 77 1 20 HELIX 42 42 GLN F 81 GLU F 97 1 17 HELIX 43 43 PRO F 102 GLY F 122 1 21 HELIX 44 44 ASP F 126 GLY F 143 1 18 HELIX 45 45 SER G 8 ILE G 21 1 14 HELIX 46 46 LEU G 22 ASP G 25 5 4 HELIX 47 47 GLU G 27 ILE G 47 1 21 HELIX 48 48 PRO G 48 ASN G 51 5 4 HELIX 49 49 LEU G 53 ASP G 58 5 6 HELIX 50 50 GLY G 64 LEU G 84 1 21 HELIX 51 51 ASP G 87 VAL G 104 1 18 HELIX 52 52 GLN G 109 LEU G 128 1 20 HELIX 53 53 ASP G 132 SER G 149 1 18 HELIX 54 54 VAL H 11 GLY H 26 1 16 HELIX 55 55 ALA H 28 HIS H 46 1 19 HELIX 56 56 PRO H 47 ARG H 55 5 9 HELIX 57 57 SER H 63 SER H 82 1 20 HELIX 58 58 THR H 86 GLU H 103 1 18 HELIX 59 59 PRO H 108 GLY H 127 1 20 HELIX 60 60 ASP H 131 GLY H 145 1 15 HELIX 61 61 SER I 8 TRP I 23 1 16 HELIX 62 62 PHE I 27 TYR I 46 1 20 HELIX 63 63 PRO I 47 LYS I 57 5 11 HELIX 64 64 GLY I 64 ASN I 82 1 19 HELIX 65 65 ASP I 86 GLN I 103 1 18 HELIX 66 66 THR I 108 LEU I 127 1 20 HELIX 67 67 ASN I 131 ALA I 147 1 17 HELIX 68 68 VAL J 6 GLY J 21 1 16 HELIX 69 69 SER J 22 VAL J 41 1 20 HELIX 70 70 PRO J 42 HIS J 52 5 11 HELIX 71 71 HIS J 58 SER J 77 1 20 HELIX 72 72 GLN J 81 GLU J 97 1 17 HELIX 73 73 PRO J 102 GLY J 122 1 21 HELIX 74 74 ASP J 126 GLY J 143 1 18 HELIX 75 75 SER K 8 ILE K 21 1 14 HELIX 76 76 LEU K 22 ASP K 25 5 4 HELIX 77 77 GLU K 27 ILE K 47 1 21 HELIX 78 78 PRO K 48 ASN K 51 5 4 HELIX 79 79 LEU K 53 ASP K 58 5 6 HELIX 80 80 GLY K 64 LEU K 84 1 21 HELIX 81 81 ASP K 87 VAL K 104 1 18 HELIX 82 82 GLN K 109 LEU K 128 1 20 HELIX 83 83 ASP K 132 SER K 149 1 18 HELIX 84 84 VAL L 11 GLY L 26 1 16 HELIX 85 85 ALA L 28 HIS L 46 1 19 HELIX 86 86 PRO L 47 ARG L 55 5 9 HELIX 87 87 SER L 63 SER L 82 1 20 HELIX 88 88 THR L 86 GLU L 103 1 18 HELIX 89 89 PRO L 108 GLY L 127 1 20 HELIX 90 90 ASP L 131 GLY L 145 1 15 HELIX 91 91 LEU M 13 LYS M 37 1 25 HELIX 92 92 ASP M 43 ASN M 56 1 14 HELIX 93 93 LEU M 80 PHE M 82 5 3 HELIX 94 94 ASP M 96 SER M 101 1 6 HELIX 95 95 LEU M 102 HIS M 106 5 5 HELIX 96 96 LEU N 10 ILE N 41 1 32 HELIX 97 97 ASP N 42 GLY N 59 1 18 HELIX 98 98 ASP N 96 LYS N 106 5 11 HELIX 99 99 ILE O 18 ASP O 40 1 23 HELIX 100 100 ASP O 40 GLU O 58 1 19 HELIX 101 101 LEU O 80 VAL O 82 5 3 HELIX 102 102 GLY O 92 ASP O 97 1 6 SHEET 1 A 2 GLU M 66 GLU M 68 0 SHEET 2 A 2 CYS M 76 HIS M 78 -1 O ILE M 77 N SER M 67 SHEET 1 B 9 SER M 110 TRP M 117 0 SHEET 2 B 9 ASP M 126 ALA M 135 -1 O VAL M 130 N TYR M 111 SHEET 3 B 9 LEU M 147 GLU M 154 -1 O ARG M 148 N ALA M 134 SHEET 4 B 9 VAL M 162 ASN M 172 -1 O GLY M 169 N LEU M 147 SHEET 5 B 9 GLU M 177 PRO M 182 -1 O ALA M 181 N ARG M 168 SHEET 6 B 9 VAL M 192 ASP M 195 -1 O CYS M 194 N LEU M 178 SHEET 7 B 9 HIS M 203 VAL M 210 -1 O ASP M 205 N ASP M 195 SHEET 8 B 9 PHE M 215 ARG M 224 -1 O PHE M 220 N CYS M 206 SHEET 9 B 9 SER M 110 TRP M 117 -1 N THR M 112 O GLN M 223 SHEET 1 C 2 THR N 66 GLN N 68 0 SHEET 2 C 2 CYS N 76 SER N 78 -1 O ILE N 77 N PHE N 67 SHEET 1 D 9 VAL N 110 TRP N 117 0 SHEET 2 D 9 HIS N 126 LYS N 136 -1 O ILE N 130 N PHE N 111 SHEET 3 D 9 ILE N 145 GLU N 152 -1 O LEU N 150 N THR N 131 SHEET 4 D 9 PHE N 166 ASN N 173 -1 O ALA N 168 N ALA N 149 SHEET 5 D 9 ARG N 178 PRO N 183 -1 O LEU N 182 N LYS N 169 SHEET 6 D 9 ALA N 192 SER N 196 -1 O CYS N 195 N LEU N 179 SHEET 7 D 9 ARG N 204 VAL N 210 -1 O VAL N 210 N ALA N 192 SHEET 8 D 9 GLN N 217 LEU N 225 -1 O LEU N 221 N CYS N 207 SHEET 9 D 9 VAL N 110 TRP N 117 -1 N THR N 116 O ASP N 220 SHEET 1 E 2 GLU N 154 GLU N 156 0 SHEET 2 E 2 ASN N 161 THR N 163 -1 O VAL N 162 N LEU N 155 SHEET 1 F 2 GLU O 66 GLN O 68 0 SHEET 2 F 2 CYS O 76 SER O 78 -1 O ILE O 77 N HIS O 67 SHEET 1 G 9 LYS O 107 ASP O 115 0 SHEET 2 G 9 HIS O 124 ILE O 134 -1 O LEU O 127 N PHE O 108 SHEET 3 G 9 ILE O 141 GLU O 151 -1 O HIS O 147 N ALA O 128 SHEET 4 G 9 GLU O 160 SER O 170 -1 O GLY O 167 N LEU O 144 SHEET 5 G 9 ARG O 175 ILE O 178 -1 O THR O 177 N GLU O 168 SHEET 6 G 9 LEU O 186 PHE O 192 -1 O LEU O 188 N ILE O 178 SHEET 7 G 9 ARG O 199 HIS O 206 -1 O VAL O 205 N GLY O 187 SHEET 8 G 9 GLU O 211 ARG O 220 -1 O PHE O 216 N GLY O 202 SHEET 9 G 9 LYS O 107 ASP O 115 -1 N ILE O 109 O HIS O 219 SSBOND 1 CYS A 6 CYS G 6 SSBOND 2 CYS A 7 CYS A 138 SSBOND 3 CYS A 129 CYS B 124 SSBOND 4 CYS B 4 CYS B 133 SSBOND 5 CYS C 6 CYS I 6 SSBOND 6 CYS C 7 CYS C 139 SSBOND 7 CYS D 9 CYS D 138 SSBOND 8 CYS E 6 CYS K 6 SSBOND 9 CYS E 7 CYS E 138 SSBOND 10 CYS E 129 CYS F 124 SSBOND 11 CYS F 4 CYS F 133 SSBOND 12 CYS G 7 CYS G 139 SSBOND 13 CYS H 9 CYS H 138 SSBOND 14 CYS I 7 CYS I 138 SSBOND 15 CYS I 129 CYS J 124 SSBOND 16 CYS J 4 CYS J 133 SSBOND 17 CYS K 7 CYS K 139 SSBOND 18 CYS L 9 CYS L 138 SSBOND 19 CYS M 62 CYS M 76 SSBOND 20 CYS M 69 CYS M 89 SSBOND 21 CYS M 83 CYS M 100 SSBOND 22 CYS M 120 CYS M 217 SSBOND 23 CYS M 194 CYS M 206 SSBOND 24 CYS N 62 CYS N 76 SSBOND 25 CYS N 69 CYS N 89 SSBOND 26 CYS N 83 CYS N 100 SSBOND 27 CYS N 120 CYS N 218 SSBOND 28 CYS N 195 CYS N 207 SSBOND 29 CYS O 62 CYS O 76 SSBOND 30 CYS O 69 CYS O 89 SSBOND 31 CYS O 83 CYS O 98 SSBOND 32 CYS O 117 CYS O 213 LINK C CMO B 161 FE HEM B 160 LINK C CMO K 161 FE HEM K 160 LINK C CMO D 161 FE HEM D 160 LINK C CMO F 161 FE HEM F 160 LINK C CMO I 161 FE HEM I 160 LINK C CMO J 161 FE HEM J 160 LINK C CMO A 161 FE HEM A 160 LINK C CMO C 161 FE HEM C 160 LINK C CMO G 161 FE HEM G 160 LINK C CMO E 161 FE HEM E 160 LINK C CMO H 161 FE HEM H 160 LINK C CMO L 161 FE HEM L 160 LINK NE2 HIS E 101 FE HEM E 160 LINK NE2 HIS F 96 FE HEM F 160 LINK NE2 HIS A 101 FE HEM A 160 LINK NE2 HIS J 96 FE HEM J 160 LINK NE2 HIS C 102 FE HEM C 160 LINK NE2 HIS I 101 FE HEM I 160 LINK NE2 HIS B 96 FE HEM B 160 LINK NE2 HIS G 102 FE HEM G 160 LINK NE2 HIS H 101 FE HEM H 160 LINK NE2 HIS L 101 FE HEM L 160 LINK NE2 HIS K 102 FE HEM K 160 LINK NE2 HIS D 101 FE HEM D 160 CRYST1 176.080 257.960 436.530 89.69 97.15 90.98 P 1 3 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 0.005679 0.000097 0.000712 0.00000 SCALE2 0.000000 0.003877 -0.000013 0.00000 SCALE3 0.000000 0.000000 0.002309 0.00000 MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1 MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1 MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1 MTRIX1 2 0.990230 -0.051970 -0.129410 -1.65217 MTRIX2 2 0.137880 0.504220 0.852490 -0.21834 MTRIX3 2 0.020950 -0.862010 0.506460 -1.62163 MTRIX1 3 0.963260 0.030470 -0.266820 -0.97235 MTRIX2 3 0.247390 -0.487280 0.837470 -2.11336 MTRIX3 3 -0.104500 -0.872710 -0.476920 -1.50619 MTRIX1 4 0.945090 0.214330 -0.246730 -2.21643 MTRIX2 4 0.211220 -0.976650 -0.039310 -2.89465 MTRIX3 4 -0.249390 -0.014960 -0.968290 -0.66088 MTRIX1 5 0.963570 0.246890 -0.102820 0.75781 MTRIX2 5 0.036020 -0.500740 -0.864850 -0.56749 MTRIX3 5 -0.265010 0.829640 -0.491390 2.44098 MTRIX1 6 0.990150 0.139970 0.003390 1.48809 MTRIX2 6 -0.067810 0.500600 -0.863020 -0.05652 MTRIX3 6 -0.122500 0.854290 0.505160 0.63077 MTRIX1 7 -0.949570 -0.104980 0.295450 -1.00599 MTRIX2 7 -0.119090 -0.750910 -0.649580 -2.30478 MTRIX3 7 0.290050 -0.652000 0.700540 -0.37744 MTRIX1 8 -0.955290 -0.235650 0.178560 -0.78939 MTRIX2 8 -0.222310 0.174340 -0.959260 0.48797 MTRIX3 8 0.194920 -0.956070 -0.218930 -1.11833 MTRIX1 9 -0.976960 -0.208330 0.046430 -2.34257 MTRIX2 9 -0.212390 0.927330 -0.308150 1.94545 MTRIX3 9 0.021140 -0.310920 -0.950200 0.94172 MTRIX1 10 -0.997140 -0.072000 -0.023070 -1.67681 MTRIX2 10 -0.068840 0.738310 0.670940 -0.16198 MTRIX3 10 -0.031270 0.670600 -0.741160 2.09542 MTRIX1 11 -0.997700 0.048610 0.047180 0.09390 MTRIX2 11 0.036460 -0.201680 0.978770 -1.78915 MTRIX3 11 0.057100 0.978240 0.199450 2.07663 MTRIX1 12 -0.975570 0.048950 0.214190 -0.87521 MTRIX2 12 0.023210 -0.946450 0.322000 -3.00517 MTRIX3 12 0.218480 0.319110 0.922190 0.40173 MTRIX1 13 0.989520 0.143950 0.011550 63.79785 MTRIX2 13 -0.144290 0.988780 0.038530 132.83920 MTRIX3 13 -0.005870 -0.039790 0.999190 216.14185 MTRIX1 14 0.999920 -0.006660 0.010720 61.71643 MTRIX2 14 -0.006120 0.487630 0.873030 131.91033 MTRIX3 14 -0.011040 -0.873020 0.487550 214.26940 MTRIX1 15 0.983490 -0.083540 -0.160510 61.33404 MTRIX2 15 0.097160 -0.504510 0.857920 130.41609 MTRIX3 15 -0.152650 -0.859350 -0.488070 214.56740 MTRIX1 16 0.957550 0.059020 -0.282160 57.77668 MTRIX2 16 0.057210 -0.998250 -0.014660 130.23473 MTRIX3 16 -0.282530 -0.002100 -0.959260 216.24950 MTRIX1 17 0.943420 0.229250 -0.239590 58.87162 MTRIX2 17 -0.097330 -0.499240 -0.860980 131.28099 MTRIX3 17 -0.316990 0.835580 -0.448680 218.29621 MTRIX1 18 0.963210 0.251830 -0.093830 63.17867 MTRIX2 18 -0.212130 0.498100 -0.840770 132.75960 MTRIX3 18 -0.164990 0.829750 0.533200 216.58716 MTRIX1 19 -0.947240 -0.239450 0.213060 59.05420 MTRIX2 19 0.039290 -0.746470 -0.664260 130.57020 MTRIX3 19 0.318100 -0.620840 0.716500 215.35065 MTRIX1 20 -0.977410 -0.206500 0.044950 57.47877 MTRIX2 20 -0.082790 0.178430 -0.980460 133.24688 MTRIX3 20 0.194450 -0.962040 -0.191500 215.86870 MTRIX1 21 -0.997500 -0.064910 -0.027860 59.69155 MTRIX2 21 -0.052120 0.942570 -0.329910 133.26482 MTRIX3 21 0.047680 -0.327630 -0.943600 216.46762 MTRIX1 22 -0.998030 0.047680 0.040790 62.93848 MTRIX2 22 0.062750 0.763820 0.642380 132.24233 MTRIX3 22 -0.000530 0.643670 -0.765300 217.88860 MTRIX1 23 -0.976610 0.058940 0.206780 62.01574 MTRIX2 23 0.194080 -0.172330 0.965730 129.82776 MTRIX3 23 0.092560 0.983270 0.156860 218.08703 MTRIX1 24 -0.946710 -0.095320 0.307670 60.90111 MTRIX2 24 0.193440 -0.932020 0.306470 128.81950 MTRIX3 24 0.257540 0.349650 0.900790 216.69973