HEADER LYASE/OXIDOREDUCTASE 14-MAR-13 4JN6
TITLE CRYSTAL STRUCTURE OF THE ALDOLASE-DEHYDROGENASE COMPLEX FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS HRV37
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-HYDROXY-2-OXOVALERATE ALDOLASE;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: HOA, 4-HYDROXY-2-KETO-PENTANOIC ACID ALDOLASE, 4-HYDROXY-2-
COMPND 5 OXOPENTANOATE ALDOLASE;
COMPND 6 EC: 4.1.3.39;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ACETALDEHYDE DEHYDROGENASE;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: ACETALDEHYDE DEHYDROGENASE [ACETYLATING];
COMPND 12 EC: 1.2.1.10;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: HRV37;
SOURCE 5 GENE: RV3534C, MT3638;
SOURCE 6 EXPRESSION_SYSTEM: RHODOCOCCUS JOSTII;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 132919;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: RHA1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTIP-QC1-HIS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 13 ORGANISM_TAXID: 1773;
SOURCE 14 STRAIN: HRV37;
SOURCE 15 GENE: MHPF, RV3535C, MT3639;
SOURCE 16 EXPRESSION_SYSTEM: RHODOCOCCUS JOSTII;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 132919;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: RHA1;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PTIP-QC1-HIS
KEYWDS ROSSMANN FOLD, TIM BARREL, ALDOLASE-DEHYDROGENASE, LYASE-
KEYWDS 2 OXIDOREDUCTASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CARERE,S.E.MCKENNA,M.S.KIMBER,S.Y.K.SEAH
REVDAT 4 20-SEP-23 4JN6 1 REMARK SEQADV LINK
REVDAT 3 25-DEC-13 4JN6 1 JRNL
REVDAT 2 20-NOV-13 4JN6 1 JRNL
REVDAT 1 08-MAY-13 4JN6 0
JRNL AUTH J.CARERE,S.E.MCKENNA,M.S.KIMBER,S.Y.SEAH
JRNL TITL CHARACTERIZATION OF AN ALDOLASE-DEHYDROGENASE COMPLEX FROM
JRNL TITL 2 THE CHOLESTEROL DEGRADATION PATHWAY OF MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS.
JRNL REF BIOCHEMISTRY V. 52 3502 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23614353
JRNL DOI 10.1021/BI400351H
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 105899
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5296
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 45.9017 - 5.9925 1.00 3496 185 0.1467 0.1674
REMARK 3 2 5.9925 - 4.7580 1.00 3451 181 0.1628 0.1845
REMARK 3 3 4.7580 - 4.1570 1.00 3410 180 0.1365 0.1548
REMARK 3 4 4.1570 - 3.7771 1.00 3415 179 0.1468 0.1660
REMARK 3 5 3.7771 - 3.5065 1.00 3427 181 0.1505 0.1846
REMARK 3 6 3.5065 - 3.2998 0.99 3388 178 0.1605 0.2165
REMARK 3 7 3.2998 - 3.1346 1.00 3438 181 0.1671 0.1892
REMARK 3 8 3.1346 - 2.9982 1.00 3404 179 0.1672 0.1955
REMARK 3 9 2.9982 - 2.8828 1.00 3411 180 0.1680 0.2154
REMARK 3 10 2.8828 - 2.7833 1.00 3421 180 0.1763 0.2250
REMARK 3 11 2.7833 - 2.6963 1.00 3373 177 0.1694 0.2335
REMARK 3 12 2.6963 - 2.6193 0.99 3399 179 0.1715 0.2099
REMARK 3 13 2.6193 - 2.5503 0.99 3357 177 0.1730 0.2354
REMARK 3 14 2.5503 - 2.4881 0.99 3356 177 0.1779 0.2288
REMARK 3 15 2.4881 - 2.4315 0.98 3387 178 0.1789 0.2263
REMARK 3 16 2.4315 - 2.3798 0.98 3379 178 0.1748 0.2361
REMARK 3 17 2.3798 - 2.3322 0.98 3302 174 0.1783 0.2124
REMARK 3 18 2.3322 - 2.2882 0.98 3383 178 0.1883 0.2473
REMARK 3 19 2.2882 - 2.2473 0.98 3319 175 0.1973 0.2404
REMARK 3 20 2.2473 - 2.2092 0.98 3304 174 0.2034 0.2286
REMARK 3 21 2.2092 - 2.1736 0.97 3331 175 0.2132 0.2644
REMARK 3 22 2.1736 - 2.1401 0.97 3315 175 0.2345 0.2969
REMARK 3 23 2.1401 - 2.1087 0.97 3279 172 0.2448 0.2726
REMARK 3 24 2.1087 - 2.0790 0.96 3280 173 0.2545 0.3038
REMARK 3 25 2.0790 - 2.0509 0.97 3293 173 0.2637 0.2906
REMARK 3 26 2.0509 - 2.0242 0.96 3288 173 0.2888 0.2849
REMARK 3 27 2.0242 - 1.9989 0.96 3238 171 0.3017 0.3324
REMARK 3 28 1.9989 - 1.9748 0.96 3257 171 0.3212 0.3234
REMARK 3 29 1.9748 - 1.9519 0.95 3282 173 0.3368 0.3446
REMARK 3 30 1.9519 - 1.9300 0.95 3220 169 0.3514 0.4057
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 9587
REMARK 3 ANGLE : 0.995 13025
REMARK 3 CHIRALITY : 0.069 1509
REMARK 3 PLANARITY : 0.005 1723
REMARK 3 DIHEDRAL : 13.155 3473
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN B AND ( RESID 3:124 OR RESID 280:298 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7148 48.4753 212.8593
REMARK 3 T TENSOR
REMARK 3 T11: 1.1523 T22: 0.5943
REMARK 3 T33: 0.6412 T12: 0.1329
REMARK 3 T13: -0.4024 T23: -0.0844
REMARK 3 L TENSOR
REMARK 3 L11: 6.6701 L22: 2.0283
REMARK 3 L33: 5.5088 L12: -0.8372
REMARK 3 L13: -0.3989 L23: -0.0916
REMARK 3 S TENSOR
REMARK 3 S11: 0.2621 S12: -0.8302 S13: -0.1413
REMARK 3 S21: 0.1612 S22: -0.0400 S23: 0.1764
REMARK 3 S31: -0.4557 S32: -0.5608 S33: -0.2223
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN D AND ( RESID 3:124 OR RESID 280:298 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8933 -57.7909 154.8679
REMARK 3 T TENSOR
REMARK 3 T11: 0.9854 T22: 0.3446
REMARK 3 T33: 0.7161 T12: 0.0693
REMARK 3 T13: -0.1814 T23: -0.0598
REMARK 3 L TENSOR
REMARK 3 L11: 3.6375 L22: 4.6877
REMARK 3 L33: 0.7430 L12: -0.5122
REMARK 3 L13: -0.9476 L23: 0.7155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0521 S12: -0.0656 S13: -1.0278
REMARK 3 S21: -0.0106 S22: 0.0330 S23: 0.1880
REMARK 3 S31: 1.1926 S32: 0.0440 S33: 0.0020
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN B AND RESID 125:279 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5340 35.9956 191.3277
REMARK 3 T TENSOR
REMARK 3 T11: 0.9745 T22: 0.3931
REMARK 3 T33: 0.5787 T12: 0.1687
REMARK 3 T13: -0.3508 T23: -0.1122
REMARK 3 L TENSOR
REMARK 3 L11: 1.0500 L22: 2.0361
REMARK 3 L33: 1.2085 L12: 0.3210
REMARK 3 L13: 0.3270 L23: 0.8553
REMARK 3 S TENSOR
REMARK 3 S11: -0.2156 S12: -0.1288 S13: 0.1666
REMARK 3 S21: 0.2344 S22: 0.1259 S23: -0.2793
REMARK 3 S31: -0.3812 S32: 0.0589 S33: 0.0875
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN D AND RESID 125:279 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3968 -32.1706 152.8724
REMARK 3 T TENSOR
REMARK 3 T11: 0.2490 T22: 0.2106
REMARK 3 T33: 0.2844 T12: 0.0630
REMARK 3 T13: -0.0546 T23: -0.0660
REMARK 3 L TENSOR
REMARK 3 L11: 2.1461 L22: 2.9689
REMARK 3 L33: 3.6753 L12: 0.8944
REMARK 3 L13: -0.4358 L23: -0.2649
REMARK 3 S TENSOR
REMARK 3 S11: -0.0460 S12: 0.1899 S13: -0.1860
REMARK 3 S21: -0.2019 S22: 0.0868 S23: 0.1771
REMARK 3 S31: 0.3339 S32: 0.0544 S33: -0.0371
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 4:341 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2589 11.7654 186.3969
REMARK 3 T TENSOR
REMARK 3 T11: 0.6228 T22: 0.3509
REMARK 3 T33: 0.4224 T12: 0.2073
REMARK 3 T13: -0.1451 T23: -0.0667
REMARK 3 L TENSOR
REMARK 3 L11: 0.8914 L22: 1.8915
REMARK 3 L33: 1.1157 L12: -0.1450
REMARK 3 L13: 0.2086 L23: 0.1210
REMARK 3 S TENSOR
REMARK 3 S11: -0.1875 S12: -0.1578 S13: 0.0211
REMARK 3 S21: 0.3704 S22: 0.1198 S23: 0.1151
REMARK 3 S31: -0.2363 S32: -0.1074 S33: 0.0530
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 4JN6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078256.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105918
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 45.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
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 <I/SIGMA(I)> 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: PHENIX
REMARK 200 STARTING MODEL: HOMOLOGY MODEL BASED ON 1NVM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 4000, 0.2 M MAGNESIUM
REMARK 280 CHLORIDE, 0.1 M TRIS, 10% GLYCEROL AND 10 MM SODIUM OXALATE, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 34.84500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.34500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.84500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 71.34500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 422 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 590 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 476 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 THR A 2
REMARK 465 ASP A 3
REMARK 465 ALA A 342
REMARK 465 ALA A 343
REMARK 465 VAL A 344
REMARK 465 THR A 345
REMARK 465 HIS A 346
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 VAL B 299
REMARK 465 GLY B 300
REMARK 465 GLY B 301
REMARK 465 ALA B 302
REMARK 465 ARG B 303
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ASP C 3
REMARK 465 ALA C 343
REMARK 465 VAL C 344
REMARK 465 THR C 345
REMARK 465 HIS C 346
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 PRO D 2
REMARK 465 VAL D 299
REMARK 465 GLY D 300
REMARK 465 GLY D 301
REMARK 465 ALA D 302
REMARK 465 ARG D 303
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 VAL C 265 O HOH C 565 1.89
REMARK 500 O HOH C 596 O HOH C 597 1.90
REMARK 500 O HOH C 613 O HOH C 617 1.99
REMARK 500 O HOH D 401 O HOH D 471 2.05
REMARK 500 O HOH A 542 O HOH A 549 2.08
REMARK 500 O HOH A 600 O HOH B 438 2.09
REMARK 500 OE1 GLU D 242 O HOH D 455 2.12
REMARK 500 O HOH C 601 O HOH C 602 2.12
REMARK 500 O ARG D 164 O HOH D 416 2.13
REMARK 500 O HOH A 589 O HOH A 593 2.13
REMARK 500 NE2 GLN A 122 O HOH A 576 2.15
REMARK 500 O HOH C 620 O HOH C 624 2.17
REMARK 500 O HOH C 626 O HOH C 627 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 O HOH D 448 O HOH D 448 2557 2.11
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 A 15 -70.06 -132.27
REMARK 500 VAL A 91 -67.15 -127.70
REMARK 500 LEU A 175 -89.49 57.45
REMARK 500 ARG A 227 -0.08 69.74
REMARK 500 PHE A 228 90.89 -38.43
REMARK 500 THR B 76 -96.77 -107.33
REMARK 500 ALA B 111 -64.16 -106.23
REMARK 500 ILE B 125 -119.53 47.61
REMARK 500 ASP B 269 -84.21 -77.59
REMARK 500 ALA B 275 44.54 -89.08
REMARK 500 LEU B 297 -82.43 -98.33
REMARK 500 ARG C 15 -70.87 -132.81
REMARK 500 VAL C 91 -64.44 -122.18
REMARK 500 LEU C 175 -90.06 49.40
REMARK 500 PHE C 228 97.42 -43.92
REMARK 500 GLN C 323 30.95 -99.43
REMARK 500 THR D 76 -92.88 -114.91
REMARK 500 ILE D 125 -127.98 43.52
REMARK 500 TYR D 270 -47.18 -132.27
REMARK 500 ALA D 275 45.20 -104.50
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 MN A 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 16 OD1
REMARK 620 2 HIS A 198 NE2 78.0
REMARK 620 3 HIS A 200 NE2 90.1 106.7
REMARK 620 4 OXL A 401 O1 168.3 101.5 101.1
REMARK 620 5 OXL A 401 O2 93.1 104.1 149.0 75.6
REMARK 620 6 HOH A 578 O 89.2 163.6 83.3 88.9 65.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 403 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 16 OD2
REMARK 620 2 HIS C 198 NE2 88.2
REMARK 620 3 HIS C 200 NE2 94.8 101.3
REMARK 620 4 OXL C 401 O4 164.7 98.5 97.3
REMARK 620 5 OXL C 401 O1 87.8 100.8 157.8 77.5
REMARK 620 6 HOH C 540 O 85.7 171.0 85.8 86.0 72.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 512 O
REMARK 620 2 HOH C 515 O 135.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 403
DBREF 4JN6 A 1 346 UNP P71867 HOA_MYCTU 1 346
DBREF 4JN6 B 1 303 UNP P71866 ACDH_MYCTU 1 303
DBREF 4JN6 C 1 346 UNP P71867 HOA_MYCTU 1 346
DBREF 4JN6 D 1 303 UNP P71866 ACDH_MYCTU 1 303
SEQADV 4JN6 GLY B -2 UNP P71866 EXPRESSION TAG
SEQADV 4JN6 SER B -1 UNP P71866 EXPRESSION TAG
SEQADV 4JN6 HIS B 0 UNP P71866 EXPRESSION TAG
SEQADV 4JN6 GLY D -2 UNP P71866 EXPRESSION TAG
SEQADV 4JN6 SER D -1 UNP P71866 EXPRESSION TAG
SEQADV 4JN6 HIS D 0 UNP P71866 EXPRESSION TAG
SEQRES 1 A 346 MET THR ASP MET TRP ASP VAL ARG ILE THR ASP THR SER
SEQRES 2 A 346 LEU ARG ASP GLY SER HIS HIS LYS ARG HIS GLN PHE THR
SEQRES 3 A 346 LYS ASP GLU VAL GLY ALA ILE VAL ALA ALA LEU ASP ALA
SEQRES 4 A 346 ALA GLY VAL PRO VAL ILE GLU VAL THR HIS GLY ASP GLY
SEQRES 5 A 346 LEU GLY GLY SER SER PHE ASN TYR GLY PHE SER LYS THR
SEQRES 6 A 346 PRO GLU GLN GLU LEU ILE LYS LEU ALA ALA ALA THR ALA
SEQRES 7 A 346 LYS GLU ALA ARG ILE ALA PHE LEU MET LEU PRO GLY VAL
SEQRES 8 A 346 GLY THR LYS ASP ASP ILE LYS GLU ALA ARG ASP ASN GLY
SEQRES 9 A 346 GLY SER ILE CYS ARG ILE ALA THR HIS CYS THR GLU ALA
SEQRES 10 A 346 ASP VAL SER ILE GLN HIS PHE GLY LEU ALA ARG GLU LEU
SEQRES 11 A 346 GLY LEU GLU THR VAL GLY PHE LEU MET MET ALA HIS THR
SEQRES 12 A 346 ILE ALA PRO GLU LYS LEU ALA ALA GLN ALA ARG ILE MET
SEQRES 13 A 346 ALA ASP ALA GLY CYS GLN CYS VAL TYR VAL VAL ASP SER
SEQRES 14 A 346 ALA GLY ALA LEU VAL LEU ASP GLY VAL ALA ASP ARG VAL
SEQRES 15 A 346 SER ALA LEU VAL ALA GLU LEU GLY GLU ASP ALA GLN VAL
SEQRES 16 A 346 GLY PHE HIS GLY HIS GLU ASN LEU GLY LEU GLY VAL ALA
SEQRES 17 A 346 ASN SER VAL ALA ALA VAL ARG ALA GLY ALA LYS GLN ILE
SEQRES 18 A 346 ASP GLY SER CYS ARG ARG PHE GLY ALA GLY ALA GLY ASN
SEQRES 19 A 346 ALA PRO VAL GLU ALA LEU ILE GLY VAL PHE ASP LYS ILE
SEQRES 20 A 346 GLY VAL LYS THR GLY ILE ASP PHE PHE ASP ILE ALA ASP
SEQRES 21 A 346 ALA ALA GLU ASP VAL VAL ARG PRO ALA MET PRO ALA GLU
SEQRES 22 A 346 CYS LEU LEU ASP ARG ASN ALA LEU ILE MET GLY TYR SER
SEQRES 23 A 346 GLY VAL TYR SER SER PHE LEU LYS HIS ALA VAL ARG GLN
SEQRES 24 A 346 ALA GLU ARG TYR GLY VAL PRO ALA SER ALA LEU LEU HIS
SEQRES 25 A 346 ARG ALA GLY GLN ARG LYS LEU ILE GLY GLY GLN GLU ASP
SEQRES 26 A 346 GLN LEU ILE ASP ILE ALA LEU GLU ILE LYS ARG GLU LEU
SEQRES 27 A 346 ASP SER GLY ALA ALA VAL THR HIS
SEQRES 1 B 306 GLY SER HIS MET PRO SER LYS ALA LYS VAL ALA ILE VAL
SEQRES 2 B 306 GLY SER GLY ASN ILE SER THR ASP LEU LEU TYR LYS LEU
SEQRES 3 B 306 LEU ARG SER GLU TRP LEU GLU PRO ARG TRP MET VAL GLY
SEQRES 4 B 306 ILE ASP PRO GLU SER ASP GLY LEU ALA ARG ALA ALA LYS
SEQRES 5 B 306 LEU GLY LEU GLU THR THR HIS GLU GLY VAL ASP TRP LEU
SEQRES 6 B 306 LEU ALA GLN PRO ASP LYS PRO ASP LEU VAL PHE GLU ALA
SEQRES 7 B 306 THR SER ALA TYR VAL HIS ARG ASP ALA ALA PRO LYS TYR
SEQRES 8 B 306 ALA GLU ALA GLY ILE ARG ALA ILE ASP LEU THR PRO ALA
SEQRES 9 B 306 ALA VAL GLY PRO ALA VAL ILE PRO PRO ALA ASN LEU ARG
SEQRES 10 B 306 GLU HIS LEU ASP ALA PRO ASN VAL ASN MET ILE THR CYS
SEQRES 11 B 306 GLY GLY GLN ALA THR ILE PRO ILE VAL TYR ALA VAL SER
SEQRES 12 B 306 ARG ILE VAL GLU VAL PRO TYR ALA GLU ILE VAL ALA SER
SEQRES 13 B 306 VAL ALA SER VAL SER ALA GLY PRO GLY THR ARG ALA ASN
SEQRES 14 B 306 ILE ASP GLU PHE THR LYS THR THR ALA ARG GLY VAL GLN
SEQRES 15 B 306 THR ILE GLY GLY ALA ALA ARG GLY LYS ALA ILE ILE ILE
SEQRES 16 B 306 LEU ASN PRO ALA ASP PRO PRO MET ILE MET ARG ASP THR
SEQRES 17 B 306 ILE PHE CYS ALA ILE PRO THR ASP ALA ASP ARG GLU ALA
SEQRES 18 B 306 ILE ALA ALA SER ILE HIS ASP VAL VAL LYS GLU VAL GLN
SEQRES 19 B 306 THR TYR VAL PRO GLY TYR ARG LEU LEU ASN GLU PRO GLN
SEQRES 20 B 306 PHE ASP GLU PRO SER ILE ASN SER GLY GLY GLN ALA LEU
SEQRES 21 B 306 VAL THR THR PHE VAL GLU VAL GLU GLY ALA GLY ASP TYR
SEQRES 22 B 306 LEU PRO PRO TYR ALA GLY ASN LEU ASP ILE MET THR ALA
SEQRES 23 B 306 ALA ALA THR LYS VAL GLY GLU GLU ILE ALA LYS GLU THR
SEQRES 24 B 306 LEU VAL VAL GLY GLY ALA ARG
SEQRES 1 C 346 MET THR ASP MET TRP ASP VAL ARG ILE THR ASP THR SER
SEQRES 2 C 346 LEU ARG ASP GLY SER HIS HIS LYS ARG HIS GLN PHE THR
SEQRES 3 C 346 LYS ASP GLU VAL GLY ALA ILE VAL ALA ALA LEU ASP ALA
SEQRES 4 C 346 ALA GLY VAL PRO VAL ILE GLU VAL THR HIS GLY ASP GLY
SEQRES 5 C 346 LEU GLY GLY SER SER PHE ASN TYR GLY PHE SER LYS THR
SEQRES 6 C 346 PRO GLU GLN GLU LEU ILE LYS LEU ALA ALA ALA THR ALA
SEQRES 7 C 346 LYS GLU ALA ARG ILE ALA PHE LEU MET LEU PRO GLY VAL
SEQRES 8 C 346 GLY THR LYS ASP ASP ILE LYS GLU ALA ARG ASP ASN GLY
SEQRES 9 C 346 GLY SER ILE CYS ARG ILE ALA THR HIS CYS THR GLU ALA
SEQRES 10 C 346 ASP VAL SER ILE GLN HIS PHE GLY LEU ALA ARG GLU LEU
SEQRES 11 C 346 GLY LEU GLU THR VAL GLY PHE LEU MET MET ALA HIS THR
SEQRES 12 C 346 ILE ALA PRO GLU LYS LEU ALA ALA GLN ALA ARG ILE MET
SEQRES 13 C 346 ALA ASP ALA GLY CYS GLN CYS VAL TYR VAL VAL ASP SER
SEQRES 14 C 346 ALA GLY ALA LEU VAL LEU ASP GLY VAL ALA ASP ARG VAL
SEQRES 15 C 346 SER ALA LEU VAL ALA GLU LEU GLY GLU ASP ALA GLN VAL
SEQRES 16 C 346 GLY PHE HIS GLY HIS GLU ASN LEU GLY LEU GLY VAL ALA
SEQRES 17 C 346 ASN SER VAL ALA ALA VAL ARG ALA GLY ALA LYS GLN ILE
SEQRES 18 C 346 ASP GLY SER CYS ARG ARG PHE GLY ALA GLY ALA GLY ASN
SEQRES 19 C 346 ALA PRO VAL GLU ALA LEU ILE GLY VAL PHE ASP LYS ILE
SEQRES 20 C 346 GLY VAL LYS THR GLY ILE ASP PHE PHE ASP ILE ALA ASP
SEQRES 21 C 346 ALA ALA GLU ASP VAL VAL ARG PRO ALA MET PRO ALA GLU
SEQRES 22 C 346 CYS LEU LEU ASP ARG ASN ALA LEU ILE MET GLY TYR SER
SEQRES 23 C 346 GLY VAL TYR SER SER PHE LEU LYS HIS ALA VAL ARG GLN
SEQRES 24 C 346 ALA GLU ARG TYR GLY VAL PRO ALA SER ALA LEU LEU HIS
SEQRES 25 C 346 ARG ALA GLY GLN ARG LYS LEU ILE GLY GLY GLN GLU ASP
SEQRES 26 C 346 GLN LEU ILE ASP ILE ALA LEU GLU ILE LYS ARG GLU LEU
SEQRES 27 C 346 ASP SER GLY ALA ALA VAL THR HIS
SEQRES 1 D 306 GLY SER HIS MET PRO SER LYS ALA LYS VAL ALA ILE VAL
SEQRES 2 D 306 GLY SER GLY ASN ILE SER THR ASP LEU LEU TYR LYS LEU
SEQRES 3 D 306 LEU ARG SER GLU TRP LEU GLU PRO ARG TRP MET VAL GLY
SEQRES 4 D 306 ILE ASP PRO GLU SER ASP GLY LEU ALA ARG ALA ALA LYS
SEQRES 5 D 306 LEU GLY LEU GLU THR THR HIS GLU GLY VAL ASP TRP LEU
SEQRES 6 D 306 LEU ALA GLN PRO ASP LYS PRO ASP LEU VAL PHE GLU ALA
SEQRES 7 D 306 THR SER ALA TYR VAL HIS ARG ASP ALA ALA PRO LYS TYR
SEQRES 8 D 306 ALA GLU ALA GLY ILE ARG ALA ILE ASP LEU THR PRO ALA
SEQRES 9 D 306 ALA VAL GLY PRO ALA VAL ILE PRO PRO ALA ASN LEU ARG
SEQRES 10 D 306 GLU HIS LEU ASP ALA PRO ASN VAL ASN MET ILE THR CYS
SEQRES 11 D 306 GLY GLY GLN ALA THR ILE PRO ILE VAL TYR ALA VAL SER
SEQRES 12 D 306 ARG ILE VAL GLU VAL PRO TYR ALA GLU ILE VAL ALA SER
SEQRES 13 D 306 VAL ALA SER VAL SER ALA GLY PRO GLY THR ARG ALA ASN
SEQRES 14 D 306 ILE ASP GLU PHE THR LYS THR THR ALA ARG GLY VAL GLN
SEQRES 15 D 306 THR ILE GLY GLY ALA ALA ARG GLY LYS ALA ILE ILE ILE
SEQRES 16 D 306 LEU ASN PRO ALA ASP PRO PRO MET ILE MET ARG ASP THR
SEQRES 17 D 306 ILE PHE CYS ALA ILE PRO THR ASP ALA ASP ARG GLU ALA
SEQRES 18 D 306 ILE ALA ALA SER ILE HIS ASP VAL VAL LYS GLU VAL GLN
SEQRES 19 D 306 THR TYR VAL PRO GLY TYR ARG LEU LEU ASN GLU PRO GLN
SEQRES 20 D 306 PHE ASP GLU PRO SER ILE ASN SER GLY GLY GLN ALA LEU
SEQRES 21 D 306 VAL THR THR PHE VAL GLU VAL GLU GLY ALA GLY ASP TYR
SEQRES 22 D 306 LEU PRO PRO TYR ALA GLY ASN LEU ASP ILE MET THR ALA
SEQRES 23 D 306 ALA ALA THR LYS VAL GLY GLU GLU ILE ALA LYS GLU THR
SEQRES 24 D 306 LEU VAL VAL GLY GLY ALA ARG
HET OXL A 401 6
HET MN A 402 1
HET OXL C 401 6
HET NA C 402 1
HET MN C 403 1
HETNAM OXL OXALATE ION
HETNAM MN MANGANESE (II) ION
HETNAM NA SODIUM ION
FORMUL 5 OXL 2(C2 O4 2-)
FORMUL 6 MN 2(MN 2+)
FORMUL 8 NA NA 1+
FORMUL 10 HOH *353(H2 O)
HELIX 1 1 ARG A 15 LYS A 21 1 7
HELIX 2 2 THR A 26 ALA A 40 1 15
HELIX 3 3 PRO A 66 ALA A 78 1 13
HELIX 4 4 THR A 93 ASN A 103 1 11
HELIX 5 5 GLU A 116 VAL A 119 5 4
HELIX 6 6 SER A 120 LEU A 130 1 11
HELIX 7 7 MET A 140 ILE A 144 5 5
HELIX 8 8 ALA A 145 ALA A 159 1 15
HELIX 9 9 LEU A 175 GLY A 190 1 16
HELIX 10 10 LEU A 205 ALA A 216 1 12
HELIX 11 11 SER A 224 PHE A 228 5 5
HELIX 12 12 PRO A 236 ILE A 247 1 12
HELIX 13 13 ASP A 254 VAL A 265 1 12
HELIX 14 14 VAL A 266 MET A 270 5 5
HELIX 15 15 ASP A 277 GLY A 287 1 11
HELIX 16 16 SER A 291 GLY A 304 1 14
HELIX 17 17 PRO A 306 ARG A 317 1 12
HELIX 18 18 GLU A 324 ASP A 339 1 16
HELIX 19 19 GLY B 13 ARG B 25 1 13
HELIX 20 20 SER B 41 LEU B 50 1 10
HELIX 21 21 GLY B 58 LEU B 63 1 6
HELIX 22 22 SER B 77 GLY B 92 1 16
HELIX 23 23 ILE B 108 LEU B 117 1 10
HELIX 24 24 THR B 126 ARG B 141 1 16
HELIX 25 25 VAL B 157 ALA B 159 5 3
HELIX 26 26 GLY B 160 ASN B 166 1 7
HELIX 27 27 ASN B 166 ILE B 181 1 16
HELIX 28 28 ASP B 215 THR B 232 1 18
HELIX 29 29 ALA B 275 THR B 296 1 22
HELIX 30 30 ARG C 15 LYS C 21 1 7
HELIX 31 31 THR C 26 GLY C 41 1 16
HELIX 32 32 PRO C 66 ALA C 78 1 13
HELIX 33 33 THR C 93 ASN C 103 1 11
HELIX 34 34 GLU C 116 VAL C 119 5 4
HELIX 35 35 SER C 120 LEU C 130 1 11
HELIX 36 36 MET C 140 ILE C 144 5 5
HELIX 37 37 ALA C 145 GLY C 160 1 16
HELIX 38 38 LEU C 175 GLY C 190 1 16
HELIX 39 39 GLU C 191 ALA C 193 5 3
HELIX 40 40 LEU C 205 ALA C 216 1 12
HELIX 41 41 SER C 224 PHE C 228 5 5
HELIX 42 42 PRO C 236 GLY C 248 1 13
HELIX 43 43 ASP C 254 VAL C 265 1 12
HELIX 44 44 VAL C 266 MET C 270 5 5
HELIX 45 45 ASP C 277 GLY C 287 1 11
HELIX 46 46 TYR C 289 SER C 291 5 3
HELIX 47 47 PHE C 292 GLY C 304 1 13
HELIX 48 48 PRO C 306 ARG C 317 1 12
HELIX 49 49 ASP C 325 GLY C 341 1 17
HELIX 50 50 GLY D 13 ARG D 25 1 13
HELIX 51 51 SER D 41 LEU D 50 1 10
HELIX 52 52 GLY D 58 LEU D 63 1 6
HELIX 53 53 SER D 77 ALA D 91 1 15
HELIX 54 54 ILE D 108 LEU D 113 1 6
HELIX 55 55 ARG D 114 LEU D 117 5 4
HELIX 56 56 THR D 126 ARG D 141 1 16
HELIX 57 57 VAL D 157 ALA D 159 5 3
HELIX 58 58 GLY D 160 ASN D 166 1 7
HELIX 59 59 ASN D 166 ILE D 181 1 16
HELIX 60 60 ASP D 215 THR D 232 1 18
HELIX 61 61 ALA D 275 LEU D 297 1 23
SHEET 1 A 9 ARG A 8 LEU A 14 0
SHEET 2 A 9 VAL A 44 VAL A 47 1 O GLU A 46 N ASP A 11
SHEET 3 A 9 ARG A 82 MET A 87 1 O ALA A 84 N VAL A 47
SHEET 4 A 9 ILE A 107 HIS A 113 1 O ALA A 111 N MET A 87
SHEET 5 A 9 GLU A 133 MET A 139 1 O VAL A 135 N ILE A 110
SHEET 6 A 9 CYS A 163 ASP A 168 1 O TYR A 165 N GLY A 136
SHEET 7 A 9 GLN A 194 GLY A 199 1 O GLY A 196 N VAL A 166
SHEET 8 A 9 GLN A 220 GLY A 223 1 O ASP A 222 N PHE A 197
SHEET 9 A 9 ARG A 8 LEU A 14 1 N THR A 10 O ILE A 221
SHEET 1 B 6 GLU B 53 THR B 55 0
SHEET 2 B 6 LEU B 29 VAL B 35 1 N ARG B 32 O GLU B 53
SHEET 3 B 6 ALA B 5 VAL B 10 1 N ILE B 9 O TRP B 33
SHEET 4 B 6 LEU B 71 GLU B 74 1 O PHE B 73 N VAL B 10
SHEET 5 B 6 ARG B 94 ASP B 97 1 O ILE B 96 N VAL B 72
SHEET 6 B 6 ASN B 121 ASN B 123 1 O VAL B 122 N ASP B 97
SHEET 1 C 5 GLY B 187 ASN B 194 0
SHEET 2 C 5 ALA B 148 ALA B 155 1 N ALA B 152 O ILE B 190
SHEET 3 C 5 MET B 202 ILE B 210 -1 O PHE B 207 N GLU B 149
SHEET 4 C 5 ALA B 256 VAL B 264 -1 O THR B 260 N ILE B 206
SHEET 5 C 5 TYR B 237 LEU B 239 -1 N ARG B 238 O GLU B 263
SHEET 1 D 5 GLY B 187 ASN B 194 0
SHEET 2 D 5 ALA B 148 ALA B 155 1 N ALA B 152 O ILE B 190
SHEET 3 D 5 MET B 202 ILE B 210 -1 O PHE B 207 N GLU B 149
SHEET 4 D 5 ALA B 256 VAL B 264 -1 O THR B 260 N ILE B 206
SHEET 5 D 5 GLN B 244 ASP B 246 -1 N GLN B 244 O THR B 259
SHEET 1 E 9 ARG C 8 LEU C 14 0
SHEET 2 E 9 VAL C 44 VAL C 47 1 O GLU C 46 N ASP C 11
SHEET 3 E 9 ARG C 82 MET C 87 1 O ALA C 84 N VAL C 47
SHEET 4 E 9 ILE C 107 HIS C 113 1 O ARG C 109 N PHE C 85
SHEET 5 E 9 GLU C 133 MET C 139 1 O GLU C 133 N CYS C 108
SHEET 6 E 9 CYS C 163 ASP C 168 1 O TYR C 165 N GLY C 136
SHEET 7 E 9 GLN C 194 GLY C 199 1 O GLY C 196 N VAL C 166
SHEET 8 E 9 GLN C 220 GLY C 223 1 O ASP C 222 N PHE C 197
SHEET 9 E 9 ARG C 8 LEU C 14 1 N THR C 12 O GLY C 223
SHEET 1 F 6 GLU D 53 THR D 55 0
SHEET 2 F 6 LEU D 29 VAL D 35 1 N ARG D 32 O GLU D 53
SHEET 3 F 6 ALA D 5 VAL D 10 1 N ILE D 9 O VAL D 35
SHEET 4 F 6 LEU D 71 GLU D 74 1 O PHE D 73 N VAL D 10
SHEET 5 F 6 ARG D 94 ASP D 97 1 O ILE D 96 N VAL D 72
SHEET 6 F 6 ASN D 121 ASN D 123 1 O VAL D 122 N ASP D 97
SHEET 1 G 5 GLY D 187 ASN D 194 0
SHEET 2 G 5 ALA D 148 ALA D 155 1 N ALA D 152 O ILE D 190
SHEET 3 G 5 MET D 202 ILE D 210 -1 O PHE D 207 N GLU D 149
SHEET 4 G 5 ALA D 256 VAL D 264 -1 O VAL D 264 N MET D 202
SHEET 5 G 5 TYR D 237 LEU D 239 -1 N ARG D 238 O GLU D 263
SHEET 1 H 5 GLY D 187 ASN D 194 0
SHEET 2 H 5 ALA D 148 ALA D 155 1 N ALA D 152 O ILE D 190
SHEET 3 H 5 MET D 202 ILE D 210 -1 O PHE D 207 N GLU D 149
SHEET 4 H 5 ALA D 256 VAL D 264 -1 O VAL D 264 N MET D 202
SHEET 5 H 5 GLN D 244 ASP D 246 -1 N GLN D 244 O THR D 259
LINK OD1 ASP A 16 MN MN A 402 1555 1555 2.31
LINK NE2 HIS A 198 MN MN A 402 1555 1555 2.31
LINK NE2 HIS A 200 MN MN A 402 1555 1555 2.30
LINK O1 OXL A 401 MN MN A 402 1555 1555 2.33
LINK O2 OXL A 401 MN MN A 402 1555 1555 2.33
LINK MN MN A 402 O HOH A 578 1555 1555 2.62
LINK OD2 ASP C 16 MN MN C 403 1555 1555 2.17
LINK NE2 HIS C 198 MN MN C 403 1555 1555 2.35
LINK NE2 HIS C 200 MN MN C 403 1555 1555 2.21
LINK O4 OXL C 401 MN MN C 403 1555 1555 2.14
LINK O1 OXL C 401 MN MN C 403 1555 1555 2.37
LINK NA NA C 402 O HOH C 512 1555 1555 2.82
LINK NA NA C 402 O HOH C 515 1555 1555 2.74
LINK MN MN C 403 O HOH C 540 1555 1555 2.49
CISPEP 1 ASP B 197 PRO B 198 0 6.37
CISPEP 2 ASP D 197 PRO D 198 0 0.82
SITE 1 AC1 12 ARG A 15 ASP A 16 PHE A 137 MET A 139
SITE 2 AC1 12 VAL A 167 SER A 169 HIS A 198 HIS A 200
SITE 3 AC1 12 TYR A 289 MN A 402 HOH A 578 HOH A 595
SITE 1 AC2 5 ASP A 16 HIS A 198 HIS A 200 OXL A 401
SITE 2 AC2 5 HOH A 578
SITE 1 AC3 12 ARG C 15 ASP C 16 PHE C 137 MET C 139
SITE 2 AC3 12 VAL C 167 SER C 169 HIS C 198 HIS C 200
SITE 3 AC3 12 TYR C 289 MN C 403 HOH C 540 HOH C 606
SITE 1 AC4 6 HIS C 19 HIS C 23 TYR C 60 HIS C 295
SITE 2 AC4 6 HOH C 512 HOH C 515
SITE 1 AC5 5 ASP C 16 HIS C 198 HIS C 200 OXL C 401
SITE 2 AC5 5 HOH C 540
CRYST1 69.690 142.690 148.170 90.00 95.08 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 0.014349 0.000000 0.001277 0.00000
SCALE2 0.000000 0.007008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006776 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
