HEADER OXIDOREDUCTASE 30-MAR-10 2XAA
TITLE ALCOHOL DEHYDROGENASE ADH-'A' FROM RHODOCOCCUS RUBER DSM 44541 AT PH
TITLE 2 8.5 IN COMPLEX WITH NAD AND BUTANE-1,4-DIOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SECONDARY ALCOHOL DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 1-345;
COMPND 5 SYNONYM: ADH-'A';
COMPND 6 EC: 1.1.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RUBER;
SOURCE 3 ORGANISM_TAXID: 1830;
SOURCE 4 STRAIN: DSM 44541;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TUNER (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 10 OTHER_DETAILS: DSM
KEYWDS CARBONYL REDUCTASE, KETOREDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.KROUTIL,K.GRUBER,G.GROGAN
REVDAT 3 20-DEC-23 2XAA 1 REMARK LINK
REVDAT 2 01-SEP-10 2XAA 1 JRNL REMARK
REVDAT 1 11-AUG-10 2XAA 0
JRNL AUTH M.KARABEC,A.LYSKOWSKI,K.C.TAUBER,G.STEINKELLNER,W.KROUTIL,
JRNL AUTH 2 G.GROGAN,K.GRUBER
JRNL TITL STRUCTURAL INSIGHTS INTO SUBSTRATE SPECIFICITY AND SOLVENT
JRNL TITL 2 TOLERANCE IN ALCOHOL DEHYDROGENASE ADH-'A' FROM RHODOCOCCUS
JRNL TITL 3 RUBER DSM 44541.
JRNL REF CHEM.COMMUN.(CAMB.) V. 46 6314 2010
JRNL REFN ISSN 1359-7345
JRNL PMID 20676439
JRNL DOI 10.1039/C0CC00929F
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 109.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 34356
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1807
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2238
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9731
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 202
REMARK 3 SOLVENT ATOMS : 142
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.79000
REMARK 3 B22 (A**2) : 3.02000
REMARK 3 B33 (A**2) : -0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.94000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.399
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.299
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.282
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10136 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13859 ; 1.635 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1354 ; 6.403 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 351 ;33.413 ;22.650
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1379 ;17.195 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 71 ;17.264 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1621 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7683 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6708 ; 0.503 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10665 ; 0.947 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3428 ; 1.420 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3193 ; 2.422 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 345 4
REMARK 3 1 B 1 B 345 4
REMARK 3 1 C 1 C 345 4
REMARK 3 1 D 1 D 345 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2341 ; 0.38 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2341 ; 0.33 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2341 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 2341 ; 0.31 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2341 ; 1.01 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2341 ; 0.81 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2341 ; 0.95 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 2341 ; 0.86 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 2XAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1290043471.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34356
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 109.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 9.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3JV7
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BISTRIS PROPANE BUFFER PH 8.5,
REMARK 280 20% (W/V) PEG MW 4000, 5 MM CDCL2, 6% V/V 2-PROPANOL, 5% (V/V) 1,
REMARK 280 4-BUTANEDIOL. PROTEIN AT 10 MG/ML
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 52.55000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 16010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -256.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 VAL A 15
REMARK 465 VAL A 16
REMARK 465 PRO A 25
REMARK 465 GLY A 26
REMARK 465 ALA A 53
REMARK 465 GLU A 70
REMARK 465 LEU A 71
REMARK 465 GLY A 72
REMARK 465 GLU A 73
REMARK 465 GLY A 74
REMARK 465 VAL A 75
REMARK 465 THR A 76
REMARK 465 PRO B 25
REMARK 465 ALA B 69
REMARK 465 GLU B 73
REMARK 465 GLN C 238
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 LYS A 2 CG CD CE NZ
REMARK 470 VAL A 4 CG1 CG2
REMARK 470 ILE A 9 CG1 CG2 CD1
REMARK 470 ILE A 18 CG1 CG2 CD1
REMARK 470 ILE A 42 CG1 CG2 CD1
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 ILE A 315 CD1
REMARK 470 ARG A 330 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 332 CG CD1 CD2
REMARK 470 VAL B 4 CG1 CG2
REMARK 470 VAL B 14 CG1 CG2
REMARK 470 THR B 22 OG1 CG2
REMARK 470 LYS B 31 CG CD CE NZ
REMARK 470 ILE B 42 CG1 CG2 CD1
REMARK 470 GLU B 70 CG CD OE1 OE2
REMARK 470 VAL B 80 CG1 CG2
REMARK 470 GLU C 73 CG CD OE1 OE2
REMARK 470 GLU D 73 CG CD OE1 OE2
REMARK 470 ILE D 271 CD1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 3 102.88 -162.26
REMARK 500 VAL A 4 106.37 -56.55
REMARK 500 SER A 11 -134.86 -111.85
REMARK 500 PRO A 13 -169.23 -76.23
REMARK 500 PRO A 23 -134.82 -74.13
REMARK 500 ALA A 50 -81.84 -54.45
REMARK 500 ARG A 102 49.87 -89.89
REMARK 500 ASP A 142 30.27 -83.96
REMARK 500 THR A 152 -9.36 -58.55
REMARK 500 ASP A 153 -50.91 -155.09
REMARK 500 LEU A 169 49.88 -106.20
REMARK 500 PHE A 282 -16.71 79.29
REMARK 500 TRP A 295 -131.30 40.55
REMARK 500 GLU A 324 8.18 -68.67
REMARK 500 GLU B 12 150.47 -47.96
REMARK 500 ALA B 34 140.96 -170.23
REMARK 500 ILE B 42 13.04 -65.11
REMARK 500 LEU B 112 7.66 -68.10
REMARK 500 ASP B 153 -61.73 -142.59
REMARK 500 LEU B 169 47.17 -85.82
REMARK 500 ALA B 273 90.60 10.65
REMARK 500 PHE B 282 -7.20 78.86
REMARK 500 PHE B 286 133.42 -33.90
REMARK 500 TRP B 295 -132.80 50.65
REMARK 500 LEU C 60 173.14 -59.42
REMARK 500 ALA C 273 109.45 -50.13
REMARK 500 TRP C 295 -127.15 43.21
REMARK 500 ARG D 102 49.51 -82.17
REMARK 500 LEU D 119 48.18 -141.54
REMARK 500 ASP D 142 20.39 -79.07
REMARK 500 ASP D 153 -66.42 -144.83
REMARK 500 LEU D 169 48.62 -87.45
REMARK 500 VAL D 180 64.38 -103.48
REMARK 500 PHE D 282 -15.09 82.42
REMARK 500 TRP D 295 -116.55 47.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS B 272 ALA B 273 148.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2005 DISTANCE = 6.26 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1346 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 38 SG
REMARK 620 2 ASP A 153 OD2 106.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1347 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 92 SG
REMARK 620 2 CYS A 95 SG 111.1
REMARK 620 3 CYS A 98 SG 113.0 106.8
REMARK 620 4 CYS A 106 SG 112.0 111.8 101.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1346 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 38 SG
REMARK 620 2 HIS B 62 NE2 95.8
REMARK 620 3 ASP B 153 OD2 101.0 79.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1348 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 92 SG
REMARK 620 2 CYS B 95 SG 109.7
REMARK 620 3 CYS B 98 SG 116.5 103.5
REMARK 620 4 CYS B 106 SG 113.1 108.9 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1346 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 38 SG
REMARK 620 2 HIS C 62 NE2 103.9
REMARK 620 3 ASP C 153 OD2 99.2 86.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1347 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 92 SG
REMARK 620 2 CYS C 95 SG 112.5
REMARK 620 3 CYS C 98 SG 116.6 103.6
REMARK 620 4 CYS C 106 SG 106.9 112.9 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1346 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 38 SG
REMARK 620 2 HIS D 62 NE2 107.0
REMARK 620 3 ASP D 153 OD2 118.1 84.0
REMARK 620 4 BU1 D1347 O6 126.3 102.2 108.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1348 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 92 SG
REMARK 620 2 CYS D 95 SG 113.0
REMARK 620 3 CYS D 98 SG 111.3 96.7
REMARK 620 4 CYS D 106 SG 114.8 118.5 99.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1347
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 B 1347
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1348
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1347
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1346
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 D 1347
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1348
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 C 1348
DBREF 2XAA A 1 345 UNP Q8KLT9 Q8KLT9_9NOCA 1 345
DBREF 2XAA B 1 345 UNP Q8KLT9 Q8KLT9_9NOCA 1 345
DBREF 2XAA C 1 345 UNP Q8KLT9 Q8KLT9_9NOCA 1 345
DBREF 2XAA D 1 345 UNP Q8KLT9 Q8KLT9_9NOCA 1 345
SEQADV 2XAA VAL A 4 UNP Q8KLT9 LEU 4 CONFLICT
SEQADV 2XAA ILE A 18 UNP Q8KLT9 VAL 18 CONFLICT
SEQADV 2XAA THR A 22 UNP Q8KLT9 ALA 22 CONFLICT
SEQADV 2XAA GLU A 73 UNP Q8KLT9 ALA 73 CONFLICT
SEQADV 2XAA VAL A 80 UNP Q8KLT9 THR 80 CONFLICT
SEQADV 2XAA ASP A 111 UNP Q8KLT9 GLU 111 CONFLICT
SEQADV 2XAA GLN A 238 UNP Q8KLT9 GLU 238 CONFLICT
SEQADV 2XAA VAL A 262 UNP Q8KLT9 ILE 262 CONFLICT
SEQADV 2XAA GLU A 303 UNP Q8KLT9 ASP 303 CONFLICT
SEQADV 2XAA VAL B 4 UNP Q8KLT9 LEU 4 CONFLICT
SEQADV 2XAA ILE B 18 UNP Q8KLT9 VAL 18 CONFLICT
SEQADV 2XAA THR B 22 UNP Q8KLT9 ALA 22 CONFLICT
SEQADV 2XAA GLU B 73 UNP Q8KLT9 ALA 73 CONFLICT
SEQADV 2XAA VAL B 80 UNP Q8KLT9 THR 80 CONFLICT
SEQADV 2XAA ASP B 111 UNP Q8KLT9 GLU 111 CONFLICT
SEQADV 2XAA GLN B 238 UNP Q8KLT9 GLU 238 CONFLICT
SEQADV 2XAA VAL B 262 UNP Q8KLT9 ILE 262 CONFLICT
SEQADV 2XAA GLU B 303 UNP Q8KLT9 ASP 303 CONFLICT
SEQADV 2XAA VAL C 4 UNP Q8KLT9 LEU 4 CONFLICT
SEQADV 2XAA ILE C 18 UNP Q8KLT9 VAL 18 CONFLICT
SEQADV 2XAA THR C 22 UNP Q8KLT9 ALA 22 CONFLICT
SEQADV 2XAA GLU C 73 UNP Q8KLT9 ALA 73 CONFLICT
SEQADV 2XAA VAL C 80 UNP Q8KLT9 THR 80 CONFLICT
SEQADV 2XAA ASP C 111 UNP Q8KLT9 GLU 111 CONFLICT
SEQADV 2XAA GLN C 238 UNP Q8KLT9 GLU 238 CONFLICT
SEQADV 2XAA VAL C 262 UNP Q8KLT9 ILE 262 CONFLICT
SEQADV 2XAA GLU C 303 UNP Q8KLT9 ASP 303 CONFLICT
SEQADV 2XAA VAL D 4 UNP Q8KLT9 LEU 4 CONFLICT
SEQADV 2XAA ILE D 18 UNP Q8KLT9 VAL 18 CONFLICT
SEQADV 2XAA THR D 22 UNP Q8KLT9 ALA 22 CONFLICT
SEQADV 2XAA GLU D 73 UNP Q8KLT9 ALA 73 CONFLICT
SEQADV 2XAA VAL D 80 UNP Q8KLT9 THR 80 CONFLICT
SEQADV 2XAA ASP D 111 UNP Q8KLT9 GLU 111 CONFLICT
SEQADV 2XAA GLN D 238 UNP Q8KLT9 GLU 238 CONFLICT
SEQADV 2XAA VAL D 262 UNP Q8KLT9 ILE 262 CONFLICT
SEQADV 2XAA GLU D 303 UNP Q8KLT9 ASP 303 CONFLICT
SEQRES 1 A 345 MET LYS ALA VAL GLN TYR THR GLU ILE GLY SER GLU PRO
SEQRES 2 A 345 VAL VAL VAL ASP ILE PRO THR PRO THR PRO GLY PRO GLY
SEQRES 3 A 345 GLU ILE LEU LEU LYS VAL THR ALA ALA GLY LEU CYS HIS
SEQRES 4 A 345 SER ASP ILE PHE VAL MET ASP MET PRO ALA ALA GLN TYR
SEQRES 5 A 345 ALA TYR GLY LEU PRO LEU THR LEU GLY HIS GLU GLY VAL
SEQRES 6 A 345 GLY THR VAL ALA GLU LEU GLY GLU GLY VAL THR GLY PHE
SEQRES 7 A 345 GLY VAL GLY ASP ALA VAL ALA VAL TYR GLY PRO TRP GLY
SEQRES 8 A 345 CYS GLY ALA CYS HIS ALA CYS ALA ARG GLY ARG GLU ASN
SEQRES 9 A 345 TYR CYS THR ARG ALA ALA ASP LEU GLY ILE THR PRO PRO
SEQRES 10 A 345 GLY LEU GLY SER PRO GLY SER MET ALA GLU TYR MET ILE
SEQRES 11 A 345 VAL ASP SER ALA ARG HIS LEU VAL PRO ILE GLY ASP LEU
SEQRES 12 A 345 ASP PRO VAL ALA ALA ALA PRO LEU THR ASP ALA GLY LEU
SEQRES 13 A 345 THR PRO TYR HIS ALA ILE SER ARG VAL LEU PRO LEU LEU
SEQRES 14 A 345 GLY PRO GLY SER THR ALA VAL VAL ILE GLY VAL GLY GLY
SEQRES 15 A 345 LEU GLY HIS VAL GLY ILE GLN ILE LEU ARG ALA VAL SER
SEQRES 16 A 345 ALA ALA ARG VAL ILE ALA VAL ASP LEU ASP ASP ASP ARG
SEQRES 17 A 345 LEU ALA LEU ALA ARG GLU VAL GLY ALA ASP ALA ALA VAL
SEQRES 18 A 345 LYS SER GLY ALA GLY ALA ALA ASP ALA ILE ARG GLU LEU
SEQRES 19 A 345 THR GLY GLY GLN GLY ALA THR ALA VAL PHE ASP PHE VAL
SEQRES 20 A 345 GLY ALA GLN SER THR ILE ASP THR ALA GLN GLN VAL VAL
SEQRES 21 A 345 ALA VAL ASP GLY HIS ILE SER VAL VAL GLY ILE HIS ALA
SEQRES 22 A 345 GLY ALA HIS ALA LYS VAL GLY PHE PHE MET ILE PRO PHE
SEQRES 23 A 345 GLY ALA SER VAL VAL THR PRO TYR TRP GLY THR ARG SER
SEQRES 24 A 345 GLU LEU MET GLU VAL VAL ALA LEU ALA ARG ALA GLY ARG
SEQRES 25 A 345 LEU ASP ILE HIS THR GLU THR PHE THR LEU ASP GLU GLY
SEQRES 26 A 345 PRO ALA ALA TYR ARG ARG LEU ARG GLU GLY SER ILE ARG
SEQRES 27 A 345 GLY ARG GLY VAL VAL VAL PRO
SEQRES 1 B 345 MET LYS ALA VAL GLN TYR THR GLU ILE GLY SER GLU PRO
SEQRES 2 B 345 VAL VAL VAL ASP ILE PRO THR PRO THR PRO GLY PRO GLY
SEQRES 3 B 345 GLU ILE LEU LEU LYS VAL THR ALA ALA GLY LEU CYS HIS
SEQRES 4 B 345 SER ASP ILE PHE VAL MET ASP MET PRO ALA ALA GLN TYR
SEQRES 5 B 345 ALA TYR GLY LEU PRO LEU THR LEU GLY HIS GLU GLY VAL
SEQRES 6 B 345 GLY THR VAL ALA GLU LEU GLY GLU GLY VAL THR GLY PHE
SEQRES 7 B 345 GLY VAL GLY ASP ALA VAL ALA VAL TYR GLY PRO TRP GLY
SEQRES 8 B 345 CYS GLY ALA CYS HIS ALA CYS ALA ARG GLY ARG GLU ASN
SEQRES 9 B 345 TYR CYS THR ARG ALA ALA ASP LEU GLY ILE THR PRO PRO
SEQRES 10 B 345 GLY LEU GLY SER PRO GLY SER MET ALA GLU TYR MET ILE
SEQRES 11 B 345 VAL ASP SER ALA ARG HIS LEU VAL PRO ILE GLY ASP LEU
SEQRES 12 B 345 ASP PRO VAL ALA ALA ALA PRO LEU THR ASP ALA GLY LEU
SEQRES 13 B 345 THR PRO TYR HIS ALA ILE SER ARG VAL LEU PRO LEU LEU
SEQRES 14 B 345 GLY PRO GLY SER THR ALA VAL VAL ILE GLY VAL GLY GLY
SEQRES 15 B 345 LEU GLY HIS VAL GLY ILE GLN ILE LEU ARG ALA VAL SER
SEQRES 16 B 345 ALA ALA ARG VAL ILE ALA VAL ASP LEU ASP ASP ASP ARG
SEQRES 17 B 345 LEU ALA LEU ALA ARG GLU VAL GLY ALA ASP ALA ALA VAL
SEQRES 18 B 345 LYS SER GLY ALA GLY ALA ALA ASP ALA ILE ARG GLU LEU
SEQRES 19 B 345 THR GLY GLY GLN GLY ALA THR ALA VAL PHE ASP PHE VAL
SEQRES 20 B 345 GLY ALA GLN SER THR ILE ASP THR ALA GLN GLN VAL VAL
SEQRES 21 B 345 ALA VAL ASP GLY HIS ILE SER VAL VAL GLY ILE HIS ALA
SEQRES 22 B 345 GLY ALA HIS ALA LYS VAL GLY PHE PHE MET ILE PRO PHE
SEQRES 23 B 345 GLY ALA SER VAL VAL THR PRO TYR TRP GLY THR ARG SER
SEQRES 24 B 345 GLU LEU MET GLU VAL VAL ALA LEU ALA ARG ALA GLY ARG
SEQRES 25 B 345 LEU ASP ILE HIS THR GLU THR PHE THR LEU ASP GLU GLY
SEQRES 26 B 345 PRO ALA ALA TYR ARG ARG LEU ARG GLU GLY SER ILE ARG
SEQRES 27 B 345 GLY ARG GLY VAL VAL VAL PRO
SEQRES 1 C 345 MET LYS ALA VAL GLN TYR THR GLU ILE GLY SER GLU PRO
SEQRES 2 C 345 VAL VAL VAL ASP ILE PRO THR PRO THR PRO GLY PRO GLY
SEQRES 3 C 345 GLU ILE LEU LEU LYS VAL THR ALA ALA GLY LEU CYS HIS
SEQRES 4 C 345 SER ASP ILE PHE VAL MET ASP MET PRO ALA ALA GLN TYR
SEQRES 5 C 345 ALA TYR GLY LEU PRO LEU THR LEU GLY HIS GLU GLY VAL
SEQRES 6 C 345 GLY THR VAL ALA GLU LEU GLY GLU GLY VAL THR GLY PHE
SEQRES 7 C 345 GLY VAL GLY ASP ALA VAL ALA VAL TYR GLY PRO TRP GLY
SEQRES 8 C 345 CYS GLY ALA CYS HIS ALA CYS ALA ARG GLY ARG GLU ASN
SEQRES 9 C 345 TYR CYS THR ARG ALA ALA ASP LEU GLY ILE THR PRO PRO
SEQRES 10 C 345 GLY LEU GLY SER PRO GLY SER MET ALA GLU TYR MET ILE
SEQRES 11 C 345 VAL ASP SER ALA ARG HIS LEU VAL PRO ILE GLY ASP LEU
SEQRES 12 C 345 ASP PRO VAL ALA ALA ALA PRO LEU THR ASP ALA GLY LEU
SEQRES 13 C 345 THR PRO TYR HIS ALA ILE SER ARG VAL LEU PRO LEU LEU
SEQRES 14 C 345 GLY PRO GLY SER THR ALA VAL VAL ILE GLY VAL GLY GLY
SEQRES 15 C 345 LEU GLY HIS VAL GLY ILE GLN ILE LEU ARG ALA VAL SER
SEQRES 16 C 345 ALA ALA ARG VAL ILE ALA VAL ASP LEU ASP ASP ASP ARG
SEQRES 17 C 345 LEU ALA LEU ALA ARG GLU VAL GLY ALA ASP ALA ALA VAL
SEQRES 18 C 345 LYS SER GLY ALA GLY ALA ALA ASP ALA ILE ARG GLU LEU
SEQRES 19 C 345 THR GLY GLY GLN GLY ALA THR ALA VAL PHE ASP PHE VAL
SEQRES 20 C 345 GLY ALA GLN SER THR ILE ASP THR ALA GLN GLN VAL VAL
SEQRES 21 C 345 ALA VAL ASP GLY HIS ILE SER VAL VAL GLY ILE HIS ALA
SEQRES 22 C 345 GLY ALA HIS ALA LYS VAL GLY PHE PHE MET ILE PRO PHE
SEQRES 23 C 345 GLY ALA SER VAL VAL THR PRO TYR TRP GLY THR ARG SER
SEQRES 24 C 345 GLU LEU MET GLU VAL VAL ALA LEU ALA ARG ALA GLY ARG
SEQRES 25 C 345 LEU ASP ILE HIS THR GLU THR PHE THR LEU ASP GLU GLY
SEQRES 26 C 345 PRO ALA ALA TYR ARG ARG LEU ARG GLU GLY SER ILE ARG
SEQRES 27 C 345 GLY ARG GLY VAL VAL VAL PRO
SEQRES 1 D 345 MET LYS ALA VAL GLN TYR THR GLU ILE GLY SER GLU PRO
SEQRES 2 D 345 VAL VAL VAL ASP ILE PRO THR PRO THR PRO GLY PRO GLY
SEQRES 3 D 345 GLU ILE LEU LEU LYS VAL THR ALA ALA GLY LEU CYS HIS
SEQRES 4 D 345 SER ASP ILE PHE VAL MET ASP MET PRO ALA ALA GLN TYR
SEQRES 5 D 345 ALA TYR GLY LEU PRO LEU THR LEU GLY HIS GLU GLY VAL
SEQRES 6 D 345 GLY THR VAL ALA GLU LEU GLY GLU GLY VAL THR GLY PHE
SEQRES 7 D 345 GLY VAL GLY ASP ALA VAL ALA VAL TYR GLY PRO TRP GLY
SEQRES 8 D 345 CYS GLY ALA CYS HIS ALA CYS ALA ARG GLY ARG GLU ASN
SEQRES 9 D 345 TYR CYS THR ARG ALA ALA ASP LEU GLY ILE THR PRO PRO
SEQRES 10 D 345 GLY LEU GLY SER PRO GLY SER MET ALA GLU TYR MET ILE
SEQRES 11 D 345 VAL ASP SER ALA ARG HIS LEU VAL PRO ILE GLY ASP LEU
SEQRES 12 D 345 ASP PRO VAL ALA ALA ALA PRO LEU THR ASP ALA GLY LEU
SEQRES 13 D 345 THR PRO TYR HIS ALA ILE SER ARG VAL LEU PRO LEU LEU
SEQRES 14 D 345 GLY PRO GLY SER THR ALA VAL VAL ILE GLY VAL GLY GLY
SEQRES 15 D 345 LEU GLY HIS VAL GLY ILE GLN ILE LEU ARG ALA VAL SER
SEQRES 16 D 345 ALA ALA ARG VAL ILE ALA VAL ASP LEU ASP ASP ASP ARG
SEQRES 17 D 345 LEU ALA LEU ALA ARG GLU VAL GLY ALA ASP ALA ALA VAL
SEQRES 18 D 345 LYS SER GLY ALA GLY ALA ALA ASP ALA ILE ARG GLU LEU
SEQRES 19 D 345 THR GLY GLY GLN GLY ALA THR ALA VAL PHE ASP PHE VAL
SEQRES 20 D 345 GLY ALA GLN SER THR ILE ASP THR ALA GLN GLN VAL VAL
SEQRES 21 D 345 ALA VAL ASP GLY HIS ILE SER VAL VAL GLY ILE HIS ALA
SEQRES 22 D 345 GLY ALA HIS ALA LYS VAL GLY PHE PHE MET ILE PRO PHE
SEQRES 23 D 345 GLY ALA SER VAL VAL THR PRO TYR TRP GLY THR ARG SER
SEQRES 24 D 345 GLU LEU MET GLU VAL VAL ALA LEU ALA ARG ALA GLY ARG
SEQRES 25 D 345 LEU ASP ILE HIS THR GLU THR PHE THR LEU ASP GLU GLY
SEQRES 26 D 345 PRO ALA ALA TYR ARG ARG LEU ARG GLU GLY SER ILE ARG
SEQRES 27 D 345 GLY ARG GLY VAL VAL VAL PRO
HET NAD A 503 44
HET ZN A1346 1
HET ZN A1347 1
HET NAD B 503 44
HET ZN B1346 1
HET BU1 B1347 6
HET ZN B1348 1
HET NAD C 503 44
HET ZN C1346 1
HET ZN C1347 1
HET BU1 C1348 6
HET NAD D 503 44
HET ZN D1346 1
HET BU1 D1347 6
HET ZN D1348 1
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM ZN ZINC ION
HETNAM BU1 1,4-BUTANEDIOL
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 6 ZN 8(ZN 2+)
FORMUL 10 BU1 3(C4 H10 O2)
FORMUL 20 HOH *142(H2 O)
HELIX 1 1 CYS A 38 MET A 45 1 8
HELIX 2 2 CYS A 95 ARG A 100 1 6
HELIX 3 3 ARG A 102 CYS A 106 5 5
HELIX 4 4 ARG A 108 GLY A 113 1 6
HELIX 5 5 SER A 133 ARG A 135 5 3
HELIX 6 6 ASP A 144 GLY A 155 1 12
HELIX 7 7 GLY A 155 ARG A 164 1 10
HELIX 8 8 VAL A 165 LEU A 169 5 5
HELIX 9 9 GLY A 181 SER A 195 1 15
HELIX 10 10 ASP A 205 VAL A 215 1 11
HELIX 11 11 GLY A 226 GLY A 236 1 11
HELIX 12 12 ALA A 249 VAL A 259 1 11
HELIX 13 13 THR A 297 ALA A 310 1 14
HELIX 14 14 GLU A 324 GLY A 335 1 12
HELIX 15 15 SER B 40 MET B 45 1 6
HELIX 16 16 CYS B 95 ARG B 100 1 6
HELIX 17 17 ARG B 102 CYS B 106 5 5
HELIX 18 18 SER B 133 ARG B 135 5 3
HELIX 19 19 ASP B 144 ALA B 149 1 6
HELIX 20 20 PRO B 150 ASP B 153 5 4
HELIX 21 21 GLY B 155 ARG B 164 1 10
HELIX 22 22 VAL B 165 LEU B 169 5 5
HELIX 23 23 LEU B 183 SER B 195 1 13
HELIX 24 24 ASP B 205 VAL B 215 1 11
HELIX 25 25 GLY B 226 GLY B 236 1 11
HELIX 26 26 ALA B 249 VAL B 259 1 11
HELIX 27 27 THR B 297 ALA B 310 1 14
HELIX 28 28 GLU B 324 GLY B 335 1 12
HELIX 29 29 CYS C 38 MET C 47 1 10
HELIX 30 30 ALA C 97 GLY C 101 5 5
HELIX 31 31 ARG C 102 CYS C 106 5 5
HELIX 32 32 ARG C 108 GLY C 113 1 6
HELIX 33 33 SER C 133 ARG C 135 5 3
HELIX 34 34 ASP C 144 ALA C 148 5 5
HELIX 35 35 ALA C 148 THR C 152 5 5
HELIX 36 36 GLY C 155 ARG C 164 1 10
HELIX 37 37 VAL C 165 LEU C 169 5 5
HELIX 38 38 GLY C 181 SER C 195 1 15
HELIX 39 39 ASP C 205 VAL C 215 1 11
HELIX 40 40 GLY C 226 GLY C 236 1 11
HELIX 41 41 ALA C 249 VAL C 259 1 11
HELIX 42 42 THR C 297 ALA C 310 1 14
HELIX 43 43 GLU C 324 GLY C 335 1 12
HELIX 44 44 CYS D 38 ASP D 46 1 9
HELIX 45 45 ALA D 97 GLY D 101 5 5
HELIX 46 46 ARG D 102 CYS D 106 5 5
HELIX 47 47 SER D 133 ARG D 135 5 3
HELIX 48 48 ASP D 144 ALA D 149 1 6
HELIX 49 49 PRO D 150 ASP D 153 5 4
HELIX 50 50 GLY D 155 ARG D 164 1 10
HELIX 51 51 VAL D 165 LEU D 169 5 5
HELIX 52 52 GLY D 181 SER D 195 1 15
HELIX 53 53 ASP D 205 VAL D 215 1 11
HELIX 54 54 GLY D 226 GLY D 236 1 11
HELIX 55 55 ALA D 249 VAL D 259 1 11
HELIX 56 56 THR D 297 ALA D 310 1 14
HELIX 57 57 THR D 321 ASP D 323 5 3
HELIX 58 58 GLU D 324 GLY D 335 1 12
SHEET 1 AA 2 TYR A 128 VAL A 131 0
SHEET 2 AA 2 ILE A 28 GLY A 36 -1 O ILE A 28 N VAL A 131
SHEET 1 AB 6 LEU A 137 PRO A 139 0
SHEET 2 AB 6 ALA A 83 VAL A 86 -1 O ALA A 85 N VAL A 138
SHEET 3 AB 6 GLU A 63 VAL A 68 -1 O GLY A 64 N VAL A 86
SHEET 4 AB 6 ILE A 28 GLY A 36 -1 O LYS A 31 N THR A 67
SHEET 5 AB 6 VAL A 342 VAL A 343 -1 O VAL A 343 N ALA A 35
SHEET 6 AB 6 THR A 319 PHE A 320 -1 N PHE A 320 O VAL A 342
SHEET 1 AC 5 LEU A 137 PRO A 139 0
SHEET 2 AC 5 ALA A 83 VAL A 86 -1 O ALA A 85 N VAL A 138
SHEET 3 AC 5 GLU A 63 VAL A 68 -1 O GLY A 64 N VAL A 86
SHEET 4 AC 5 ILE A 28 GLY A 36 -1 O LYS A 31 N THR A 67
SHEET 5 AC 5 TYR A 128 VAL A 131 -1 O MET A 129 N LEU A 30
SHEET 1 AD 6 ALA A 219 LYS A 222 0
SHEET 2 AD 6 ARG A 198 ASP A 203 1 O ALA A 201 N VAL A 221
SHEET 3 AD 6 THR A 174 ILE A 178 1 O ALA A 175 N ILE A 200
SHEET 4 AD 6 ALA A 240 ASP A 245 1 O ALA A 242 N VAL A 176
SHEET 5 AD 6 VAL A 260 VAL A 268 1 N ALA A 261 O ALA A 240
SHEET 6 AD 6 SER A 289 VAL A 291 1 O SER A 289 N ILE A 266
SHEET 1 AE 2 ALA A 277 VAL A 279 0
SHEET 2 AE 2 ALA D 277 VAL D 279 -1 O ALA D 277 N VAL A 279
SHEET 1 BA 3 VAL B 14 ASP B 17 0
SHEET 2 BA 3 LYS B 2 TYR B 6 -1 O ALA B 3 N VAL B 16
SHEET 3 BA 3 LEU B 58 THR B 59 -1 O LEU B 58 N TYR B 6
SHEET 1 BB 2 TYR B 128 VAL B 131 0
SHEET 2 BB 2 ILE B 28 GLY B 36 -1 O ILE B 28 N VAL B 131
SHEET 1 BC 6 LEU B 137 PRO B 139 0
SHEET 2 BC 6 ALA B 83 VAL B 86 -1 O ALA B 85 N VAL B 138
SHEET 3 BC 6 GLU B 63 THR B 67 -1 O GLY B 64 N VAL B 86
SHEET 4 BC 6 ILE B 28 GLY B 36 -1 O LYS B 31 N THR B 67
SHEET 5 BC 6 ARG B 340 VAL B 343 -1 O VAL B 343 N ALA B 35
SHEET 6 BC 6 THR B 317 PHE B 320 -1 O GLU B 318 N VAL B 342
SHEET 1 BD 5 LEU B 137 PRO B 139 0
SHEET 2 BD 5 ALA B 83 VAL B 86 -1 O ALA B 85 N VAL B 138
SHEET 3 BD 5 GLU B 63 THR B 67 -1 O GLY B 64 N VAL B 86
SHEET 4 BD 5 ILE B 28 GLY B 36 -1 O LYS B 31 N THR B 67
SHEET 5 BD 5 TYR B 128 VAL B 131 -1 O MET B 129 N LEU B 30
SHEET 1 BE 6 ALA B 219 LYS B 222 0
SHEET 2 BE 6 ARG B 198 ASP B 203 1 O VAL B 199 N ALA B 219
SHEET 3 BE 6 THR B 174 ILE B 178 1 O ALA B 175 N ILE B 200
SHEET 4 BE 6 ALA B 240 ASP B 245 1 N THR B 241 O THR B 174
SHEET 5 BE 6 VAL B 260 VAL B 268 1 N ALA B 261 O ALA B 240
SHEET 6 BE 6 SER B 289 VAL B 291 1 O SER B 289 N ILE B 266
SHEET 1 BF 2 ALA B 277 VAL B 279 0
SHEET 2 BF 2 ALA C 277 VAL C 279 -1 O ALA C 277 N VAL B 279
SHEET 1 CA 3 VAL C 14 ASP C 17 0
SHEET 2 CA 3 LYS C 2 TYR C 6 -1 O ALA C 3 N VAL C 16
SHEET 3 CA 3 LEU C 58 THR C 59 -1 O LEU C 58 N TYR C 6
SHEET 1 CB 2 TYR C 128 VAL C 131 0
SHEET 2 CB 2 ILE C 28 GLY C 36 -1 O ILE C 28 N VAL C 131
SHEET 1 CC 6 LEU C 137 PRO C 139 0
SHEET 2 CC 6 ALA C 83 VAL C 86 -1 O ALA C 85 N VAL C 138
SHEET 3 CC 6 GLU C 63 LEU C 71 -1 O GLY C 64 N VAL C 86
SHEET 4 CC 6 ILE C 28 GLY C 36 -1 O LEU C 29 N ALA C 69
SHEET 5 CC 6 ARG C 340 VAL C 343 -1 O VAL C 343 N ALA C 35
SHEET 6 CC 6 THR C 317 PHE C 320 -1 O GLU C 318 N VAL C 342
SHEET 1 CD 5 LEU C 137 PRO C 139 0
SHEET 2 CD 5 ALA C 83 VAL C 86 -1 O ALA C 85 N VAL C 138
SHEET 3 CD 5 GLU C 63 LEU C 71 -1 O GLY C 64 N VAL C 86
SHEET 4 CD 5 ILE C 28 GLY C 36 -1 O LEU C 29 N ALA C 69
SHEET 5 CD 5 TYR C 128 VAL C 131 -1 O MET C 129 N LEU C 30
SHEET 1 CE 6 ALA C 219 LYS C 222 0
SHEET 2 CE 6 ARG C 198 ASP C 203 1 O ALA C 201 N VAL C 221
SHEET 3 CE 6 THR C 174 ILE C 178 1 O ALA C 175 N ILE C 200
SHEET 4 CE 6 ALA C 240 ASP C 245 1 O ALA C 242 N VAL C 176
SHEET 5 CE 6 VAL C 260 VAL C 268 1 N ALA C 261 O ALA C 240
SHEET 6 CE 6 SER C 289 VAL C 291 1 O SER C 289 N ILE C 266
SHEET 1 DA 3 VAL D 14 ASP D 17 0
SHEET 2 DA 3 LYS D 2 TYR D 6 -1 O ALA D 3 N VAL D 16
SHEET 3 DA 3 LEU D 58 THR D 59 -1 O LEU D 58 N TYR D 6
SHEET 1 DB 2 TYR D 128 VAL D 131 0
SHEET 2 DB 2 ILE D 28 LEU D 37 -1 O ILE D 28 N VAL D 131
SHEET 1 DC 6 LEU D 137 PRO D 139 0
SHEET 2 DC 6 ALA D 83 VAL D 86 -1 O ALA D 85 N VAL D 138
SHEET 3 DC 6 GLU D 63 LEU D 71 -1 O GLY D 64 N VAL D 86
SHEET 4 DC 6 ILE D 28 LEU D 37 -1 O LEU D 29 N ALA D 69
SHEET 5 DC 6 ARG D 340 VAL D 343 -1 O GLY D 341 N LEU D 37
SHEET 6 DC 6 THR D 317 PHE D 320 -1 O GLU D 318 N VAL D 342
SHEET 1 DD 5 LEU D 137 PRO D 139 0
SHEET 2 DD 5 ALA D 83 VAL D 86 -1 O ALA D 85 N VAL D 138
SHEET 3 DD 5 GLU D 63 LEU D 71 -1 O GLY D 64 N VAL D 86
SHEET 4 DD 5 ILE D 28 LEU D 37 -1 O LEU D 29 N ALA D 69
SHEET 5 DD 5 TYR D 128 VAL D 131 -1 O MET D 129 N LEU D 30
SHEET 1 DE 6 ALA D 219 LYS D 222 0
SHEET 2 DE 6 ARG D 198 ASP D 203 1 O VAL D 199 N ALA D 219
SHEET 3 DE 6 THR D 174 ILE D 178 1 O ALA D 175 N ILE D 200
SHEET 4 DE 6 ALA D 240 ASP D 245 1 O ALA D 242 N VAL D 176
SHEET 5 DE 6 VAL D 260 VAL D 268 1 N ALA D 261 O ALA D 240
SHEET 6 DE 6 SER D 289 VAL D 291 1 O SER D 289 N ILE D 266
LINK SG BCYS A 38 ZN ZN A1346 1555 1555 2.52
LINK SG CYS A 92 ZN ZN A1347 1555 1555 2.26
LINK SG CYS A 95 ZN ZN A1347 1555 1555 2.24
LINK SG CYS A 98 ZN ZN A1347 1555 1555 2.16
LINK SG CYS A 106 ZN ZN A1347 1555 1555 2.33
LINK OD2 ASP A 153 ZN ZN A1346 1555 1555 2.17
LINK SG CYS B 38 ZN ZN B1346 1555 1555 2.28
LINK NE2 HIS B 62 ZN ZN B1346 1555 1555 2.17
LINK SG CYS B 92 ZN ZN B1348 1555 1555 2.23
LINK SG CYS B 95 ZN ZN B1348 1555 1555 2.19
LINK SG CYS B 98 ZN ZN B1348 1555 1555 2.43
LINK SG CYS B 106 ZN ZN B1348 1555 1555 2.18
LINK OD2 ASP B 153 ZN ZN B1346 1555 1555 2.00
LINK SG CYS C 38 ZN ZN C1346 1555 1555 2.31
LINK NE2 HIS C 62 ZN ZN C1346 1555 1555 2.12
LINK SG CYS C 92 ZN ZN C1347 1555 1555 2.27
LINK SG CYS C 95 ZN ZN C1347 1555 1555 2.23
LINK SG CYS C 98 ZN ZN C1347 1555 1555 2.22
LINK SG CYS C 106 ZN ZN C1347 1555 1555 2.37
LINK OD2 ASP C 153 ZN ZN C1346 1555 1555 1.71
LINK SG CYS D 38 ZN ZN D1346 1555 1555 2.23
LINK NE2 HIS D 62 ZN ZN D1346 1555 1555 2.07
LINK SG CYS D 92 ZN ZN D1348 1555 1555 2.41
LINK SG CYS D 95 ZN ZN D1348 1555 1555 2.43
LINK SG CYS D 98 ZN ZN D1348 1555 1555 2.24
LINK SG CYS D 106 ZN ZN D1348 1555 1555 2.36
LINK OD2 ASP D 153 ZN ZN D1346 1555 1555 1.95
LINK ZN ZN D1346 O6 BU1 D1347 1555 1555 2.32
CISPEP 1 LEU A 56 PRO A 57 0 10.21
CISPEP 2 LEU B 56 PRO B 57 0 -3.26
CISPEP 3 LEU C 56 PRO C 57 0 -3.23
CISPEP 4 LEU D 56 PRO D 57 0 1.13
SITE 1 AC1 5 CYS A 38 SER A 40 HIS A 62 ASP A 153
SITE 2 AC1 5 NAD A 503
SITE 1 AC2 4 CYS A 92 CYS A 95 CYS A 98 CYS A 106
SITE 1 AC3 23 CYS A 38 HIS A 39 SER A 40 ASP A 153
SITE 2 AC3 23 THR A 157 GLY A 181 GLY A 182 LEU A 183
SITE 3 AC3 23 ASP A 203 LEU A 204 ARG A 208 SER A 223
SITE 4 AC3 23 PHE A 246 VAL A 247 VAL A 269 ILE A 271
SITE 5 AC3 23 PRO A 293 TYR A 294 TRP A 295 ARG A 340
SITE 6 AC3 23 ZN A1346 HOH A2010 PHE D 281
SITE 1 AC4 6 CYS B 38 SER B 40 HIS B 62 ASP B 153
SITE 2 AC4 6 NAD B 503 BU1 B1347
SITE 1 AC5 4 SER B 40 ILE B 271 NAD B 503 ZN B1346
SITE 1 AC6 4 CYS B 92 CYS B 95 CYS B 98 CYS B 106
SITE 1 AC7 28 HIS B 39 SER B 40 ASP B 153 THR B 157
SITE 2 AC7 28 GLY B 179 VAL B 180 GLY B 181 GLY B 182
SITE 3 AC7 28 LEU B 183 ASP B 203 LEU B 204 ARG B 208
SITE 4 AC7 28 SER B 223 PHE B 246 VAL B 247 THR B 252
SITE 5 AC7 28 VAL B 269 GLY B 270 ILE B 271 PRO B 293
SITE 6 AC7 28 TYR B 294 TRP B 295 LEU B 332 ARG B 340
SITE 7 AC7 28 ZN B1346 BU1 B1347 HOH B2039 PHE C 281
SITE 1 AC8 6 CYS C 38 SER C 40 HIS C 62 ASP C 153
SITE 2 AC8 6 NAD C 503 BU1 C1348
SITE 1 AC9 4 CYS C 92 CYS C 95 CYS C 98 CYS C 106
SITE 1 BC1 29 PHE B 281 HIS C 39 SER C 40 ASP C 153
SITE 2 BC1 29 THR C 157 ILE C 178 GLY C 179 VAL C 180
SITE 3 BC1 29 GLY C 181 GLY C 182 LEU C 183 VAL C 202
SITE 4 BC1 29 ASP C 203 LEU C 204 ARG C 208 SER C 223
SITE 5 BC1 29 PHE C 246 VAL C 247 VAL C 269 GLY C 270
SITE 6 BC1 29 ILE C 271 PRO C 293 TYR C 294 TRP C 295
SITE 7 BC1 29 LEU C 332 ARG C 340 ZN C1346 BU1 C1348
SITE 8 BC1 29 HOH C2038
SITE 1 BC2 6 CYS D 38 SER D 40 HIS D 62 ASP D 153
SITE 2 BC2 6 NAD D 503 BU1 D1347
SITE 1 BC3 5 SER D 40 HIS D 62 ASP D 153 NAD D 503
SITE 2 BC3 5 ZN D1346
SITE 1 BC4 4 CYS D 92 CYS D 95 CYS D 98 CYS D 106
SITE 1 BC5 27 HIS D 39 SER D 40 ASP D 153 GLY D 179
SITE 2 BC5 27 VAL D 180 GLY D 181 GLY D 182 LEU D 183
SITE 3 BC5 27 ASP D 203 LEU D 204 ARG D 208 SER D 223
SITE 4 BC5 27 PHE D 246 VAL D 247 VAL D 269 GLY D 270
SITE 5 BC5 27 ILE D 271 PRO D 293 TYR D 294 TRP D 295
SITE 6 BC5 27 ARG D 340 ZN D1346 BU1 D1347 HOH D2015
SITE 7 BC5 27 HOH D2020 HOH D2036 HOH D2037
SITE 1 BC6 4 SER C 40 ILE C 271 NAD C 503 ZN C1346
CRYST1 65.674 105.100 109.176 90.00 91.27 90.00 P 1 21 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 0.015227 0.000000 0.000338 0.00000
SCALE2 0.000000 0.009515 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009162 0.00000
MTRIX1 1 0.982000 -0.158500 0.103100 -2.51800 1
MTRIX2 1 -0.157000 -0.987300 -0.023000 1.59200 1
MTRIX3 1 0.105400 0.006406 -0.994400 51.24000 1
MTRIX1 2 -0.982200 0.153100 -0.108500 31.02000 1
MTRIX2 2 0.155700 0.342000 -0.926700 21.83000 1
MTRIX3 2 -0.104800 -0.927100 -0.359800 36.94000 1
MTRIX1 3 -1.000000 -0.002726 0.004900 28.23000 1
MTRIX2 3 0.005550 -0.356100 0.934400 -25.58000 1
MTRIX3 3 0.000802 0.934400 0.356100 17.63000 1
(ATOM LINES ARE NOT SHOWN.)
END