HEADER OXIDOREDUCTASE 22-JUL-15 5A9S
TITLE NADPH COMPLEX OF IMINE REDUCTASE FROM AMYCOLATOPSIS ORIENTALIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMINE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.5.1.48;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: IMINE REDUCTASE;
COMPND 8 CHAIN: B;
COMPND 9 EC: 1.5.1.48;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AMYCOLATOPSIS ORIENTALIS;
SOURCE 3 ORGANISM_TAXID: 31958;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PETYSBLIC-3C;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: AMYCOLATOPSIS ORIENTALIS;
SOURCE 11 ORGANISM_TAXID: 31958;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PETYSBLIC-3C
KEYWDS OXIDOREDUCTASE, IMINE REDUCTASE, NADPH, AMINE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MAN,G.ALEKU,N.J.TURNER,G.GROGAN
REVDAT 3 10-JAN-24 5A9S 1 REMARK LINK
REVDAT 2 25-APR-18 5A9S 1 JRNL REMARK
REVDAT 1 01-JUN-16 5A9S 0
JRNL AUTH G.A.ALEKU,H.MAN,S.P.FRANCE,F.LEIPOLD,S.HUSSAIN,
JRNL AUTH 2 L.TOCA-GONZALEZ,R.MARCHINGTON,S.HART,J.P.TURKENBURG,
JRNL AUTH 3 G.GROGAN,N.J.TURNER
JRNL TITL STEREOSELECTIVITY AND STRUCTURAL CHARACTERIZATION OF AN
JRNL TITL 2 IMINE REDUCTASE (IRED) FROM AMYCOLATOPSIS ORIENTALIS
JRNL REF ACS CATALYSIS V. 6 3880 2016
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.6B00782
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0124
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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 31173
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1597
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) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.11
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2281
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4068
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.21000
REMARK 3 B22 (A**2) : -0.52000
REMARK 3 B33 (A**2) : 2.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.175
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.113
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4224 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4003 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5783 ; 1.867 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9176 ; 1.544 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 566 ; 6.156 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 149 ;36.650 ;24.161
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 607 ;16.865 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;19.430 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 682 ; 0.124 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4828 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 900 ; 0.006 ; 0.020
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): 2252 ; 2.993 ; 3.267
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2251 ; 2.993 ; 3.266
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2807 ; 4.183 ; 4.879
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1972 ; 4.185 ; 3.820
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 : 1.20
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.
REMARK 4
REMARK 4 5A9S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1290064467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97935
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32831
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 49.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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 3ZGY
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 0.1 M TRIS PH
REMARK 280 9.0, 8% (W/V) PEG 550 MME, 8% (W/V) PEG 20K WITH PROTEIN AT A
REMARK 280 CONCENTRATION OF 20 MG PER ML, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.39500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.94000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.03000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.94000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.39500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.03000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MET A 1
REMARK 465 TYR A 72
REMARK 465 ASP A 73
REMARK 465 ALA A 74
REMARK 465 GLU A 228
REMARK 465 GLY A 229
REMARK 465 VAL A 230
REMARK 465 TYR A 231
REMARK 465 PRO A 232
REMARK 465 GLY A 233
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASP B 3
REMARK 465 GLN B 4
REMARK 465 TYR B 72
REMARK 465 GLU B 228
REMARK 465 GLY B 229
REMARK 465 VAL B 230
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 47 CE NZ
REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 83 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 84 CD OE1 OE2
REMARK 470 LYS A 100 NZ
REMARK 470 ARG A 107 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 239 CG CD OE1 OE2
REMARK 470 GLU A 279 CG CD OE1 OE2
REMARK 470 ASN B 5 CG OD1 ND2
REMARK 470 LEU B 6 CG CD1 CD2
REMARK 470 LYS B 40 CE NZ
REMARK 470 ARG B 50 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 53 CG OD1 OD2
REMARK 470 ARG B 63 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 87 CD NE CZ NH1 NH2
REMARK 470 LYS B 100 CG CD CE NZ
REMARK 470 LYS B 148 CD CE NZ
REMARK 470 GLU B 149 CG CD OE1 OE2
REMARK 470 ASP B 227 CG OD1 OD2
REMARK 470 GLU B 239 CG CD OE1 OE2
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 OG SER A 140 OE2 GLU A 201 1455 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET B 127 CG - SD - CE ANGL. DEV. = 11.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 6 126.02 -38.10
REMARK 500 ASN A 95 43.45 -143.28
REMARK 500 SER A 140 124.93 -38.35
REMARK 500 GLU A 279 -16.51 68.19
REMARK 500 LEU B 6 70.37 43.45
REMARK 500 ARG B 83 -119.38 43.97
REMARK 500 SER B 96 139.26 -29.59
REMARK 500 PRO B 232 66.61 -116.37
REMARK 500 ASP B 234 147.69 -170.77
REMARK 500 VAL B 285 -38.32 -39.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 500 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 220 O
REMARK 620 2 ALA A 221 O 85.3
REMARK 620 3 ALA A 223 O 100.1 105.7
REMARK 620 4 ILE A 226 O 99.1 156.3 96.5
REMARK 620 5 HOH A2061 O 162.8 79.3 91.6 92.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 500 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 220 O
REMARK 620 2 ALA B 221 O 81.2
REMARK 620 3 ALA B 223 O 93.5 102.3
REMARK 620 4 ILE B 226 O 97.7 161.9 95.8
REMARK 620 5 HOH B2048 O 93.5 83.4 171.6 78.6
REMARK 620 6 HOH B2049 O 165.3 84.1 89.0 96.5 85.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A9R RELATED DB: PDB
REMARK 900 APO FORM OF IMINE REDUCTASE FROM AMYCOLATOPSIS ORIENTALIS
REMARK 900 RELATED ID: 5A9T RELATED DB: PDB
REMARK 900 IMINE REDUCTASE FROM AMYCOLATOPSIS ORIENTALIS IN COMPLEX WITH (R)-
REMARK 900 METHYLTETRAHYDROISOQUINOLINE
DBREF 5A9S A 1 290 UNP R4SNK4 R4SNK4_AMYOR 1 290
DBREF 5A9S B 1 290 UNP R4SNK4 R4SNK4_AMYOR 1 290
SEQADV 5A9S GLN B 222 UNP R4SNK4 GLU 222 CONFLICT
SEQRES 1 A 290 MET THR ASP GLN ASN LEU PRO VAL THR VAL ALA GLY LEU
SEQRES 2 A 290 GLY PRO MET GLY SER ALA LEU ALA ALA ALA LEU LEU ASP
SEQRES 3 A 290 ARG GLY HIS ASP VAL THR VAL TRP ASN ARG SER PRO GLY
SEQRES 4 A 290 LYS ALA ALA PRO LEU VAL ALA LYS GLY ALA ARG GLN ALA
SEQRES 5 A 290 ASP ASP ILE VAL ASP ALA VAL SER ALA SER ARG LEU LEU
SEQRES 6 A 290 VAL VAL CYS LEU ALA ASP TYR ASP ALA LEU TYR SER ALA
SEQRES 7 A 290 LEU GLY PRO ALA ARG GLU ALA LEU ARG GLY ARG VAL VAL
SEQRES 8 A 290 VAL ASN LEU ASN SER GLY THR PRO LYS GLU ALA ASN GLU
SEQRES 9 A 290 ALA LEU ARG TRP ALA GLU ARG HIS GLY THR GLY TYR LEU
SEQRES 10 A 290 ASP GLY ALA ILE MET VAL PRO PRO ALA MET VAL GLY HIS
SEQRES 11 A 290 PRO GLY SER VAL PHE LEU TYR SER GLY SER ALA GLU VAL
SEQRES 12 A 290 PHE GLU GLU TYR LYS GLU THR LEU ALA GLY LEU GLY ASP
SEQRES 13 A 290 PRO VAL HIS LEU GLY THR GLU ALA GLY LEU ALA VAL LEU
SEQRES 14 A 290 TYR ASN THR ALA LEU LEU SER MET MET TYR SER SER MET
SEQRES 15 A 290 ASN GLY PHE LEU HIS ALA ALA ALA LEU VAL GLY SER ALA
SEQRES 16 A 290 GLY VAL PRO ALA ALA GLU PHE THR LYS LEU ALA VAL ASP
SEQRES 17 A 290 TRP PHE LEU PRO ALA VAL ILE GLY GLN ILE ILE LYS ALA
SEQRES 18 A 290 GLU ALA PRO THR ILE ASP GLU GLY VAL TYR PRO GLY ASP
SEQRES 19 A 290 ALA GLY SER LEU GLU MET ASN VAL THR THR LEU LYS HIS
SEQRES 20 A 290 ILE ILE GLY THR SER GLN GLU GLN GLY VAL ASP THR GLU
SEQRES 21 A 290 ILE PRO VAL ARG ASN LYS GLU LEU LEU ASP ARG ALA VAL
SEQRES 22 A 290 ALA ALA GLY PHE GLY GLU SER SER TYR TYR SER VAL ILE
SEQRES 23 A 290 GLU LEU TRP ARG
SEQRES 1 B 290 MET THR ASP GLN ASN LEU PRO VAL THR VAL ALA GLY LEU
SEQRES 2 B 290 GLY PRO MET GLY SER ALA LEU ALA ALA ALA LEU LEU ASP
SEQRES 3 B 290 ARG GLY HIS ASP VAL THR VAL TRP ASN ARG SER PRO GLY
SEQRES 4 B 290 LYS ALA ALA PRO LEU VAL ALA LYS GLY ALA ARG GLN ALA
SEQRES 5 B 290 ASP ASP ILE VAL ASP ALA VAL SER ALA SER ARG LEU LEU
SEQRES 6 B 290 VAL VAL CYS LEU ALA ASP TYR ASP ALA LEU TYR SER ALA
SEQRES 7 B 290 LEU GLY PRO ALA ARG GLU ALA LEU ARG GLY ARG VAL VAL
SEQRES 8 B 290 VAL ASN LEU ASN SER GLY THR PRO LYS GLU ALA ASN GLU
SEQRES 9 B 290 ALA LEU ARG TRP ALA GLU ARG HIS GLY THR GLY TYR LEU
SEQRES 10 B 290 ASP GLY ALA ILE MET VAL PRO PRO ALA MET VAL GLY HIS
SEQRES 11 B 290 PRO GLY SER VAL PHE LEU TYR SER GLY SER ALA GLU VAL
SEQRES 12 B 290 PHE GLU GLU TYR LYS GLU THR LEU ALA GLY LEU GLY ASP
SEQRES 13 B 290 PRO VAL HIS LEU GLY THR GLU ALA GLY LEU ALA VAL LEU
SEQRES 14 B 290 TYR ASN THR ALA LEU LEU SER MET MET TYR SER SER MET
SEQRES 15 B 290 ASN GLY PHE LEU HIS ALA ALA ALA LEU VAL GLY SER ALA
SEQRES 16 B 290 GLY VAL PRO ALA ALA GLU PHE THR LYS LEU ALA VAL ASP
SEQRES 17 B 290 TRP PHE LEU PRO ALA VAL ILE GLY GLN ILE ILE LYS ALA
SEQRES 18 B 290 GLN ALA PRO THR ILE ASP GLU GLY VAL TYR PRO GLY ASP
SEQRES 19 B 290 ALA GLY SER LEU GLU MET ASN VAL THR THR LEU LYS HIS
SEQRES 20 B 290 ILE ILE GLY THR SER GLN GLU GLN GLY VAL ASP THR GLU
SEQRES 21 B 290 ILE PRO VAL ARG ASN LYS GLU LEU LEU ASP ARG ALA VAL
SEQRES 22 B 290 ALA ALA GLY PHE GLY GLU SER SER TYR TYR SER VAL ILE
SEQRES 23 B 290 GLU LEU TRP ARG
HET CA A 500 1
HET NAP A1000 48
HET CA B 500 1
HETNAM CA CALCIUM ION
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 CA 2(CA 2+)
FORMUL 4 NAP C21 H28 N7 O17 P3
FORMUL 6 HOH *143(H2 O)
HELIX 1 1 GLY A 14 ARG A 27 1 14
HELIX 2 2 ALA A 41 LYS A 47 1 7
HELIX 3 3 ASP A 54 ALA A 61 1 8
HELIX 4 4 LEU A 75 GLY A 80 1 6
HELIX 5 5 PRO A 81 ARG A 87 5 7
HELIX 6 6 THR A 98 HIS A 112 1 15
HELIX 7 7 PRO A 124 VAL A 128 5 5
HELIX 8 8 SER A 140 GLY A 153 1 14
HELIX 9 9 GLY A 165 SER A 194 1 30
HELIX 10 10 PRO A 198 TRP A 209 1 12
HELIX 11 11 TRP A 209 VAL A 214 1 6
HELIX 12 12 VAL A 214 ALA A 223 1 10
HELIX 13 13 SER A 237 GLY A 256 1 20
HELIX 14 14 THR A 259 ALA A 275 1 17
HELIX 15 15 SER A 281 ARG A 290 5 10
HELIX 16 16 GLY B 14 ARG B 27 1 14
HELIX 17 17 SER B 37 LYS B 40 5 4
HELIX 18 18 ALA B 41 LYS B 47 1 7
HELIX 19 19 ASP B 54 ALA B 61 1 8
HELIX 20 20 ASP B 73 GLY B 80 1 8
HELIX 21 21 PRO B 81 ARG B 87 5 7
HELIX 22 22 THR B 98 HIS B 112 1 15
HELIX 23 23 PRO B 124 VAL B 128 5 5
HELIX 24 24 SER B 140 GLY B 153 1 14
HELIX 25 25 GLY B 165 SER B 194 1 30
HELIX 26 26 PRO B 198 TRP B 209 1 12
HELIX 27 27 TRP B 209 VAL B 214 1 6
HELIX 28 28 VAL B 214 ALA B 223 1 10
HELIX 29 29 SER B 237 GLY B 256 1 20
HELIX 30 30 THR B 259 GLY B 276 1 18
HELIX 31 31 SER B 281 ARG B 290 5 10
SHEET 1 AA 8 ARG A 50 GLN A 51 0
SHEET 2 AA 8 VAL A 31 TRP A 34 1 O VAL A 31 N ARG A 50
SHEET 3 AA 8 VAL A 8 ALA A 11 1 O VAL A 8 N THR A 32
SHEET 4 AA 8 LEU A 64 VAL A 67 1 O LEU A 64 N THR A 9
SHEET 5 AA 8 VAL A 90 ASN A 93 1 O VAL A 90 N LEU A 65
SHEET 6 AA 8 GLY A 115 ILE A 121 1 O GLY A 115 N VAL A 91
SHEET 7 AA 8 VAL A 134 GLY A 139 -1 O LEU A 136 N ALA A 120
SHEET 8 AA 8 ASP A 156 HIS A 159 1 O ASP A 156 N PHE A 135
SHEET 1 BA 8 ARG B 50 GLN B 51 0
SHEET 2 BA 8 VAL B 31 TRP B 34 1 O VAL B 31 N ARG B 50
SHEET 3 BA 8 VAL B 8 ALA B 11 1 O VAL B 8 N THR B 32
SHEET 4 BA 8 LEU B 64 VAL B 67 1 O LEU B 64 N THR B 9
SHEET 5 BA 8 VAL B 90 ASN B 93 1 O VAL B 90 N LEU B 65
SHEET 6 BA 8 GLY B 115 ILE B 121 1 O GLY B 115 N VAL B 91
SHEET 7 BA 8 VAL B 134 GLY B 139 -1 O LEU B 136 N ALA B 120
SHEET 8 BA 8 ASP B 156 HIS B 159 1 O ASP B 156 N PHE B 135
LINK O LYS A 220 CA CA A 500 1555 1555 2.46
LINK O ALA A 221 CA CA A 500 1555 1555 2.52
LINK O ALA A 223 CA CA A 500 1555 1555 2.31
LINK O ILE A 226 CA CA A 500 1555 1555 2.34
LINK CA CA A 500 O HOH A2061 1555 1555 2.57
LINK O LYS B 220 CA CA B 500 1555 1555 2.63
LINK O ALA B 221 CA CA B 500 1555 1555 2.58
LINK O ALA B 223 CA CA B 500 1555 1555 2.41
LINK O ILE B 226 CA CA B 500 1555 1555 2.29
LINK CA CA B 500 O HOH B2048 1555 1555 2.76
LINK CA CA B 500 O HOH B2049 1555 1555 2.66
CISPEP 1 PRO B 232 GLY B 233 0 0.76
SITE 1 AC1 21 GLY A 12 LEU A 13 GLY A 14 PRO A 15
SITE 2 AC1 21 MET A 16 GLY A 17 ASN A 35 ARG A 36
SITE 3 AC1 21 SER A 37 LYS A 40 CYS A 68 LEU A 69
SITE 4 AC1 21 ALA A 70 ASN A 95 ILE A 121 VAL A 123
SITE 5 AC1 21 PRO A 125 HOH A2012 HOH A2018 HOH A2020
SITE 6 AC1 21 MET B 240
SITE 1 AC2 6 LYS B 220 ALA B 221 ALA B 223 ILE B 226
SITE 2 AC2 6 HOH B2048 HOH B2049
SITE 1 AC3 5 LYS A 220 ALA A 221 ALA A 223 ILE A 226
SITE 2 AC3 5 HOH A2061
CRYST1 52.790 66.060 147.880 90.00 90.00 90.00 P 21 21 21 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 0.018943 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015138 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006762 0.00000
MTRIX1 1 -0.999900 0.009316 -0.009296 91.78000
MTRIX2 1 0.000091 -0.701400 -0.712700 20.87000
MTRIX3 1 -0.013160 -0.712700 0.701400 9.24900
(ATOM LINES ARE NOT SHOWN.)
END
