HEADER OXIDOREDUCTASE/INHIBITOR 03-JUN-13 4L1O
TITLE CRYSTAL STRUCTURE OF HUMAN ALDH3A1 WITH INHIBITOR 1-{[4-(1,3-
TITLE 2 BENZODIOXOL-5-YLMETHYL)PIPERAZIN-1-YL]METHYL}-1H-INDOLE-2,3-DIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDEHYDE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALDHIII, ALDEHYDE DEHYDROGENASE 3, ALDEHYDE DEHYDROGENASE
COMPND 5 FAMILY 3 MEMBER A1;
COMPND 6 EC: 1.2.1.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALDH3, ALDH3A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CATALYZES BENZALDEHYDE, ROSSMANN FOLD, DEHYDROGENASE, NADP+ BINDING,
KEYWDS 2 OXIDOREDUCTASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.D.HURLEY,B.PARAJULI
REVDAT 4 20-SEP-23 4L1O 1 REMARK
REVDAT 3 21-DEC-22 4L1O 1 REMARK SEQADV LINK
REVDAT 2 12-NOV-14 4L1O 1 KEYWDS
REVDAT 1 16-APR-14 4L1O 0
JRNL AUTH B.PARAJULI,A.KIMBLE-HILL,C.H.CHEN,D.MOCHLY-ROSEN,T.D.HURLEY
JRNL TITL DISCOVERY OF INDOLE-2,3-DIONES AS NOVEL CLASS OF INHIBITORS
JRNL TITL 2 FOR ALDH ISOZYMES.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 37399
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1990
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2529
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7019
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 648
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.88000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : 0.50000
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): 0.483
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.245
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.435
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7366 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7128 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10011 ; 1.089 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16468 ; 0.724 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 937 ; 5.494 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 317 ;37.161 ;24.479
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1297 ;12.650 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;10.917 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1116 ; 0.056 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8349 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1613 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 4L1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080068.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC CONFOCAL BLUE
REMARK 200 OPTICS : OSMIC CONFOCAL BLUE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37399
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.14600
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.14600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3SZA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM ACETATE, 20% PEG 3350,
REMARK 280 (3 MICROLITRES OF 3MG/ML OF ALDH3A1+ 3 MICROLITRES OF MOTHER
REMARK 280 LIQUOR), PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298.15K
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 30.62850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.11250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.19800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.11250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.62850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.19800
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: 9520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 LYS A 448
REMARK 465 MET A 449
REMARK 465 THR A 450
REMARK 465 GLN A 451
REMARK 465 HIS A 452
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
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 GLU A 62 -66.72 -155.31
REMARK 500 LEU A 210 -154.01 -117.92
REMARK 500 ILE A 391 -52.76 71.47
REMARK 500 HIS A 413 128.59 90.50
REMARK 500 GLU B 62 -69.11 -157.33
REMARK 500 LEU B 210 -165.80 -111.70
REMARK 500 ILE B 391 -54.76 71.93
REMARK 500 HIS B 413 137.83 90.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1VL A 601
REMARK 610 1VL B 601
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 K A 602 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 321 O
REMARK 620 2 ASP A 322 O 64.6
REMARK 620 3 HOH A 715 O 54.4 100.5
REMARK 620 4 HOH A 821 O 106.7 80.0 74.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 439 O
REMARK 620 2 TYR A 442 O 82.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 602 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 79 O
REMARK 620 2 TRP B 80 O 70.8
REMARK 620 3 ALA B 82 O 93.5 76.0
REMARK 620 4 HOH B 893 O 145.3 78.8 95.0
REMARK 620 5 HOH B 991 O 77.4 98.5 170.6 91.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 439 O
REMARK 620 2 TYR B 442 O 91.5
REMARK 620 3 HOH B 829 O 161.3 96.4
REMARK 620 4 HOH B 854 O 111.8 80.2 86.3
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 1VL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1VL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SZA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ALDH3A1-APO FORM
REMARK 900 RELATED ID: 3SZB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ALDH3A1 MODIFIED WITH THE BETA
REMARK 900 ELIMINATION PRODUCT OF ALDI-1; 1-PHENYL-2-PROPEN-1-ONE
REMARK 900 RELATED ID: 4L2O RELATED DB: PDB
DBREF 4L1O A 0 452 UNP P30838 AL3A1_HUMAN 1 453
DBREF 4L1O B 0 452 UNP P30838 AL3A1_HUMAN 1 453
SEQADV 4L1O HIS A -16 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS A -15 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS A -14 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS A -13 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS A -12 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS A -11 UNP P30838 EXPRESSION TAG
SEQADV 4L1O SER A -10 UNP P30838 EXPRESSION TAG
SEQADV 4L1O SER A -9 UNP P30838 EXPRESSION TAG
SEQADV 4L1O GLY A -8 UNP P30838 EXPRESSION TAG
SEQADV 4L1O LEU A -7 UNP P30838 EXPRESSION TAG
SEQADV 4L1O VAL A -6 UNP P30838 EXPRESSION TAG
SEQADV 4L1O PRO A -5 UNP P30838 EXPRESSION TAG
SEQADV 4L1O ARG A -4 UNP P30838 EXPRESSION TAG
SEQADV 4L1O GLY A -3 UNP P30838 EXPRESSION TAG
SEQADV 4L1O SER A -2 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS A -1 UNP P30838 EXPRESSION TAG
SEQADV 4L1O ALA A 133 UNP P30838 SER 134 VARIANT
SEQADV 4L1O HIS B -16 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS B -15 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS B -14 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS B -13 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS B -12 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS B -11 UNP P30838 EXPRESSION TAG
SEQADV 4L1O SER B -10 UNP P30838 EXPRESSION TAG
SEQADV 4L1O SER B -9 UNP P30838 EXPRESSION TAG
SEQADV 4L1O GLY B -8 UNP P30838 EXPRESSION TAG
SEQADV 4L1O LEU B -7 UNP P30838 EXPRESSION TAG
SEQADV 4L1O VAL B -6 UNP P30838 EXPRESSION TAG
SEQADV 4L1O PRO B -5 UNP P30838 EXPRESSION TAG
SEQADV 4L1O ARG B -4 UNP P30838 EXPRESSION TAG
SEQADV 4L1O GLY B -3 UNP P30838 EXPRESSION TAG
SEQADV 4L1O SER B -2 UNP P30838 EXPRESSION TAG
SEQADV 4L1O HIS B -1 UNP P30838 EXPRESSION TAG
SEQADV 4L1O ALA B 133 UNP P30838 SER 134 VARIANT
SEQRES 1 A 469 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 469 GLY SER HIS MET SER LYS ILE SER GLU ALA VAL LYS ARG
SEQRES 3 A 469 ALA ARG ALA ALA PHE SER SER GLY ARG THR ARG PRO LEU
SEQRES 4 A 469 GLN PHE ARG ILE GLN GLN LEU GLU ALA LEU GLN ARG LEU
SEQRES 5 A 469 ILE GLN GLU GLN GLU GLN GLU LEU VAL GLY ALA LEU ALA
SEQRES 6 A 469 ALA ASP LEU HIS LYS ASN GLU TRP ASN ALA TYR TYR GLU
SEQRES 7 A 469 GLU VAL VAL TYR VAL LEU GLU GLU ILE GLU TYR MET ILE
SEQRES 8 A 469 GLN LYS LEU PRO GLU TRP ALA ALA ASP GLU PRO VAL GLU
SEQRES 9 A 469 LYS THR PRO GLN THR GLN GLN ASP GLU LEU TYR ILE HIS
SEQRES 10 A 469 SER GLU PRO LEU GLY VAL VAL LEU VAL ILE GLY THR TRP
SEQRES 11 A 469 ASN TYR PRO PHE ASN LEU THR ILE GLN PRO MET VAL GLY
SEQRES 12 A 469 ALA ILE ALA ALA GLY ASN ALA VAL VAL LEU LYS PRO SER
SEQRES 13 A 469 GLU LEU SER GLU ASN MET ALA SER LEU LEU ALA THR ILE
SEQRES 14 A 469 ILE PRO GLN TYR LEU ASP LYS ASP LEU TYR PRO VAL ILE
SEQRES 15 A 469 ASN GLY GLY VAL PRO GLU THR THR GLU LEU LEU LYS GLU
SEQRES 16 A 469 ARG PHE ASP HIS ILE LEU TYR THR GLY SER THR GLY VAL
SEQRES 17 A 469 GLY LYS ILE ILE MET THR ALA ALA ALA LYS HIS LEU THR
SEQRES 18 A 469 PRO VAL THR LEU GLU LEU GLY GLY LYS SER PRO CYS TYR
SEQRES 19 A 469 VAL ASP LYS ASN CYS ASP LEU ASP VAL ALA CYS ARG ARG
SEQRES 20 A 469 ILE ALA TRP GLY LYS PHE MET ASN SER GLY GLN THR CYS
SEQRES 21 A 469 VAL ALA PRO ASP TYR ILE LEU CYS ASP PRO SER ILE GLN
SEQRES 22 A 469 ASN GLN ILE VAL GLU LYS LEU LYS LYS SER LEU LYS GLU
SEQRES 23 A 469 PHE TYR GLY GLU ASP ALA LYS LYS SER ARG ASP TYR GLY
SEQRES 24 A 469 ARG ILE ILE SER ALA ARG HIS PHE GLN ARG VAL MET GLY
SEQRES 25 A 469 LEU ILE GLU GLY GLN LYS VAL ALA TYR GLY GLY THR GLY
SEQRES 26 A 469 ASP ALA ALA THR ARG TYR ILE ALA PRO THR ILE LEU THR
SEQRES 27 A 469 ASP VAL ASP PRO GLN SER PRO VAL MET GLN GLU GLU ILE
SEQRES 28 A 469 PHE GLY PRO VAL LEU PRO ILE VAL CYS VAL ARG SER LEU
SEQRES 29 A 469 GLU GLU ALA ILE GLN PHE ILE ASN GLN ARG GLU LYS PRO
SEQRES 30 A 469 LEU ALA LEU TYR MET PHE SER SER ASN ASP LYS VAL ILE
SEQRES 31 A 469 LYS LYS MET ILE ALA GLU THR SER SER GLY GLY VAL ALA
SEQRES 32 A 469 ALA ASN ASP VAL ILE VAL HIS ILE THR LEU HIS SER LEU
SEQRES 33 A 469 PRO PHE GLY GLY VAL GLY ASN SER GLY MET GLY SER TYR
SEQRES 34 A 469 HIS GLY LYS LYS SER PHE GLU THR PHE SER HIS ARG ARG
SEQRES 35 A 469 SER CYS LEU VAL ARG PRO LEU MET ASN ASP GLU GLY LEU
SEQRES 36 A 469 LYS VAL ARG TYR PRO PRO SER PRO ALA LYS MET THR GLN
SEQRES 37 A 469 HIS
SEQRES 1 B 469 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 B 469 GLY SER HIS MET SER LYS ILE SER GLU ALA VAL LYS ARG
SEQRES 3 B 469 ALA ARG ALA ALA PHE SER SER GLY ARG THR ARG PRO LEU
SEQRES 4 B 469 GLN PHE ARG ILE GLN GLN LEU GLU ALA LEU GLN ARG LEU
SEQRES 5 B 469 ILE GLN GLU GLN GLU GLN GLU LEU VAL GLY ALA LEU ALA
SEQRES 6 B 469 ALA ASP LEU HIS LYS ASN GLU TRP ASN ALA TYR TYR GLU
SEQRES 7 B 469 GLU VAL VAL TYR VAL LEU GLU GLU ILE GLU TYR MET ILE
SEQRES 8 B 469 GLN LYS LEU PRO GLU TRP ALA ALA ASP GLU PRO VAL GLU
SEQRES 9 B 469 LYS THR PRO GLN THR GLN GLN ASP GLU LEU TYR ILE HIS
SEQRES 10 B 469 SER GLU PRO LEU GLY VAL VAL LEU VAL ILE GLY THR TRP
SEQRES 11 B 469 ASN TYR PRO PHE ASN LEU THR ILE GLN PRO MET VAL GLY
SEQRES 12 B 469 ALA ILE ALA ALA GLY ASN ALA VAL VAL LEU LYS PRO SER
SEQRES 13 B 469 GLU LEU SER GLU ASN MET ALA SER LEU LEU ALA THR ILE
SEQRES 14 B 469 ILE PRO GLN TYR LEU ASP LYS ASP LEU TYR PRO VAL ILE
SEQRES 15 B 469 ASN GLY GLY VAL PRO GLU THR THR GLU LEU LEU LYS GLU
SEQRES 16 B 469 ARG PHE ASP HIS ILE LEU TYR THR GLY SER THR GLY VAL
SEQRES 17 B 469 GLY LYS ILE ILE MET THR ALA ALA ALA LYS HIS LEU THR
SEQRES 18 B 469 PRO VAL THR LEU GLU LEU GLY GLY LYS SER PRO CYS TYR
SEQRES 19 B 469 VAL ASP LYS ASN CYS ASP LEU ASP VAL ALA CYS ARG ARG
SEQRES 20 B 469 ILE ALA TRP GLY LYS PHE MET ASN SER GLY GLN THR CYS
SEQRES 21 B 469 VAL ALA PRO ASP TYR ILE LEU CYS ASP PRO SER ILE GLN
SEQRES 22 B 469 ASN GLN ILE VAL GLU LYS LEU LYS LYS SER LEU LYS GLU
SEQRES 23 B 469 PHE TYR GLY GLU ASP ALA LYS LYS SER ARG ASP TYR GLY
SEQRES 24 B 469 ARG ILE ILE SER ALA ARG HIS PHE GLN ARG VAL MET GLY
SEQRES 25 B 469 LEU ILE GLU GLY GLN LYS VAL ALA TYR GLY GLY THR GLY
SEQRES 26 B 469 ASP ALA ALA THR ARG TYR ILE ALA PRO THR ILE LEU THR
SEQRES 27 B 469 ASP VAL ASP PRO GLN SER PRO VAL MET GLN GLU GLU ILE
SEQRES 28 B 469 PHE GLY PRO VAL LEU PRO ILE VAL CYS VAL ARG SER LEU
SEQRES 29 B 469 GLU GLU ALA ILE GLN PHE ILE ASN GLN ARG GLU LYS PRO
SEQRES 30 B 469 LEU ALA LEU TYR MET PHE SER SER ASN ASP LYS VAL ILE
SEQRES 31 B 469 LYS LYS MET ILE ALA GLU THR SER SER GLY GLY VAL ALA
SEQRES 32 B 469 ALA ASN ASP VAL ILE VAL HIS ILE THR LEU HIS SER LEU
SEQRES 33 B 469 PRO PHE GLY GLY VAL GLY ASN SER GLY MET GLY SER TYR
SEQRES 34 B 469 HIS GLY LYS LYS SER PHE GLU THR PHE SER HIS ARG ARG
SEQRES 35 B 469 SER CYS LEU VAL ARG PRO LEU MET ASN ASP GLU GLY LEU
SEQRES 36 B 469 LYS VAL ARG TYR PRO PRO SER PRO ALA LYS MET THR GLN
SEQRES 37 B 469 HIS
HET 1VL A 601 18
HET K A 602 1
HET K A 603 1
HET ACT A 604 4
HET 1VL B 601 18
HET K B 602 1
HET K B 603 1
HET ACT B 604 4
HETNAM 1VL (3S)-1-{[4-(1,3-BENZODIOXOL-5-YLMETHYL)PIPERAZIN-1-
HETNAM 2 1VL YL]METHYL}-3-HYDROXY-1,3-DIHYDRO-2H-INDOL-2-ONE
HETNAM K POTASSIUM ION
HETNAM ACT ACETATE ION
FORMUL 3 1VL 2(C21 H23 N3 O4)
FORMUL 4 K 4(K 1+)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 11 HOH *648(H2 O)
HELIX 1 1 SER A 1 SER A 16 1 16
HELIX 2 2 PRO A 21 GLN A 39 1 19
HELIX 3 3 GLN A 39 HIS A 52 1 14
HELIX 4 4 ASN A 54 GLU A 61 1 8
HELIX 5 5 GLU A 62 ALA A 82 1 21
HELIX 6 6 THR A 89 GLN A 93 5 5
HELIX 7 7 PHE A 117 ALA A 130 1 14
HELIX 8 8 SER A 142 LEU A 157 1 16
HELIX 9 9 GLY A 168 LEU A 176 1 9
HELIX 10 10 SER A 188 LYS A 201 1 14
HELIX 11 11 ASP A 223 MET A 237 1 15
HELIX 12 12 ASN A 238 GLN A 241 5 4
HELIX 13 13 ILE A 255 GLY A 272 1 18
HELIX 14 14 ASP A 274 SER A 278 5 5
HELIX 15 15 SER A 286 GLU A 298 1 13
HELIX 16 16 SER A 327 GLN A 331 5 5
HELIX 17 17 SER A 346 ARG A 357 1 12
HELIX 18 18 ASN A 369 THR A 380 1 12
HELIX 19 19 ILE A 391 LEU A 396 5 6
HELIX 20 20 VAL A 404 ASN A 406 5 3
HELIX 21 21 GLY A 414 PHE A 421 1 8
HELIX 22 22 LEU A 438 TYR A 442 5 5
HELIX 23 23 LYS B 2 SER B 16 1 15
HELIX 24 24 PRO B 21 GLN B 39 1 19
HELIX 25 25 GLN B 39 HIS B 52 1 14
HELIX 26 26 ASN B 54 GLU B 61 1 8
HELIX 27 27 GLU B 62 ALA B 82 1 21
HELIX 28 28 THR B 89 GLN B 93 5 5
HELIX 29 29 PHE B 117 ALA B 130 1 14
HELIX 30 30 SER B 142 LEU B 157 1 16
HELIX 31 31 GLY B 168 LEU B 176 1 9
HELIX 32 32 SER B 188 LYS B 201 1 14
HELIX 33 33 ASP B 223 MET B 237 1 15
HELIX 34 34 ASN B 238 GLN B 241 5 4
HELIX 35 35 ASP B 252 SER B 254 5 3
HELIX 36 36 ILE B 255 GLY B 272 1 18
HELIX 37 37 ASP B 274 SER B 278 5 5
HELIX 38 38 SER B 286 GLU B 298 1 13
HELIX 39 39 SER B 327 GLN B 331 5 5
HELIX 40 40 SER B 346 ARG B 357 1 12
HELIX 41 41 ASN B 369 THR B 380 1 12
HELIX 42 42 ILE B 391 THR B 395 5 5
HELIX 43 43 VAL B 404 ASN B 406 5 3
HELIX 44 44 GLY B 414 PHE B 421 1 8
HELIX 45 45 ASP B 435 TYR B 442 5 8
SHEET 1 A10 GLU A 84 PRO A 85 0
SHEET 2 A10 GLU A 96 PRO A 103 -1 O ILE A 99 N GLU A 84
SHEET 3 A10 SER A 422 VAL A 429 -1 O HIS A 423 N GLU A 102
SHEET 4 A10 GLY B 384 ALA B 387 1 O ALA B 387 N LEU A 428
SHEET 5 A10 ALA B 362 PHE B 366 1 N LEU B 363 O ALA B 386
SHEET 6 A10 PRO B 215 VAL B 218 1 N TYR B 217 O PHE B 366
SHEET 7 A10 TYR B 248 CYS B 251 1 O LEU B 250 N VAL B 218
SHEET 8 A10 VAL B 338 CYS B 343 1 O VAL B 342 N ILE B 249
SHEET 9 A10 THR B 318 THR B 321 1 N THR B 318 O LEU B 339
SHEET 10 A10 LYS B 301 TYR B 304 -1 N ALA B 303 O ILE B 319
SHEET 1 B 5 ALA A 133 LYS A 137 0
SHEET 2 B 5 VAL A 106 ILE A 110 1 N VAL A 107 O ALA A 133
SHEET 3 B 5 HIS A 182 THR A 186 1 O LEU A 184 N ILE A 110
SHEET 4 B 5 VAL A 206 GLU A 209 1 O THR A 207 N ILE A 183
SHEET 5 B 5 GLY A 408 MET A 409 -1 O MET A 409 N LEU A 208
SHEET 1 C10 LYS A 301 TYR A 304 0
SHEET 2 C10 THR A 318 THR A 321 -1 O ILE A 319 N ALA A 303
SHEET 3 C10 VAL A 338 CYS A 343 1 O LEU A 339 N THR A 318
SHEET 4 C10 TYR A 248 CYS A 251 1 N ILE A 249 O VAL A 342
SHEET 5 C10 PRO A 215 VAL A 218 1 N VAL A 218 O LEU A 250
SHEET 6 C10 ALA A 362 PHE A 366 1 O PHE A 366 N TYR A 217
SHEET 7 C10 GLY A 384 ALA A 387 1 O ALA A 386 N LEU A 363
SHEET 8 C10 SER B 422 VAL B 429 1 O LEU B 428 N ALA A 387
SHEET 9 C10 GLU B 96 PRO B 103 -1 N HIS B 100 O ARG B 425
SHEET 10 C10 GLU B 84 PRO B 85 -1 N GLU B 84 O ILE B 99
SHEET 1 D 2 GLY A 308 ASP A 309 0
SHEET 2 D 2 TYR A 314 ILE A 315 -1 O TYR A 314 N ASP A 309
SHEET 1 E 5 ALA B 133 LYS B 137 0
SHEET 2 E 5 VAL B 106 ILE B 110 1 N VAL B 107 O ALA B 133
SHEET 3 E 5 HIS B 182 THR B 186 1 O LEU B 184 N ILE B 110
SHEET 4 E 5 VAL B 206 GLU B 209 1 O GLU B 209 N TYR B 185
SHEET 5 E 5 GLY B 408 MET B 409 -1 O MET B 409 N LEU B 208
SHEET 1 F 2 GLY B 308 ASP B 309 0
SHEET 2 F 2 TYR B 314 ILE B 315 -1 O TYR B 314 N ASP B 309
LINK SG CYS A 243 C7 1VL A 601 1555 1555 1.83
LINK SG CYS B 243 C7 1VL B 601 1555 1555 1.83
LINK O THR A 321 K K A 602 1555 1555 3.24
LINK O ASP A 322 K K A 602 1555 1555 2.90
LINK O LYS A 439 K K A 603 1555 1555 3.04
LINK O TYR A 442 K K A 603 1555 1555 2.97
LINK K K A 602 O HOH A 715 1555 1555 2.59
LINK K K A 602 O HOH A 821 1555 1555 3.02
LINK O GLU B 79 K K B 602 1555 1555 2.80
LINK O TRP B 80 K K B 602 1555 1555 3.33
LINK O ALA B 82 K K B 602 1555 1555 3.00
LINK O LYS B 439 K K B 603 1555 1555 2.74
LINK O TYR B 442 K K B 603 1555 1555 2.87
LINK K K B 602 O HOH B 893 1555 1555 2.93
LINK K K B 602 O HOH B 991 1555 1555 2.79
LINK K K B 603 O HOH B 829 1555 1555 2.63
LINK K K B 603 O HOH B 854 1555 1555 2.75
CISPEP 1 PRO A 443 PRO A 444 0 1.42
CISPEP 2 PRO B 443 PRO B 444 0 -0.65
SITE 1 AC1 18 GLU A 61 TYR A 65 ASN A 114 TYR A 115
SITE 2 AC1 18 ASN A 118 LEU A 119 GLU A 209 MET A 237
SITE 3 AC1 18 THR A 242 CYS A 243 ILE A 391 ILE A 394
SITE 4 AC1 18 THR A 395 PHE A 401 TYR A 412 HIS A 413
SITE 5 AC1 18 HOH A 888 HOH A1011
SITE 1 AC2 7 LYS A 277 THR A 321 ASP A 322 HOH A 715
SITE 2 AC2 7 HOH A 753 HOH A 805 HOH A 821
SITE 1 AC3 3 LYS A 439 TYR A 442 PRO A 444
SITE 1 AC4 4 ASN A 434 ASP A 435 TYR A 442 ARG B 230
SITE 1 AC5 16 ASN B 114 TYR B 115 ASN B 118 LEU B 119
SITE 2 AC5 16 GLU B 209 MET B 237 THR B 242 CYS B 243
SITE 3 AC5 16 ILE B 391 ILE B 394 THR B 395 PHE B 401
SITE 4 AC5 16 TYR B 412 HIS B 413 HOH B 763 HOH B 944
SITE 1 AC6 5 GLU B 79 TRP B 80 ALA B 82 HOH B 893
SITE 2 AC6 5 HOH B 991
SITE 1 AC7 4 LYS B 439 TYR B 442 HOH B 829 HOH B 854
SITE 1 AC8 5 ARG A 230 HOH A 814 ASN B 434 ASP B 435
SITE 2 AC8 5 TYR B 442
CRYST1 61.257 86.396 170.225 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 0.016325 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011575 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005875 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
