HEADER OXIDOREDUCTASE 15-FEB-13 3ZNO
TITLE IN VITRO AND IN VIVO INHIBITION OF HUMAN D-AMINO ACID OXIDASE:
TITLE 2 REGULATION OF D-SERINE CONCENTRATION IN THE BRAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-AMINO-ACID OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DAAO, DAMOX, DAO;
COMPND 5 EC: 1.4.3.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS OXIDOREDUCTASE, NEUROTRANSMISSION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.HOPKINS,M.L.R.HEFFERNAN,L.D.SARASWAT,C.A.BOWEN,L.MELNICK,
AUTHOR 2 L.W.HARDY,M.A.ORSINI,M.S.ALLEN,P.KOCH,K.L.SPEAR,R.J.FOGLESONG,
AUTHOR 3 M.SOUKRI,M.CHYTIL,Q.K.FANG,S.W.JONES,M.A.VARNEY,A.PANATIER,
AUTHOR 4 S.H.R.OLIET,L.POLLEGIONI,L.PIUBELLI,G.MOLLA,M.NARDINI,T.H.LARGE
REVDAT 3 20-DEC-23 3ZNO 1 REMARK
REVDAT 2 22-MAY-13 3ZNO 1 JRNL
REVDAT 1 15-MAY-13 3ZNO 0
JRNL AUTH S.C.HOPKINS,M.L.R.HEFFERNAN,L.D.SARASWAT,C.A.BOWEN,
JRNL AUTH 2 L.MELNICK,L.W.HARDY,M.A.ORSINI,M.S.ALLEN,P.KOCH,K.L.SPEAR,
JRNL AUTH 3 R.J.FOGLESONG,M.SOUKRI,M.CHYTIL,Q.K.FANG,S.W.JONES,
JRNL AUTH 4 M.A.VARNEY,A.PANATIER,S.H.R.OLIET,L.POLLEGIONI,L.PIUBELLI,
JRNL AUTH 5 G.MOLLA,M.NARDINI,T.H.LARGE
JRNL TITL STRUCTURAL, KINETIC, AND PHARMACODYNAMIC MECHANISMS OF
JRNL TITL 2 D-AMINO ACID OXIDASE INHIBITION BY SMALL MOLECULES.
JRNL REF J.MED.CHEM. V. 56 3710 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23631755
JRNL DOI 10.1021/JM4002583
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 29206
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1471
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.58
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2907
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2238
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2748
REMARK 3 BIN R VALUE (WORKING SET) : 0.2184
REMARK 3 BIN FREE R VALUE : 0.3215
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.47
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 159
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5466
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 235
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.17150
REMARK 3 B22 (A**2) : 10.96070
REMARK 3 B33 (A**2) : -8.78910
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.332
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.606
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.311
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.536
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.309
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.863
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5861 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8006 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1959 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 175 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 863 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5861 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 728 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6678 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.80
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.85
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|1 - A|360 }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9132 -21.3527 -55.6000
REMARK 3 T TENSOR
REMARK 3 T11: -0.1419 T22: -0.0817
REMARK 3 T33: -0.0480 T12: -0.0046
REMARK 3 T13: -0.0337 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 0.9841 L22: 0.8113
REMARK 3 L33: 1.8840 L12: -0.0644
REMARK 3 L13: 0.2572 L23: -0.0084
REMARK 3 S TENSOR
REMARK 3 S11: 0.0538 S12: 0.0136 S13: -0.0392
REMARK 3 S21: 0.0233 S22: -0.0066 S23: 0.0056
REMARK 3 S31: 0.0649 S32: 0.0429 S33: -0.0473
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|1 - B|360 }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3599 -3.0747 -15.7078
REMARK 3 T TENSOR
REMARK 3 T11: -0.0983 T22: -0.0049
REMARK 3 T33: -0.1610 T12: 0.0143
REMARK 3 T13: -0.0791 T23: -0.1528
REMARK 3 L TENSOR
REMARK 3 L11: 1.0880 L22: 2.0126
REMARK 3 L33: 1.2583 L12: -0.6834
REMARK 3 L13: -0.6419 L23: 1.0527
REMARK 3 S TENSOR
REMARK 3 S11: -0.0578 S12: -0.3762 S13: 0.3073
REMARK 3 S21: 0.3244 S22: 0.1599 S23: -0.2796
REMARK 3 S31: 0.0699 S32: 0.1359 S33: -0.1021
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES A296-A303, A338-A340 B303,
REMARK 3 B338-B340 ARE DISORDERED. POOR DENSITY IS PRESENT FOR RESIDUES
REMARK 3 A296, A297, A298, A299, A300, A301, A302, A303, A338, A339, A340,
REMARK 3 B55,B56, B57, B58, B59, B60, B61, B162, B163, B296, B297, B298,
REMARK 3 B299, B300, B301, B302, B303, B338, B339, B340 FINAL STRUCTURE
REMARK 3 HAS NO RESIDUES IN THE DISALLOWED REGION OF THE RAMACHANDRAN
REMARK 3 PLOT AS DEFINED IN THE CCP4 PROCHECK PROGRAM.
REMARK 4
REMARK 4 3ZNO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1290055840.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 FR-E
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29214
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 64.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 4.210
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
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) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.87
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 2DU8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 22.01550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 129.86150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.52800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 129.86150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.01550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.52800
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: 6540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.1 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 ARG A 341
REMARK 465 MET A 342
REMARK 465 PRO A 343
REMARK 465 PRO A 344
REMARK 465 SER A 345
REMARK 465 HIS A 346
REMARK 465 LEU A 347
REMARK 465 ARG B 341
REMARK 465 MET B 342
REMARK 465 PRO B 343
REMARK 465 PRO B 344
REMARK 465 SER B 345
REMARK 465 HIS B 346
REMARK 465 LEU B 347
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 PRO A 29 51.10 -96.08
REMARK 500 PHE A 39 -163.08 -116.10
REMARK 500 THR A 40 -63.66 -11.50
REMARK 500 GLN A 53 111.37 -163.18
REMARK 500 PRO A 82 10.54 -62.23
REMARK 500 SER A 136 -157.64 -129.74
REMARK 500 ASP A 192 86.73 -152.90
REMARK 500 THR A 298 112.46 -36.57
REMARK 500 ASN A 308 78.14 -159.31
REMARK 500 LYS A 338 71.83 60.49
REMARK 500 LEU A 339 25.31 -145.56
REMARK 500 PRO B 29 97.31 -65.66
REMARK 500 THR B 40 -49.05 -18.97
REMARK 500 GLN B 53 109.66 -167.22
REMARK 500 SER B 136 -150.59 -120.48
REMARK 500 ASN B 225 40.13 -109.84
REMARK 500 ARG B 297 82.22 -69.66
REMARK 500 LEU B 339 -18.53 -144.33
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 A 583 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH A 606 DISTANCE = 7.02 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SE5 A 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SE5 B 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1341
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZNN RELATED DB: PDB
REMARK 900 IN VITRO AND IN VIVO INHIBITION OF HUMAN D-AMINO ACID OXIDASE:
REMARK 900 REGULATION OF D-SERINE CONCENTRATION IN THE BRAIN
REMARK 900 RELATED ID: 3ZNP RELATED DB: PDB
REMARK 900 IN VITRO AND IN VIVO INHIBITION OF HUMAN D-AMINO ACID OXIDASE:
REMARK 900 REGULATION OF D-SERINE CONCENTRATION IN THE BRAIN
REMARK 900 RELATED ID: 3ZNQ RELATED DB: PDB
REMARK 900 IN VITRO AND IN VIVO INHIBITION OF HUMAN D-AMINO ACID OXIDASE:
REMARK 900 REGULATION OF D-SERINE CONCENTRATION IN THE BRAIN
DBREF 3ZNO A 1 347 UNP P14920 OXDA_HUMAN 1 347
DBREF 3ZNO B 1 347 UNP P14920 OXDA_HUMAN 1 347
SEQRES 1 A 347 MET ARG VAL VAL VAL ILE GLY ALA GLY VAL ILE GLY LEU
SEQRES 2 A 347 SER THR ALA LEU CYS ILE HIS GLU ARG TYR HIS SER VAL
SEQRES 3 A 347 LEU GLN PRO LEU ASP ILE LYS VAL TYR ALA ASP ARG PHE
SEQRES 4 A 347 THR PRO LEU THR THR THR ASP VAL ALA ALA GLY LEU TRP
SEQRES 5 A 347 GLN PRO TYR LEU SER ASP PRO ASN ASN PRO GLN GLU ALA
SEQRES 6 A 347 ASP TRP SER GLN GLN THR PHE ASP TYR LEU LEU SER HIS
SEQRES 7 A 347 VAL HIS SER PRO ASN ALA GLU ASN LEU GLY LEU PHE LEU
SEQRES 8 A 347 ILE SER GLY TYR ASN LEU PHE HIS GLU ALA ILE PRO ASP
SEQRES 9 A 347 PRO SER TRP LYS ASP THR VAL LEU GLY PHE ARG LYS LEU
SEQRES 10 A 347 THR PRO ARG GLU LEU ASP MET PHE PRO ASP TYR GLY TYR
SEQRES 11 A 347 GLY TRP PHE HIS THR SER LEU ILE LEU GLU GLY LYS ASN
SEQRES 12 A 347 TYR LEU GLN TRP LEU THR GLU ARG LEU THR GLU ARG GLY
SEQRES 13 A 347 VAL LYS PHE PHE GLN ARG LYS VAL GLU SER PHE GLU GLU
SEQRES 14 A 347 VAL ALA ARG GLU GLY ALA ASP VAL ILE VAL ASN CYS THR
SEQRES 15 A 347 GLY VAL TRP ALA GLY ALA LEU GLN ARG ASP PRO LEU LEU
SEQRES 16 A 347 GLN PRO GLY ARG GLY GLN ILE MET LYS VAL ASP ALA PRO
SEQRES 17 A 347 TRP MET LYS HIS PHE ILE LEU THR HIS ASP PRO GLU ARG
SEQRES 18 A 347 GLY ILE TYR ASN SER PRO TYR ILE ILE PRO GLY THR GLN
SEQRES 19 A 347 THR VAL THR LEU GLY GLY ILE PHE GLN LEU GLY ASN TRP
SEQRES 20 A 347 SER GLU LEU ASN ASN ILE GLN ASP HIS ASN THR ILE TRP
SEQRES 21 A 347 GLU GLY CYS CYS ARG LEU GLU PRO THR LEU LYS ASN ALA
SEQRES 22 A 347 ARG ILE ILE GLY GLU ARG THR GLY PHE ARG PRO VAL ARG
SEQRES 23 A 347 PRO GLN ILE ARG LEU GLU ARG GLU GLN LEU ARG THR GLY
SEQRES 24 A 347 PRO SER ASN THR GLU VAL ILE HIS ASN TYR GLY HIS GLY
SEQRES 25 A 347 GLY TYR GLY LEU THR ILE HIS TRP GLY CYS ALA LEU GLU
SEQRES 26 A 347 ALA ALA LYS LEU PHE GLY ARG ILE LEU GLU GLU LYS LYS
SEQRES 27 A 347 LEU SER ARG MET PRO PRO SER HIS LEU
SEQRES 1 B 347 MET ARG VAL VAL VAL ILE GLY ALA GLY VAL ILE GLY LEU
SEQRES 2 B 347 SER THR ALA LEU CYS ILE HIS GLU ARG TYR HIS SER VAL
SEQRES 3 B 347 LEU GLN PRO LEU ASP ILE LYS VAL TYR ALA ASP ARG PHE
SEQRES 4 B 347 THR PRO LEU THR THR THR ASP VAL ALA ALA GLY LEU TRP
SEQRES 5 B 347 GLN PRO TYR LEU SER ASP PRO ASN ASN PRO GLN GLU ALA
SEQRES 6 B 347 ASP TRP SER GLN GLN THR PHE ASP TYR LEU LEU SER HIS
SEQRES 7 B 347 VAL HIS SER PRO ASN ALA GLU ASN LEU GLY LEU PHE LEU
SEQRES 8 B 347 ILE SER GLY TYR ASN LEU PHE HIS GLU ALA ILE PRO ASP
SEQRES 9 B 347 PRO SER TRP LYS ASP THR VAL LEU GLY PHE ARG LYS LEU
SEQRES 10 B 347 THR PRO ARG GLU LEU ASP MET PHE PRO ASP TYR GLY TYR
SEQRES 11 B 347 GLY TRP PHE HIS THR SER LEU ILE LEU GLU GLY LYS ASN
SEQRES 12 B 347 TYR LEU GLN TRP LEU THR GLU ARG LEU THR GLU ARG GLY
SEQRES 13 B 347 VAL LYS PHE PHE GLN ARG LYS VAL GLU SER PHE GLU GLU
SEQRES 14 B 347 VAL ALA ARG GLU GLY ALA ASP VAL ILE VAL ASN CYS THR
SEQRES 15 B 347 GLY VAL TRP ALA GLY ALA LEU GLN ARG ASP PRO LEU LEU
SEQRES 16 B 347 GLN PRO GLY ARG GLY GLN ILE MET LYS VAL ASP ALA PRO
SEQRES 17 B 347 TRP MET LYS HIS PHE ILE LEU THR HIS ASP PRO GLU ARG
SEQRES 18 B 347 GLY ILE TYR ASN SER PRO TYR ILE ILE PRO GLY THR GLN
SEQRES 19 B 347 THR VAL THR LEU GLY GLY ILE PHE GLN LEU GLY ASN TRP
SEQRES 20 B 347 SER GLU LEU ASN ASN ILE GLN ASP HIS ASN THR ILE TRP
SEQRES 21 B 347 GLU GLY CYS CYS ARG LEU GLU PRO THR LEU LYS ASN ALA
SEQRES 22 B 347 ARG ILE ILE GLY GLU ARG THR GLY PHE ARG PRO VAL ARG
SEQRES 23 B 347 PRO GLN ILE ARG LEU GLU ARG GLU GLN LEU ARG THR GLY
SEQRES 24 B 347 PRO SER ASN THR GLU VAL ILE HIS ASN TYR GLY HIS GLY
SEQRES 25 B 347 GLY TYR GLY LEU THR ILE HIS TRP GLY CYS ALA LEU GLU
SEQRES 26 B 347 ALA ALA LYS LEU PHE GLY ARG ILE LEU GLU GLU LYS LYS
SEQRES 27 B 347 LEU SER ARG MET PRO PRO SER HIS LEU
HET FAD A 350 53
HET SE5 A 360 17
HET GOL A1341 6
HET FAD B 350 53
HET SE5 B 360 17
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM SE5 4-(4-CHLOROPHENETHYL)-1H-PYRROLE-2-CARBOXYLIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 SE5 2(C13 H12 CL N O2)
FORMUL 5 GOL C3 H8 O3
FORMUL 8 HOH *235(H2 O)
HELIX 1 1 GLY A 9 HIS A 24 1 16
HELIX 2 2 THR A 44 ALA A 48 5 5
HELIX 3 3 ASN A 61 VAL A 79 1 19
HELIX 4 4 ASN A 83 GLY A 88 1 6
HELIX 5 5 THR A 118 ASP A 123 1 6
HELIX 6 6 GLU A 140 ARG A 155 1 16
HELIX 7 7 SER A 166 GLU A 173 1 8
HELIX 8 8 THR A 182 LEU A 189 5 8
HELIX 9 9 ASN A 252 GLU A 267 1 16
HELIX 10 10 PRO A 268 ALA A 273 5 6
HELIX 11 11 TYR A 314 LYS A 338 1 25
HELIX 12 12 GLY B 9 HIS B 24 1 16
HELIX 13 13 THR B 43 ALA B 48 1 6
HELIX 14 14 PRO B 62 HIS B 78 1 17
HELIX 15 15 ASN B 83 GLY B 88 1 6
HELIX 16 16 PRO B 105 THR B 110 5 6
HELIX 17 17 THR B 118 ASP B 123 1 6
HELIX 18 18 GLU B 140 GLU B 154 1 15
HELIX 19 19 SER B 166 GLU B 173 1 8
HELIX 20 20 THR B 182 LEU B 189 5 8
HELIX 21 21 ASN B 252 GLU B 267 1 16
HELIX 22 22 PRO B 268 ALA B 273 5 6
HELIX 23 23 HIS B 311 GLY B 313 5 3
HELIX 24 24 TYR B 314 LYS B 337 1 24
SHEET 1 AA 6 LYS A 158 GLN A 161 0
SHEET 2 AA 6 ASP A 31 ALA A 36 1 O ILE A 32 N LYS A 158
SHEET 3 AA 6 ARG A 2 ILE A 6 1 O VAL A 3 N LYS A 33
SHEET 4 AA 6 VAL A 177 ASN A 180 1 O VAL A 177 N VAL A 4
SHEET 5 AA 6 THR A 303 TYR A 309 1 O GLU A 304 N ILE A 178
SHEET 6 AA 6 ARG A 290 LEU A 296 -1 O ARG A 290 N TYR A 309
SHEET 1 AB 8 LEU A 112 LYS A 116 0
SHEET 2 AB 8 TYR A 130 LEU A 139 -1 O PHE A 133 N ARG A 115
SHEET 3 AB 8 LEU A 89 PHE A 98 -1 O PHE A 90 N ILE A 138
SHEET 4 AB 8 PHE A 213 HIS A 217 1 O PHE A 213 N TYR A 95
SHEET 5 AB 8 TYR A 228 PRO A 231 -1 O ILE A 229 N ILE A 214
SHEET 6 AB 8 VAL A 236 GLY A 239 -1 O THR A 237 N ILE A 230
SHEET 7 AB 8 GLN A 196 ASP A 206 -1 O MET A 203 N LEU A 238
SHEET 8 AB 8 GLN A 243 LEU A 244 1 O GLN A 243 N ARG A 199
SHEET 1 AC 8 LEU A 112 LYS A 116 0
SHEET 2 AC 8 TYR A 130 LEU A 139 -1 O PHE A 133 N ARG A 115
SHEET 3 AC 8 LEU A 89 PHE A 98 -1 O PHE A 90 N ILE A 138
SHEET 4 AC 8 PHE A 213 HIS A 217 1 O PHE A 213 N TYR A 95
SHEET 5 AC 8 TYR A 228 PRO A 231 -1 O ILE A 229 N ILE A 214
SHEET 6 AC 8 VAL A 236 GLY A 239 -1 O THR A 237 N ILE A 230
SHEET 7 AC 8 GLN A 196 ASP A 206 -1 O MET A 203 N LEU A 238
SHEET 8 AC 8 ARG A 274 VAL A 285 -1 O ARG A 274 N ASP A 206
SHEET 1 AD 2 GLN A 243 LEU A 244 0
SHEET 2 AD 2 GLN A 196 ASP A 206 1 O ARG A 199 N GLN A 243
SHEET 1 BA 6 LYS B 158 GLN B 161 0
SHEET 2 BA 6 ASP B 31 ALA B 36 1 O ILE B 32 N LYS B 158
SHEET 3 BA 6 ARG B 2 ILE B 6 1 O VAL B 3 N LYS B 33
SHEET 4 BA 6 VAL B 177 ASN B 180 1 O VAL B 177 N VAL B 4
SHEET 5 BA 6 THR B 303 TYR B 309 1 O GLU B 304 N ILE B 178
SHEET 6 BA 6 ARG B 290 LEU B 296 -1 O ARG B 290 N TYR B 309
SHEET 1 BB 8 LEU B 112 LYS B 116 0
SHEET 2 BB 8 TYR B 130 LEU B 139 -1 O PHE B 133 N ARG B 115
SHEET 3 BB 8 LEU B 89 PHE B 98 -1 O PHE B 90 N ILE B 138
SHEET 4 BB 8 HIS B 212 THR B 216 1 O PHE B 213 N TYR B 95
SHEET 5 BB 8 TYR B 228 PRO B 231 -1 O ILE B 229 N ILE B 214
SHEET 6 BB 8 VAL B 236 GLY B 239 -1 O THR B 237 N ILE B 230
SHEET 7 BB 8 GLN B 196 ASP B 206 -1 O MET B 203 N LEU B 238
SHEET 8 BB 8 GLN B 243 LEU B 244 1 N GLN B 243 O ARG B 199
SHEET 1 BC 8 LEU B 112 LYS B 116 0
SHEET 2 BC 8 TYR B 130 LEU B 139 -1 O PHE B 133 N ARG B 115
SHEET 3 BC 8 LEU B 89 PHE B 98 -1 O PHE B 90 N ILE B 138
SHEET 4 BC 8 HIS B 212 THR B 216 1 O PHE B 213 N TYR B 95
SHEET 5 BC 8 TYR B 228 PRO B 231 -1 O ILE B 229 N ILE B 214
SHEET 6 BC 8 VAL B 236 GLY B 239 -1 O THR B 237 N ILE B 230
SHEET 7 BC 8 GLN B 196 ASP B 206 -1 O MET B 203 N LEU B 238
SHEET 8 BC 8 ARG B 274 VAL B 285 -1 O ARG B 274 N ASP B 206
SHEET 1 BD 2 GLN B 243 LEU B 244 0
SHEET 2 BD 2 GLN B 196 ASP B 206 1 O ARG B 199 N GLN B 243
CISPEP 1 PRO A 59 ASN A 60 0 -6.96
SITE 1 AC1 41 ILE A 6 GLY A 7 ALA A 8 GLY A 9
SITE 2 AC1 41 VAL A 10 ILE A 11 ALA A 36 ASP A 37
SITE 3 AC1 41 ARG A 38 THR A 43 THR A 44 THR A 45
SITE 4 AC1 41 VAL A 47 ALA A 48 ALA A 49 GLY A 50
SITE 5 AC1 41 LEU A 51 ARG A 162 LYS A 163 VAL A 164
SITE 6 AC1 41 CYS A 181 THR A 182 GLY A 183 TRP A 185
SITE 7 AC1 41 ILE A 202 TYR A 228 GLY A 281 ARG A 283
SITE 8 AC1 41 HIS A 311 GLY A 312 GLY A 313 TYR A 314
SITE 9 AC1 41 GLY A 315 LEU A 316 THR A 317 SE5 A 360
SITE 10 AC1 41 HOH A 537 HOH A 579 HOH A 581 HOH A 582
SITE 11 AC1 41 HOH A 601
SITE 1 AC2 9 LEU A 56 LEU A 215 ILE A 223 TYR A 224
SITE 2 AC2 9 TYR A 228 ILE A 230 ARG A 283 GLY A 313
SITE 3 AC2 9 FAD A 350
SITE 1 AC3 32 ILE B 6 GLY B 7 ALA B 8 GLY B 9
SITE 2 AC3 32 VAL B 10 ILE B 11 ALA B 36 ASP B 37
SITE 3 AC3 32 ARG B 38 THR B 44 THR B 45 ALA B 48
SITE 4 AC3 32 GLY B 50 LEU B 51 ARG B 162 VAL B 164
SITE 5 AC3 32 CYS B 181 THR B 182 GLY B 183 TRP B 185
SITE 6 AC3 32 ILE B 202 TYR B 228 ARG B 283 GLY B 312
SITE 7 AC3 32 GLY B 313 TYR B 314 GLY B 315 LEU B 316
SITE 8 AC3 32 THR B 317 SE5 B 360 HOH B 526 HOH B 591
SITE 1 AC4 7 HIS B 217 ILE B 223 TYR B 224 TYR B 228
SITE 2 AC4 7 ARG B 283 GLY B 313 FAD B 350
SITE 1 AC5 5 HIS A 212 GLU A 267 HOH A 567 HIS B 80
SITE 2 AC5 5 LEU B 91
CRYST1 44.031 61.056 259.723 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 0.022711 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003850 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
