HEADER TRANSFERASE 18-NOV-15 5EUN
TITLE THE CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II, PLP-
TITLE 2 BOUND FORM, AT 1.83 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: KAT/AADAT,2-AMINOADIPATE AMINOTRANSFERASE,2-AMINOADIPATE
COMPND 6 TRANSAMINASE,ALPHA-AMINOADIPATE AMINOTRANSFERASE,AADAT,KYNURENINE
COMPND 7 AMINOTRANSFERASE II,KYNURENINE--OXOGLUTARATE AMINOTRANSFERASE II,
COMPND 8 KYNURENINE--OXOGLUTARATE TRANSAMINASE 2,KYNURENINE--OXOGLUTARATE
COMPND 9 TRANSAMINASE II;
COMPND 10 EC: 2.6.1.39,2.6.1.7;
COMPND 11 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: AADAT, KAT2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS KYNURENINE AMINOTRANSFERASE II, LLP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NEMATOLLAHI,G.SUN,A.KWAN,C.M.JEFFRIES,S.J.HARROP,J.R.HANRAHAN,
AUTHOR 2 N.A.NADVI,W.B.CHURCH
REVDAT 5 02-APR-25 5EUN 1 REMARK
REVDAT 4 10-AUG-16 5EUN 1 JRNL
REVDAT 3 13-APR-16 5EUN 1 JRNL
REVDAT 2 02-MAR-16 5EUN 1 REMARK
REVDAT 1 16-DEC-15 5EUN 0
JRNL AUTH A.NEMATOLLAHI,G.SUN,S.J.HARROP,J.R.HANRAHAN,W.B.CHURCH
JRNL TITL STRUCTURE OF THE PLP-FORM OF THE HUMAN KYNURENINE
JRNL TITL 2 AMINOTRANSFERASE II IN A NOVEL SPACEGROUP AT 1.83 ANGSTROM
JRNL TITL 3 RESOLUTION.
JRNL REF INT J MOL SCI V. 17 446 2016
JRNL REFN ESSN 1422-0067
JRNL PMID 27023527
JRNL DOI 10.3390/IJMS17040446
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: 2015)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 39644
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1942
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.4724 - 3.9314 1.00 4170 211 0.1707 0.1912
REMARK 3 2 3.9314 - 3.1208 1.00 3993 206 0.1653 0.1821
REMARK 3 3 3.1208 - 2.7264 1.00 3927 204 0.1769 0.2101
REMARK 3 4 2.7264 - 2.4772 0.99 3871 201 0.1758 0.1916
REMARK 3 5 2.4772 - 2.2997 0.98 3851 196 0.1680 0.1929
REMARK 3 6 2.2997 - 2.1641 0.98 3800 197 0.1650 0.2254
REMARK 3 7 2.1641 - 2.0557 0.97 3754 197 0.1711 0.1787
REMARK 3 8 2.0557 - 1.9662 0.95 3676 189 0.1761 0.2078
REMARK 3 9 1.9662 - 1.8905 0.95 3665 189 0.1951 0.2270
REMARK 3 10 1.8905 - 1.8253 0.77 2995 152 0.2151 0.2686
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 3430
REMARK 3 ANGLE : 0.716 4658
REMARK 3 CHIRALITY : 0.047 515
REMARK 3 PLANARITY : 0.005 600
REMARK 3 DIHEDRAL : 18.767 1285
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9102 16.7610 13.6756
REMARK 3 T TENSOR
REMARK 3 T11: 0.0299 T22: 0.0461
REMARK 3 T33: 0.0401 T12: 0.0000
REMARK 3 T13: 0.0018 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.4043 L22: 0.3121
REMARK 3 L33: 0.2820 L12: 0.0279
REMARK 3 L13: 0.1641 L23: -0.0090
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: -0.0742 S13: 0.0100
REMARK 3 S21: 0.0046 S22: -0.0260 S23: 0.0162
REMARK 3 S31: 0.0203 S32: -0.0319 S33: -0.0047
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5EUN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40742
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.825
REMARK 200 RESOLUTION RANGE LOW (A) : 45.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.02300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.18600
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: PHENIX (1.10.1_2155: 2015)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (1 UL) AT A CONCENTRATION OF 7
REMARK 280 MG/ML WERE MIXED WITH AN EQUAL VOLUME OF A RESERVOIR SOLUTION
REMARK 280 CONTAINING 200 MM NACL, 0.1M NACITRATE PH 5.6, 24% PEG4K AND
REMARK 280 EQUILIBRATED AGAINST 1 ML OF A RESERVOIR SOLUTION AT 293 K.,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.11800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.22750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.22750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 64.67700
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.22750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.22750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 21.55900
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.22750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.22750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 64.67700
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.22750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.22750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 21.55900
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 43.11800
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 549 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 678 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 681 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 743 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 824 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 558 O HOH A 855 1.97
REMARK 500 O HOH A 713 O HOH A 852 1.99
REMARK 500 O HOH A 931 O HOH A 936 2.03
REMARK 500 O HOH A 509 O HOH A 748 2.05
REMARK 500 O HOH A 513 O HOH A 718 2.05
REMARK 500 O HOH A 517 O HOH A 756 2.05
REMARK 500 O HOH A 532 O HOH A 602 2.08
REMARK 500 O HOH A 832 O HOH A 857 2.12
REMARK 500 O HOH A 936 O HOH A 938 2.13
REMARK 500 O HOH A 790 O HOH A 875 2.13
REMARK 500 O HOH A 864 O HOH A 873 2.14
REMARK 500 O HOH A 695 O HOH A 737 2.18
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 PRO A 18 -172.69 -68.10
REMARK 500 ARG A 20 -115.30 -101.27
REMARK 500 THR A 21 62.28 -68.84
REMARK 500 MET A 22 -47.18 -134.72
REMARK 500 ARG A 28 -17.23 -143.40
REMARK 500 ASN A 96 62.46 31.74
REMARK 500 ASP A 162 -157.57 -136.99
REMARK 500 PRO A 186 4.17 -66.15
REMARK 500 SER A 266 131.34 -177.56
REMARK 500 SER A 291 -102.68 -122.10
REMARK 500 LEU A 293 -50.39 76.70
REMARK 500 MET A 354 23.62 -140.19
REMARK 500 ILE A 370 -62.39 -95.37
REMARK 500 SER A 404 -32.36 -132.15
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 SER A 17 PRO A 18 -143.80
REMARK 500 LYS A 188 ASN A 189 141.00
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 924 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 925 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 926 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 927 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 928 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A 929 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A 930 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A 931 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A 932 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A 933 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH A 934 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH A 935 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH A 936 DISTANCE = 8.06 ANGSTROMS
REMARK 525 HOH A 937 DISTANCE = 8.40 ANGSTROMS
REMARK 525 HOH A 938 DISTANCE = 9.36 ANGSTROMS
DBREF 5EUN A 1 425 UNP Q8N5Z0 AADAT_HUMAN 1 425
SEQRES 1 A 425 MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA
SEQRES 2 A 425 ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU
SEQRES 3 A 425 SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY
SEQRES 4 A 425 LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL
SEQRES 5 A 425 ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU
SEQRES 6 A 425 GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA
SEQRES 7 A 425 GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN
SEQRES 8 A 425 ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO
SEQRES 9 A 425 SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER
SEQRES 10 A 425 GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN
SEQRES 11 A 425 PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER
SEQRES 12 A 425 GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE
SEQRES 13 A 425 ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP
SEQRES 14 A 425 SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP
SEQRES 15 A 425 ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR
SEQRES 16 A 425 THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU
SEQRES 17 A 425 THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG
SEQRES 18 A 425 LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR
SEQRES 19 A 425 PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU
SEQRES 20 A 425 SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER
SEQRES 21 A 425 PHE SER LLP ILE ILE SER SER GLY LEU ARG ILE GLY PHE
SEQRES 22 A 425 LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU
SEQRES 23 A 425 HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN
SEQRES 24 A 425 GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU
SEQRES 25 A 425 GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE
SEQRES 26 A 425 TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP
SEQRES 27 A 425 LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA
SEQRES 28 A 425 ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN
SEQRES 29 A 425 ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET
SEQRES 30 A 425 GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP
SEQRES 31 A 425 SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER
SEQRES 32 A 425 SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL
SEQRES 33 A 425 LEU ALA GLN LEU ILE LYS GLU SER LEU
MODRES 5EUN LLP A 263 LYS MODIFIED RESIDUE
HET LLP A 263 38
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP C14 H22 N3 O7 P
FORMUL 2 HOH *438(H2 O)
HELIX 1 AA1 ASN A 2 ILE A 7 5 6
HELIX 2 AA2 THR A 8 ARG A 14 1 7
HELIX 3 AA3 ASN A 42 PHE A 46 5 5
HELIX 4 AA4 GLY A 64 LEU A 72 1 9
HELIX 5 AA5 ILE A 80 ASN A 96 1 17
HELIX 6 AA6 PRO A 103 GLY A 107 5 5
HELIX 7 AA7 GLY A 116 ILE A 129 1 14
HELIX 8 AA8 TYR A 142 HIS A 150 1 9
HELIX 9 AA9 PRO A 151 GLY A 153 5 3
HELIX 10 AB1 VAL A 167 SER A 176 1 10
HELIX 11 AB2 ARG A 177 TRP A 178 5 2
HELIX 12 AB3 LYS A 179 ASN A 189 5 11
HELIX 13 AB4 THR A 209 TYR A 223 1 15
HELIX 14 AB5 PHE A 246 ASP A 250 5 5
HELIX 15 AB6 LYS A 278 VAL A 290 1 13
HELIX 16 AB7 SER A 296 LEU A 341 1 46
HELIX 17 AB8 VAL A 366 GLU A 372 1 7
HELIX 18 AB9 GLU A 372 MET A 377 1 6
HELIX 19 AC1 ASN A 385 TYR A 388 5 4
HELIX 20 AC2 SER A 406 LEU A 425 1 20
SHEET 1 AA1 2 ALA A 51 ILE A 53 0
SHEET 2 AA1 2 ILE A 61 PHE A 63 -1 O ILE A 61 N ILE A 53
SHEET 1 AA2 7 MET A 109 THR A 114 0
SHEET 2 AA2 7 GLY A 272 PRO A 277 -1 O LEU A 274 N CYS A 112
SHEET 3 AA2 7 VAL A 255 SER A 260 -1 N ARG A 257 O THR A 275
SHEET 4 AA2 7 LEU A 226 ASP A 230 1 N GLU A 229 O ILE A 256
SHEET 5 AA2 7 PHE A 193 THR A 196 1 N LEU A 194 O ILE A 228
SHEET 6 AA2 7 ASN A 134 LEU A 137 1 N LEU A 136 O TYR A 195
SHEET 7 AA2 7 ASN A 155 ASN A 158 1 O ILE A 157 N VAL A 135
SHEET 1 AA3 2 SER A 161 ASP A 162 0
SHEET 2 AA3 2 GLY A 165 ILE A 166 -1 O GLY A 165 N ASP A 162
SHEET 1 AA4 4 ALA A 345 TRP A 347 0
SHEET 2 AA4 4 PHE A 355 VAL A 360 -1 O LYS A 359 N GLU A 346
SHEET 3 AA4 4 TYR A 397 SER A 401 -1 O ALA A 400 N LEU A 356
SHEET 4 AA4 4 LEU A 382 PRO A 383 -1 N LEU A 382 O ARG A 399
LINK C SER A 262 N LLP A 263 1555 1555 1.33
LINK C LLP A 263 N ILE A 264 1555 1555 1.33
CISPEP 1 GLU A 139 PRO A 140 0 -0.60
CISPEP 2 ASN A 202 PRO A 203 0 16.28
CRYST1 102.455 102.455 86.236 90.00 90.00 90.00 P 43 21 2 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 0.009760 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009760 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011596 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
