HEADER TRANSFERASE 26-OCT-15 5EFS
TITLE THE CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II
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, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NEMATOLLAHI,G.SUN,A.KWAN,S.J.HARROP,J.R.HANRAHAN,N.A.NADVI,
AUTHOR 2 W.B.CHURCH
REVDAT 2 06-MAR-24 5EFS 1 REMARK
REVDAT 1 11-NOV-15 5EFS 0
JRNL AUTH A.NEMATOLLAHI,G.SUN,A.KWAN,C.M.JEFFRIES,S.J.HARROP,
JRNL AUTH 2 J.R.HANRAHAN,N.A.NADVI,W.B.CHURCH
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE
JRNL TITL 2 II
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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 : 39646
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.192
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 - 4.3975 1.00 3032 152 0.1749 0.2007
REMARK 3 2 4.3975 - 3.4910 1.00 2867 148 0.1537 0.1617
REMARK 3 3 3.4910 - 3.0499 1.00 2835 147 0.1647 0.2068
REMARK 3 4 3.0499 - 2.7711 1.00 2800 145 0.1697 0.1995
REMARK 3 5 2.7711 - 2.5725 0.99 2771 143 0.1749 0.2091
REMARK 3 6 2.5725 - 2.4209 0.99 2769 143 0.1646 0.1684
REMARK 3 7 2.4209 - 2.2997 0.98 2740 140 0.1604 0.1630
REMARK 3 8 2.2997 - 2.1996 0.98 2720 140 0.1629 0.2303
REMARK 3 9 2.1996 - 2.1149 0.97 2699 142 0.1683 0.1751
REMARK 3 10 2.1149 - 2.0419 0.97 2672 141 0.1709 0.1928
REMARK 3 11 2.0419 - 1.9781 0.95 2632 135 0.1733 0.1845
REMARK 3 12 1.9781 - 1.9215 0.95 2622 133 0.1867 0.2242
REMARK 3 13 1.9215 - 1.8709 0.93 2553 129 0.2023 0.2162
REMARK 3 14 1.8709 - 1.8253 0.72 1992 104 0.2111 0.2266
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.28
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 3415
REMARK 3 ANGLE : 0.709 4636
REMARK 3 CHIRALITY : 0.046 515
REMARK 3 PLANARITY : 0.004 600
REMARK 3 DIHEDRAL : 21.667 2079
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): 16.7643 26.9686 29.4014
REMARK 3 T TENSOR
REMARK 3 T11: 0.0252 T22: 0.0001
REMARK 3 T33: 0.0188 T12: -0.0001
REMARK 3 T13: 0.0125 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.3625 L22: 0.4967
REMARK 3 L33: 0.3287 L12: 0.0345
REMARK 3 L13: 0.0100 L23: -0.2610
REMARK 3 S TENSOR
REMARK 3 S11: -0.0412 S12: 0.0009 S13: -0.0190
REMARK 3 S21: -0.1097 S22: 0.0044 S23: -0.0147
REMARK 3 S31: 0.0060 S32: -0.0318 S33: -0.0089
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 5EFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214799.
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 : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40804
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.825
REMARK 200 RESOLUTION RANGE LOW (A) : 45.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 14.30
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
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) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 14.00
REMARK 200 R MERGE FOR SHELL (I) : 0.80500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER PHASER MODULE: 2.6.0
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): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM NACL, 0.1M NACITRATE PH 5.6,
REMARK 280 24% PEG4K, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 300K
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 86.23600
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 602 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 730 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 783 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 856 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 954 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 958 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 H ASN A 57 O HOH A 508 1.56
REMARK 500 O HOH A 571 O HOH A 707 1.98
REMARK 500 O HOH A 698 O HOH A 914 2.06
REMARK 500 O HOH A 580 O HOH A 899 2.07
REMARK 500 O HOH A 655 O HOH A 884 2.07
REMARK 500 O HOH A 808 O HOH A 909 2.11
REMARK 500 O HOH A 501 O HOH A 877 2.11
REMARK 500 O HOH A 543 O HOH A 560 2.13
REMARK 500 O HOH A 868 O HOH A 889 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 17 C PRO A 18 N 0.198
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 ASN A 96 62.34 32.97
REMARK 500 ASP A 162 -157.65 -136.16
REMARK 500 SER A 266 129.17 -177.28
REMARK 500 SER A 291 -97.71 -123.59
REMARK 500 LEU A 293 -49.89 76.58
REMARK 500 LYS A 373 52.00 -94.34
REMARK 500 ALA A 374 -79.31 -103.41
REMARK 500 LYS A 376 -73.05 -58.39
REMARK 500 SER A 404 -31.59 -133.52
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 LYS A 240 PHE A 241 135.64
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 954 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 955 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 956 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 957 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 958 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A 959 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A 960 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A 961 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH A 962 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH A 963 DISTANCE = 7.98 ANGSTROMS
REMARK 525 HOH A 964 DISTANCE = 8.51 ANGSTROMS
REMARK 525 HOH A 965 DISTANCE = 9.56 ANGSTROMS
REMARK 525 HOH A 966 DISTANCE = 11.04 ANGSTROMS
DBREF 5EFS 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 LYS 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
FORMUL 2 HOH *466(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 185 5 7
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 ASP A 365 GLU A 372 1 8
HELIX 18 AB9 ASN A 385 TYR A 388 5 4
HELIX 19 AC1 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 LEU A 398 N ILE A 358
SHEET 4 AA4 4 LEU A 382 PRO A 383 -1 N LEU A 382 O ARG A 399
CISPEP 1 GLU A 139 PRO A 140 0 -0.97
CISPEP 2 ASN A 202 PRO A 203 0 16.95
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
