longtext: 4KYV-pdb

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HEADER    DE NOVO PROTEIN                         29-MAY-13   4KYV
TITLE     CRYSTAL STRUCTURE OF DEHALOGENASE HALOTAG2 WITH HALTS AT THE
TITLE    2 RESOLUTION 1.8A. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
TITLE    3 TARGET OR150
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DEHALOGENASE HALOTAG2;
COMPND   3 CHAIN: A, B;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE   3 ORGANISM_TAXID: 32630;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15_NESG
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE,
KEYWDS   2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, HALTS, HALOGENASE,
KEYWDS   3 DE NOVO PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.KUZIN,S.LEW,J.SEETHARAMAN,M.MAGLAQUI,R.XIAO,E.KOHAN,H.WANG,
AUTHOR   2 J.K.EVERETT,G.ACTON,T.B.,KORNHABER,G.T.MONTELIONE,J.F.HUNT,L.TONG,
AUTHOR   3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT   1   24-JUL-13 4KYV    0
JRNL        AUTH   A.KUZIN,S.LEW,J.SEETHARAMAN,M.MAGLAQUI,R.XIAO,E.KOHAN,
JRNL        AUTH 2 H.WANG,J.K.EVERETT,G.ACTON,T.B.,KORNHABER,G.T.MONTELIONE,
JRNL        AUTH 3 J.F.HUNT,L.TONG
JRNL        TITL   NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR150
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1269)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.61
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.460
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2
REMARK   3   NUMBER OF REFLECTIONS             : 101600
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154
REMARK   3   R VALUE            (WORKING SET) : 0.153
REMARK   3   FREE R VALUE                     : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.790
REMARK   3   FREE R VALUE TEST SET COUNT      : 3853
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 29.6140 -  5.4440    0.94     3477   136  0.1580 0.1740
REMARK   3     2  5.4440 -  4.3250    0.96     3534   147  0.1250 0.1610
REMARK   3     3  4.3250 -  3.7800    0.97     3629   139  0.1270 0.1400
REMARK   3     4  3.7800 -  3.4350    0.98     3649   136  0.1420 0.1380
REMARK   3     5  3.4350 -  3.1890    0.97     3584   131  0.1450 0.1850
REMARK   3     6  3.1890 -  3.0010    0.97     3602   151  0.1510 0.1780
REMARK   3     7  3.0010 -  2.8510    0.98     3584   143  0.1540 0.2110
REMARK   3     8  2.8510 -  2.7270    0.97     3597   139  0.1480 0.1730
REMARK   3     9  2.7270 -  2.6220    0.97     3619   140  0.1490 0.2000
REMARK   3    10  2.6220 -  2.5320    0.97     3574   144  0.1490 0.1940
REMARK   3    11  2.5320 -  2.4520    0.96     3621   137  0.1490 0.1930
REMARK   3    12  2.4520 -  2.3820    0.96     3469   143  0.1450 0.1640
REMARK   3    13  2.3820 -  2.3200    0.95     3585   148  0.1460 0.1760
REMARK   3    14  2.3200 -  2.2630    0.95     3483   131  0.1450 0.1930
REMARK   3    15  2.2630 -  2.2120    0.94     3512   132  0.1540 0.1800
REMARK   3    16  2.2120 -  2.1650    0.94     3445   148  0.1540 0.1920
REMARK   3    17  2.1650 -  2.1210    0.93     3488   144  0.1590 0.2120
REMARK   3    18  2.1210 -  2.0810    0.93     3466   119  0.1620 0.2210
REMARK   3    19  2.0810 -  2.0440    0.93     3363   147  0.1640 0.2240
REMARK   3    20  2.0440 -  2.0100    0.92     3509   116  0.1720 0.2060
REMARK   3    21  2.0100 -  1.9770    0.93     3390   154  0.1690 0.2240
REMARK   3    22  1.9770 -  1.9470    0.92     3407   120  0.1790 0.2410
REMARK   3    23  1.9470 -  1.9180    0.91     3449   132  0.1800 0.2260
REMARK   3    24  1.9180 -  1.8910    0.92     3333   138  0.1880 0.2370
REMARK   3    25  1.8910 -  1.8650    0.92     3375   141  0.1900 0.2570
REMARK   3    26  1.8650 -  1.8410    0.91     3428   121  0.1970 0.2460
REMARK   3    27  1.8410 -  1.8180    0.91     3325   127  0.2050 0.2470
REMARK   3    28  1.8180 -  1.7960    0.88     3250   149  0.2120 0.2610
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)     : 0.170
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.030
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 13.43
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.57
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      :  0.007           5010
REMARK   3   ANGLE     :  1.122           6853
REMARK   3   CHIRALITY :  0.077            715
REMARK   3   PLANARITY :  0.007            901
REMARK   3   DIHEDRAL  : 12.773           1825
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):  10.4718  10.2827  20.2585
REMARK   3    T TENSOR
REMARK   3      T11:   0.0832 T22:   0.0984
REMARK   3      T33:   0.1173 T12:  -0.0007
REMARK   3      T13:  -0.0134 T23:   0.0082
REMARK   3    L TENSOR
REMARK   3      L11:   0.1144 L22:   0.3206
REMARK   3      L33:   0.5163 L12:  -0.1004
REMARK   3      L13:  -0.1862 L23:   0.2758
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0066 S12:   0.0090 S13:   0.0057
REMARK   3      S21:  -0.0075 S22:  -0.0203 S23:   0.0221
REMARK   3      S31:  -0.0009 S32:  -0.0161 S33:   0.0304
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 4KYV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079967.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X4A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56625
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.760
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6
REMARK 200  DATA REDUNDANCY                : 3.900
REMARK 200  R MERGE                    (I) : 0.09700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 26.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 4KAC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM DTT,
REMARK 280  0.02% NAN3, 10MM TRIS-HCL (PH 7.5) . RESERVOIR SOLUTION:.1M
REMARK 280  NH4NO3 .1M SODIUM ACETATE 24% PEG 20000 , MICROBATCH UNDER OIL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.38500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MSE A     1
REMARK 465     GLY A     2
REMARK 465     HIS A     3
REMARK 465     SER A     9
REMARK 465     HIS A    10
REMARK 465     MSE A    11
REMARK 465     GLY A    12
REMARK 465     SER A    13
REMARK 465     MSE B     1
REMARK 465     GLY B     2
REMARK 465     HIS B     3
REMARK 465     HIS B    10
REMARK 465     MSE B    11
REMARK 465     GLY B    12
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     SER B  13    OG
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   OD1  ASP B    42     NH2  ARG B   157     2546     2.16
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  53       49.81    -99.94
REMARK 500    THR A  54     -160.06   -108.12
REMARK 500    SER A  55     -168.77   -161.54
REMARK 500    GLU A 109      -94.00   -104.96
REMARK 500    ASP A 117     -127.08     54.00
REMARK 500    ARG A 164       47.89    -88.91
REMARK 500    ASP A 167      -72.67    -97.76
REMARK 500    VAL A 256      -67.87   -136.26
REMARK 500    LEU A 282      -93.94   -118.51
REMARK 500    PRO B  53       50.18   -100.51
REMARK 500    THR B  54     -158.32   -109.36
REMARK 500    SER B  55     -169.40   -162.66
REMARK 500    GLU B 109      -91.05   -110.66
REMARK 500    ASP B 117     -129.48     54.37
REMARK 500    ARG B 164       41.65    -89.79
REMARK 500    ASP B 167      -72.65    -97.39
REMARK 500    VAL B 256      -68.33   -138.40
REMARK 500    LEU B 282      -96.67   -120.47
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                              NA B 403  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B  52   OD1
REMARK 620 2 LEU B 213   O   148.7
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA A 402  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 291   OD1
REMARK 620 2 HOH A 599   O   143.4
REMARK 620 3 ASN A  61   O   151.2  58.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B 402  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 291   OD1
REMARK 620 2 HOH B 623   O   138.4
REMARK 620 3 ASN B  61   O   156.5  57.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA A 403  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 213   O
REMARK 620 2 ASN A  52   OD1 119.2
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q9 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q9 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KAC   RELATED DB: PDB
REMARK 900 100% IDENTITY
REMARK 900 RELATED ID: NESG-OR150   RELATED DB: TARGETTRACK
DBREF  4KYV A    1   306  PDB    4KYV     4KYV             1    306
DBREF  4KYV B    1   306  PDB    4KYV     4KYV             1    306
SEQRES   1 A  306  MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE GLY SER
SEQRES   2 A  306  GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES   3 A  306  GLU VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY
SEQRES   4 A  306  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES   5 A  306  PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS
SEQRES   6 A  306  VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES   7 A  306  GLY MSE GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE
SEQRES   8 A  306  PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU
SEQRES   9 A  306  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES  10 A  306  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES  11 A  306  PRO GLU ARG VAL LYS GLY ILE ALA CYS MSE GLU PHE ILE
SEQRES  12 A  306  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES  13 A  306  ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY
SEQRES  14 A  306  ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY
SEQRES  15 A  306  ALA LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES  16 A  306  GLU MSE ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES  17 A  306  ASP ARG GLU PRO LEU TRP ARG LEU PRO ASN GLU LEU PRO
SEQRES  18 A  306  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES  19 A  306  ALA TYR MSE ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES  20 A  306  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES  21 A  306  ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS
SEQRES  22 A  306  LYS THR VAL ASP ILE GLY PRO GLY LEU PHE LEU LEU GLN
SEQRES  23 A  306  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES  24 A  306  TRP LEU PRO GLY LEU ALA GLY
SEQRES   1 B  306  MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE GLY SER
SEQRES   2 B  306  GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES   3 B  306  GLU VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY
SEQRES   4 B  306  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES   5 B  306  PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS
SEQRES   6 B  306  VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES   7 B  306  GLY MSE GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE
SEQRES   8 B  306  PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU
SEQRES   9 B  306  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES  10 B  306  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES  11 B  306  PRO GLU ARG VAL LYS GLY ILE ALA CYS MSE GLU PHE ILE
SEQRES  12 B  306  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES  13 B  306  ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY
SEQRES  14 B  306  ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY
SEQRES  15 B  306  ALA LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES  16 B  306  GLU MSE ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES  17 B  306  ASP ARG GLU PRO LEU TRP ARG LEU PRO ASN GLU LEU PRO
SEQRES  18 B  306  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES  19 B  306  ALA TYR MSE ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES  20 B  306  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES  21 B  306  ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS
SEQRES  22 B  306  LYS THR VAL ASP ILE GLY PRO GLY LEU PHE LEU LEU GLN
SEQRES  23 B  306  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES  24 B  306  TRP LEU PRO GLY LEU ALA GLY
MODRES 4KYV MSE A   33  MET  SELENOMETHIONINE
MODRES 4KYV MSE A   80  MET  SELENOMETHIONINE
MODRES 4KYV MSE A  140  MET  SELENOMETHIONINE
MODRES 4KYV MSE A  186  MET  SELENOMETHIONINE
MODRES 4KYV MSE A  197  MET  SELENOMETHIONINE
MODRES 4KYV MSE A  237  MET  SELENOMETHIONINE
MODRES 4KYV MSE B   33  MET  SELENOMETHIONINE
MODRES 4KYV MSE B   80  MET  SELENOMETHIONINE
MODRES 4KYV MSE B  140  MET  SELENOMETHIONINE
MODRES 4KYV MSE B  186  MET  SELENOMETHIONINE
MODRES 4KYV MSE B  197  MET  SELENOMETHIONINE
MODRES 4KYV MSE B  237  MET  SELENOMETHIONINE
HET    MSE  A  33       8
HET    MSE  A  80       8
HET    MSE  A 140       8
HET    MSE  A 186       8
HET    MSE  A 197      13
HET    MSE  A 237       8
HET    MSE  B  33       8
HET    MSE  B  80       8
HET    MSE  B 140       8
HET    MSE  B 186       8
HET    MSE  B 197       8
HET    MSE  B 237       8
HET    1Q9  A 401      18
HET     NA  A 402       1
HET     NA  A 403       1
HET    1Q9  B 401      18
HET     NA  B 402       1
HET     NA  B 403       1
HETNAM     MSE SELENOMETHIONINE
HETNAM     1Q9 N-(2-ETHOXY-3,5-DIMETHYLBENZYL)-1H-TETRAZOL-5-AMINE
HETNAM      NA SODIUM ION
FORMUL   1  MSE    12(C5 H11 N O2 SE)
FORMUL   3  1Q9    2(C12 H17 N5 O)
FORMUL   4   NA    4(NA 1+)
FORMUL   9  HOH   *680(H2 O)
HELIX    1   1 SER A   55  ARG A   60  5                                   6
HELIX    2   2 ILE A   62  ALA A   67  1                                   6
HELIX    3   3 PHE A   91  LEU A  106  1                                  16
HELIX    4   4 ASP A  117  ASN A  130  1                                  14
HELIX    5   5 THR A  148  TRP A  152  5                                   5
HELIX    6   6 PRO A  153  PHE A  155  5                                   3
HELIX    7   7 ALA A  156  ARG A  164  1                                   9
HELIX    8   8 ASP A  167  ILE A  174  1                                   8
HELIX    9   9 ASN A  177  GLY A  182  1                                   6
HELIX   10  10 GLY A  182  GLY A  187  1                                   6
HELIX   11  11 THR A  193  GLU A  202  1                                  10
HELIX   12  12 PRO A  203  LEU A  205  5                                   3
HELIX   13  13 LYS A  206  ASP A  209  5                                   4
HELIX   14  14 ARG A  210  LEU A  220  1                                  11
HELIX   15  15 PRO A  226  SER A  243  1                                  18
HELIX   16  16 PRO A  259  LEU A  270  1                                  12
HELIX   17  17 LEU A  284  ASN A  289  1                                   6
HELIX   18  18 ASN A  289  LEU A  301  1                                  13
HELIX   19  19 PRO A  302  ALA A  305  5                                   4
HELIX   20  20 SER B   55  ARG B   60  5                                   6
HELIX   21  21 ILE B   62  ALA B   67  1                                   6
HELIX   22  22 PHE B   91  GLY B  107  1                                  17
HELIX   23  23 ASP B  117  ASN B  130  1                                  14
HELIX   24  24 THR B  148  TRP B  152  5                                   5
HELIX   25  25 PRO B  153  ARG B  164  1                                  12
HELIX   26  26 ASP B  167  ILE B  174  1                                   8
HELIX   27  27 ASN B  177  GLY B  182  1                                   6
HELIX   28  28 GLY B  182  GLY B  187  1                                   6
HELIX   29  29 THR B  193  GLU B  202  1                                  10
HELIX   30  30 PRO B  203  LEU B  205  5                                   3
HELIX   31  31 LYS B  206  ASP B  209  5                                   4
HELIX   32  32 ARG B  210  LEU B  216  1                                   7
HELIX   33  33 PRO B  217  LEU B  220  5                                   4
HELIX   34  34 PRO B  226  SER B  243  1                                  18
HELIX   35  35 PRO B  259  LEU B  270  1                                  12
HELIX   36  36 LEU B  284  ASP B  288  5                                   5
HELIX   37  37 ASN B  289  LEU B  301  1                                  13
HELIX   38  38 PRO B  302  ALA B  305  5                                   4
SHEET    1   A 8 HIS A  24  VAL A  28  0
SHEET    2   A 8 GLU A  31  VAL A  38 -1  O  GLU A  31   N  VAL A  28
SHEET    3   A 8 CYS A  72  PRO A  75 -1  O  CYS A  72   N  VAL A  38
SHEET    4   A 8 VAL A  46  LEU A  49  1  N  PHE A  48   O  ILE A  73
SHEET    5   A 8 VAL A 111  HIS A 116  1  O  VAL A 112   N  LEU A  47
SHEET    6   A 8 VAL A 134  MSE A 140  1  O  ALA A 138   N  LEU A 113
SHEET    7   A 8 LYS A 247  PRO A 254  1  O  LEU A 248   N  CYS A 139
SHEET    8   A 8 CYS A 273  GLY A 281  1  O  LYS A 274   N  LEU A 249
SHEET    1   B 8 HIS B  24  VAL B  28  0
SHEET    2   B 8 GLU B  31  VAL B  38 -1  O  GLU B  31   N  VAL B  28
SHEET    3   B 8 CYS B  72  PRO B  75 -1  O  CYS B  72   N  VAL B  38
SHEET    4   B 8 VAL B  46  LEU B  49  1  N  PHE B  48   O  ILE B  73
SHEET    5   B 8 VAL B 111  HIS B 116  1  O  VAL B 112   N  LEU B  47
SHEET    6   B 8 VAL B 134  MSE B 140  1  O  ALA B 138   N  LEU B 113
SHEET    7   B 8 LYS B 247  PRO B 254  1  O  LEU B 248   N  CYS B 139
SHEET    8   B 8 CYS B 273  GLY B 281  1  O  LYS B 274   N  LEU B 249
LINK         C   ARG A  32                 N   MSE A  33     1555   1555  1.33
LINK         C   MSE A  33                 N   HIS A  34     1555   1555  1.32
LINK         C   GLY A  79                 N   MSE A  80     1555   1555  1.33
LINK         C   MSE A  80                 N   GLY A  81     1555   1555  1.33
LINK         C   CYS A 139                 N   MSE A 140     1555   1555  1.33
LINK         C   MSE A 140                 N   GLU A 141     1555   1555  1.33
LINK         C   PRO A 185                 N   MSE A 186     1555   1555  1.33
LINK         C   MSE A 186                 N   GLY A 187     1555   1555  1.33
LINK         C   GLU A 196                 N   MSE A 197     1555   1555  1.33
LINK         C   MSE A 197                 N   ASP A 198     1555   1555  1.33
LINK         C   TYR A 236                 N   MSE A 237     1555   1555  1.33
LINK         C   MSE A 237                 N   ASN A 238     1555   1555  1.34
LINK         C   ARG B  32                 N   MSE B  33     1555   1555  1.33
LINK         C   MSE B  33                 N   HIS B  34     1555   1555  1.32
LINK         C   GLY B  79                 N   MSE B  80     1555   1555  1.33
LINK         C   MSE B  80                 N   GLY B  81     1555   1555  1.33
LINK         C   CYS B 139                 N   MSE B 140     1555   1555  1.33
LINK         C   MSE B 140                 N   GLU B 141     1555   1555  1.33
LINK         C   PRO B 185                 N   MSE B 186     1555   1555  1.33
LINK         C   MSE B 186                 N   GLY B 187     1555   1555  1.33
LINK         C   GLU B 196                 N   MSE B 197     1555   1555  1.33
LINK         C   MSE B 197                 N   ASP B 198     1555   1555  1.33
LINK         C   TYR B 236                 N   MSE B 237     1555   1555  1.33
LINK         C   MSE B 237                 N   ASN B 238     1555   1555  1.33
LINK         OD1 ASN B  52                NA    NA B 403     1555   1555  2.19
LINK         OD1 ASP A 291                NA    NA A 402     1555   1555  2.22
LINK         OD1 ASP B 291                NA    NA B 402     1555   1555  2.27
LINK         O   LEU B 213                NA    NA B 403     1555   1555  2.59
LINK         O   LEU A 213                NA    NA A 403     1555   1555  2.67
LINK         OD1 ASN A  52                NA    NA A 403     1555   1555  2.76
LINK        NA    NA A 402                 O   HOH A 599     1555   1555  2.88
LINK        NA    NA B 402                 O   HOH B 623     1555   1555  2.99
LINK         O   ASN B  61                NA    NA B 402     1555   1555  3.00
LINK         O   ASN A  61                NA    NA A 402     1555   1555  3.16
CISPEP   1 ASN A   52    PRO A   53          0       -11.41
CISPEP   2 GLU A  225    PRO A  226          0        -3.59
CISPEP   3 THR A  253    PRO A  254          0         6.88
CISPEP   4 ASN B   52    PRO B   53          0        -8.76
CISPEP   5 GLU B  225    PRO B  226          0        -3.18
CISPEP   6 THR B  253    PRO B  254          0         2.64
SITE     1 AC1 12 PRO A  53  ASP A 117  TRP A 118  TRP A 152
SITE     2 AC1 12 ALA A 156  PHE A 160  PHE A 179  ALA A 183
SITE     3 AC1 12 PRO A 217  LEU A 220  VAL A 256  PHE A 283
SITE     1 AC2  4 ASN A  61  HIS A  65  ASP A 291  HOH A 599
SITE     1 AC3  4 ASN A  52  PHE A 179  LEU A 213  PRO A 217
SITE     1 AC4 13 ASN B  52  PRO B  53  ASP B 117  TRP B 118
SITE     2 AC4 13 TRP B 152  PHE B 160  PHE B 179  ALA B 183
SITE     3 AC4 13 MSE B 186  PRO B 217  LEU B 220  VAL B 256
SITE     4 AC4 13 PHE B 283
SITE     1 AC5  4 ASN B  61  HIS B  65  ASP B 291  HOH B 623
SITE     1 AC6  4 ASN B  52  PHE B 179  LEU B 213  PRO B 217
CRYST1   42.938   94.770   73.483  90.00  93.11  90.00 P 1 21 1      4
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      0.023289  0.000000  0.001267        0.00000
SCALE2      0.000000  0.010552  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013629        0.00000
TER    2406      GLY A 306
TER    4805      GLY B 306
MASTER      380    0   18   38   16    0   11    6 5505    2  175   48
END