4KYV-pdb | 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
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