| content |
HEADER HYDROLASE 22-APR-13 4KAF
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE HALOTAG7 AT THE
TITLE 2 RESOLUTION 1.5A, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
TITLE 3 TARGET OR151
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.P.KUZIN,S.LEW,T.K.NEKLESA,D.NOBLIN,J.SEETHARAMAN,M.MAGLAQUI,R.XIAO,
AUTHOR 2 E.KOHAN,H.WANG,J.K.EVERETT,T.B.ACTON,G.KORNHABER,G.T.MONTELIONE,
AUTHOR 3 C.CREWS,L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 1 05-JUN-13 4KAF 0
JRNL AUTH A.P.KUZIN,S.LEW,T.K.NEKLESA,D.NOBLIN,J.SEETHARAMAN,
JRNL AUTH 2 M.MAGLAQUI,R.XIAO,E.KOHAN,H.WANG,J.K.EVERETT,T.B.ACTON,
JRNL AUTH 3 G.KORNHABER,G.T.MONTELIONE,C.CREWS,L.TONG
JRNL TITL NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR151
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 203210
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3857
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 44.4186 - 4.5412 0.99 7136 146 0.1806 0.1895
REMARK 3 2 4.5412 - 3.6050 1.00 7197 137 0.1424 0.1772
REMARK 3 3 3.6050 - 3.1494 1.00 7190 133 0.1498 0.1902
REMARK 3 4 3.1494 - 2.8615 1.00 7197 140 0.1526 0.1505
REMARK 3 5 2.8615 - 2.6565 1.00 7183 147 0.1439 0.1391
REMARK 3 6 2.6565 - 2.4999 1.00 7208 136 0.1441 0.1668
REMARK 3 7 2.4999 - 2.3747 1.00 7182 136 0.1364 0.1458
REMARK 3 8 2.3747 - 2.2713 1.00 7227 142 0.1370 0.1526
REMARK 3 9 2.2713 - 2.1839 1.00 7207 145 0.1413 0.1665
REMARK 3 10 2.1839 - 2.1085 1.00 7168 128 0.1406 0.1549
REMARK 3 11 2.1085 - 2.0426 1.00 7205 151 0.1410 0.1850
REMARK 3 12 2.0426 - 1.9842 1.00 7173 132 0.1381 0.1476
REMARK 3 13 1.9842 - 1.9320 1.00 7168 154 0.1418 0.1582
REMARK 3 14 1.9320 - 1.8848 1.00 7225 119 0.1383 0.1266
REMARK 3 15 1.8848 - 1.8420 1.00 7172 142 0.1385 0.1659
REMARK 3 16 1.8420 - 1.8028 1.00 7162 147 0.1388 0.1597
REMARK 3 17 1.8028 - 1.7667 1.00 7178 130 0.1392 0.1477
REMARK 3 18 1.7667 - 1.7334 1.00 7199 136 0.1460 0.1686
REMARK 3 19 1.7334 - 1.7024 1.00 7164 139 0.1516 0.1806
REMARK 3 20 1.7024 - 1.6736 0.99 7133 125 0.1482 0.1525
REMARK 3 21 1.6736 - 1.6466 1.00 7151 152 0.1509 0.1692
REMARK 3 22 1.6466 - 1.6212 0.99 7190 137 0.1487 0.1347
REMARK 3 23 1.6212 - 1.5974 0.99 7084 162 0.1520 0.1628
REMARK 3 24 1.5974 - 1.5749 0.99 7148 111 0.1542 0.2037
REMARK 3 25 1.5749 - 1.5536 0.99 7104 126 0.1610 0.1815
REMARK 3 26 1.5536 - 1.5334 0.99 7152 160 0.1684 0.1542
REMARK 3 27 1.5334 - 1.5142 0.95 6875 146 0.1841 0.1917
REMARK 3 28 1.5142 - 1.4960 0.83 5975 98 0.1939 0.2246
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) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17100
REMARK 3 B22 (A**2) : 0.20000
REMARK 3 B33 (A**2) : -0.02900
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 : 0.009 5035
REMARK 3 ANGLE : 1.364 6883
REMARK 3 CHIRALITY : 0.079 727
REMARK 3 PLANARITY : 0.008 909
REMARK 3 DIHEDRAL : 12.134 1858
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): 0.1329 -31.3022 25.4694
REMARK 3 T TENSOR
REMARK 3 T11: 0.0616 T22: 0.0493
REMARK 3 T33: 0.0775 T12: 0.0017
REMARK 3 T13: -0.0056 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.2038 L22: 0.1399
REMARK 3 L33: 0.4888 L12: 0.0192
REMARK 3 L13: -0.1150 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0096 S12: -0.0018 S13: -0.0114
REMARK 3 S21: -0.0015 S22: 0.0038 S23: 0.0021
REMARK 3 S31: 0.0181 S32: 0.0017 S33: 0.0077
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 4KAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB079093.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
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 : NULL
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 203311
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.496
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 36.6000
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 4E46
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
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: AMMONIUM
REMARK 280 THIOCYNATE, MES 0.1M, PEG 4000 20%, MICROBATCH UNDER OIL,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 34.46500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.25100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.25100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.46500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.40000
REMARK 290 SMTRY3 4 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 300 REMARK: MONOMER,35.49 KD,99.1%
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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 SER A 9
REMARK 465 HIS A 10
REMARK 465 MSE A 11
REMARK 465 MSE B -9
REMARK 465 GLY B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
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 PHE B 20 O1 EDO B 405 2.14
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 52 45.17 -105.67
REMARK 500 GLU A 108 -95.19 -107.16
REMARK 500 ASP A 116 -134.71 58.18
REMARK 500 ASP A 166 -49.99 72.34
REMARK 500 VAL A 255 -62.93 -131.48
REMARK 500 LEU A 281 -98.92 -116.45
REMARK 500 PRO B 52 46.26 -108.54
REMARK 500 GLU B 108 -93.21 -107.97
REMARK 500 ASP B 116 -135.16 57.50
REMARK 500 ASP B 166 -55.36 73.92
REMARK 500 VAL B 255 -68.30 -127.86
REMARK 500 LEU B 281 -100.12 -119.02
REMARK 500 SER B 306 35.46 117.57
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 A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 224 OE2
REMARK 620 2 HOH B 581 O 108.7
REMARK 620 3 HOH A 715 O 105.0 108.8
REMARK 620 4 HOH A 536 O 148.0 76.5 102.7
REMARK 620 N 1 2 3
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 GLU B 224 OE2
REMARK 620 2 HOH A 592 O 120.8
REMARK 620 3 HOH B 736 O 99.9 113.0
REMARK 620 4 HOH B 540 O 143.4 77.5 100.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 21 OD2
REMARK 620 2 ASP A 21 OD1 58.3
REMARK 620 3 ASP A 36 O 144.2 149.0
REMARK 620 4 HOH A 523 O 98.5 84.3 72.6
REMARK 620 N 1 2 3
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 HOH B 590 O
REMARK 620 2 HOH B 792 O 117.9
REMARK 620 N 1
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 PRO A 184 O
REMARK 620 2 ARG A 189 O 131.1
REMARK 620 3 VAL A 187 O 67.2 69.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN 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 NA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E46 RELATED DB: PDB
REMARK 900 HOMOLOGY IS 92.49%
REMARK 900 RELATED ID: NESG-OR151 RELATED DB: TARGETTRACK
DBREF 4KAF A 9 303 UNP P0A3G3 DHAA_RHOSO 2 293
DBREF 4KAF B -1 303 UNP P0A3G3 DHAA_RHOSO 2 293
SEQADV 4KAF MSE A 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF GLY A 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS A 4 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS A 5 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS A 6 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS A 7 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS A 8 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS A 10 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF MSE A 11 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF ALA A 12 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF VAL A 57 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 4KAF THR A 68 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 4KAF GLY A 88 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 4KAF PHE A 97 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 4KAF MSE A 98 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 4KAF ILE A 133 UNP P0A3G3 VAL 123 ENGINEERED MUTATION
SEQADV 4KAF PHE A 138 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 4KAF THR A 165 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 4KAF LYS A 170 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 4KAF VAL A 177 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 4KAF THR A 182 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 4KAF MSE A 185 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 4KAF GLY A 186 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 4KAF ASN A 205 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 4KAF GLU A 234 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 4KAF ASP A 237 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 4KAF LYS A 267 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 4KAF ALA A 274 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 4KAF ASN A 282 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 4KAF LEU A 283 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 4KAF SER A 301 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 4KAF THR A 302 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 4KAF GLU A 304 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF ILE A 305 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF SER A 306 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF GLY A 307 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF MSE B -9 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF GLY B -8 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS B -7 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS B -6 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS B -5 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS B -4 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS B -3 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS B -2 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF HIS B 0 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF MSE B 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF ALA B 12 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF VAL B 57 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 4KAF THR B 68 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 4KAF GLY B 88 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 4KAF PHE B 97 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 4KAF MSE B 98 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 4KAF ILE B 133 UNP P0A3G3 VAL 123 ENGINEERED MUTATION
SEQADV 4KAF PHE B 138 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 4KAF THR B 165 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 4KAF LYS B 170 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 4KAF VAL B 177 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 4KAF THR B 182 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 4KAF MSE B 185 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 4KAF GLY B 186 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 4KAF ASN B 205 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 4KAF GLU B 234 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 4KAF ASP B 237 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 4KAF LYS B 267 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 4KAF ALA B 274 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 4KAF ASN B 282 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 4KAF LEU B 283 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 4KAF SER B 301 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 4KAF THR B 302 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 4KAF GLU B 304 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF ILE B 305 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF SER B 306 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAF GLY B 307 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 307 MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE ALA GLU
SEQRES 2 A 307 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 3 A 307 VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY PRO
SEQRES 4 A 307 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 5 A 307 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 6 A 307 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 7 A 307 MSE GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 8 A 307 ASP ASP HIS VAL ARG PHE MSE ASP ALA PHE ILE GLU ALA
SEQRES 9 A 307 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 10 A 307 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 11 A 307 GLU ARG ILE LYS GLY ILE ALA PHE MSE GLU PHE ILE ARG
SEQRES 12 A 307 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 13 A 307 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 14 A 307 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 15 A 307 LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 16 A 307 MSE ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 17 A 307 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 18 A 307 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 19 A 307 TYR MSE ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 20 A 307 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 21 A 307 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 22 A 307 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 23 A 307 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 24 A 307 LEU SER THR LEU GLU ILE SER GLY
SEQRES 1 B 307 MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE ALA GLU
SEQRES 2 B 307 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 3 B 307 VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY PRO
SEQRES 4 B 307 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 5 B 307 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 6 B 307 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 7 B 307 MSE GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 8 B 307 ASP ASP HIS VAL ARG PHE MSE ASP ALA PHE ILE GLU ALA
SEQRES 9 B 307 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 10 B 307 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 11 B 307 GLU ARG ILE LYS GLY ILE ALA PHE MSE GLU PHE ILE ARG
SEQRES 12 B 307 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 13 B 307 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 14 B 307 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 15 B 307 LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 16 B 307 MSE ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 17 B 307 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 18 B 307 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 19 B 307 TYR MSE ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 20 B 307 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 21 B 307 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 22 B 307 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 23 B 307 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 24 B 307 LEU SER THR LEU GLU ILE SER GLY
MODRES 4KAF MSE A 32 MET SELENOMETHIONINE
MODRES 4KAF MSE A 79 MET SELENOMETHIONINE
MODRES 4KAF MSE A 98 MET SELENOMETHIONINE
MODRES 4KAF MSE A 139 MET SELENOMETHIONINE
MODRES 4KAF MSE A 185 MET SELENOMETHIONINE
MODRES 4KAF MSE A 196 MET SELENOMETHIONINE
MODRES 4KAF MSE A 236 MET SELENOMETHIONINE
MODRES 4KAF MSE B 1 MET SELENOMETHIONINE
MODRES 4KAF MSE B 32 MET SELENOMETHIONINE
MODRES 4KAF MSE B 79 MET SELENOMETHIONINE
MODRES 4KAF MSE B 98 MET SELENOMETHIONINE
MODRES 4KAF MSE B 139 MET SELENOMETHIONINE
MODRES 4KAF MSE B 185 MET SELENOMETHIONINE
MODRES 4KAF MSE B 196 MET SELENOMETHIONINE
MODRES 4KAF MSE B 236 MET SELENOMETHIONINE
HET MSE A 32 17
HET MSE A 79 31
HET MSE A 98 17
HET MSE A 139 17
HET MSE A 185 34
HET MSE A 196 17
HET MSE A 236 17
HET MSE B 1 17
HET MSE B 32 17
HET MSE B 79 34
HET MSE B 98 17
HET MSE B 139 17
HET MSE B 185 17
HET MSE B 196 17
HET MSE B 236 17
HET SCN A 401 3
HET SCN B 401 3
HET NA A 402 1
HET NA A 403 1
HET NA A 404 1
HET NA A 405 1
HET NA B 402 1
HET NA B 403 1
HET EDO B 404 4
HET EDO B 405 4
HET PEG B 406 14
HETNAM MSE SELENOMETHIONINE
HETNAM SCN THIOCYANATE ION
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 15(C5 H11 N O2 SE)
FORMUL 3 SCN 2(C N S 1-)
FORMUL 5 NA 6(NA 1+)
FORMUL 11 EDO 2(C2 H6 O2)
FORMUL 13 PEG C4 H10 O3
FORMUL 14 HOH *686(H2 O)
HELIX 1 1 SER A 54 ARG A 59 5 6
HELIX 2 2 ILE A 61 ALA A 66 1 6
HELIX 3 3 PHE A 90 LEU A 105 1 16
HELIX 4 4 ASP A 116 ASN A 129 1 14
HELIX 5 5 THR A 147 TRP A 151 5 5
HELIX 6 6 PRO A 152 ARG A 163 1 12
HELIX 7 7 ASP A 166 ILE A 173 1 8
HELIX 8 8 ASN A 176 GLY A 181 1 6
HELIX 9 9 LEU A 183 VAL A 187 5 5
HELIX 10 10 THR A 192 GLU A 201 1 10
HELIX 11 11 PRO A 202 LEU A 204 5 3
HELIX 12 12 ASN A 205 ASP A 208 5 4
HELIX 13 13 ARG A 209 LEU A 219 1 11
HELIX 14 14 PRO A 225 SER A 242 1 18
HELIX 15 15 PRO A 258 LEU A 269 1 12
HELIX 16 16 LEU A 283 ASN A 288 1 6
HELIX 17 17 ASN A 288 SER A 301 1 14
HELIX 18 18 SER B 54 ARG B 59 5 6
HELIX 19 19 ILE B 61 ALA B 66 1 6
HELIX 20 20 PHE B 90 LEU B 105 1 16
HELIX 21 21 ASP B 116 ASN B 129 1 14
HELIX 22 22 THR B 147 TRP B 151 5 5
HELIX 23 23 PRO B 152 ARG B 163 1 12
HELIX 24 24 ASP B 166 ILE B 173 1 8
HELIX 25 25 ASN B 176 GLY B 181 1 6
HELIX 26 26 GLY B 181 GLY B 186 1 6
HELIX 27 27 THR B 192 GLU B 201 1 10
HELIX 28 28 PRO B 202 LEU B 204 5 3
HELIX 29 29 ASN B 205 ASP B 208 5 4
HELIX 30 30 ARG B 209 LEU B 219 1 11
HELIX 31 31 PRO B 225 SER B 242 1 18
HELIX 32 32 PRO B 258 LEU B 269 1 12
HELIX 33 33 LEU B 283 ASN B 288 1 6
HELIX 34 34 ASN B 288 SER B 301 1 14
SHEET 1 A 8 HIS A 23 VAL A 27 0
SHEET 2 A 8 GLU A 30 VAL A 37 -1 O GLU A 30 N VAL A 27
SHEET 3 A 8 CYS A 71 PRO A 74 -1 O CYS A 71 N VAL A 37
SHEET 4 A 8 VAL A 45 LEU A 48 1 N PHE A 47 O ILE A 72
SHEET 5 A 8 VAL A 110 HIS A 115 1 O VAL A 111 N LEU A 46
SHEET 6 A 8 ILE A 133 MSE A 139 1 O ALA A 137 N LEU A 112
SHEET 7 A 8 LYS A 246 PRO A 253 1 O LEU A 247 N PHE A 138
SHEET 8 A 8 CYS A 272 GLY A 280 1 O ILE A 277 N TRP A 250
SHEET 1 B 8 HIS B 23 VAL B 27 0
SHEET 2 B 8 GLU B 30 VAL B 37 -1 O GLU B 30 N VAL B 27
SHEET 3 B 8 CYS B 71 PRO B 74 -1 O CYS B 71 N VAL B 37
SHEET 4 B 8 VAL B 45 LEU B 48 1 N PHE B 47 O ILE B 72
SHEET 5 B 8 VAL B 110 HIS B 115 1 O VAL B 111 N LEU B 46
SHEET 6 B 8 ILE B 133 MSE B 139 1 O ALA B 137 N LEU B 112
SHEET 7 B 8 LYS B 246 PRO B 253 1 O LEU B 247 N PHE B 138
SHEET 8 B 8 CYS B 272 GLY B 280 1 O VAL B 275 N LEU B 248
LINK C ARG A 31 N MSE A 32 1555 1555 1.33
LINK C MSE A 32 N HIS A 33 1555 1555 1.32
LINK C GLY A 78 N MSE A 79 1555 1555 1.33
LINK C MSE A 79 N GLY A 80 1555 1555 1.33
LINK C PHE A 97 N MSE A 98 1555 1555 1.33
LINK C MSE A 98 N ASP A 99 1555 1555 1.34
LINK C PHE A 138 N MSE A 139 1555 1555 1.33
LINK C MSE A 139 N GLU A 140 1555 1555 1.33
LINK C PRO A 184 N AMSE A 185 1555 1555 1.32
LINK C PRO A 184 N BMSE A 185 1555 1555 1.33
LINK C AMSE A 185 N GLY A 186 1555 1555 1.33
LINK C BMSE A 185 N GLY A 186 1555 1555 1.33
LINK C GLU A 195 N MSE A 196 1555 1555 1.33
LINK C MSE A 196 N ASP A 197 1555 1555 1.33
LINK C TYR A 235 N MSE A 236 1555 1555 1.33
LINK C MSE A 236 N ASP A 237 1555 1555 1.34
LINK C HIS B 0 N MSE B 1 1555 1555 1.32
LINK C MSE B 1 N ALA B 12 1555 1555 1.33
LINK C ARG B 31 N MSE B 32 1555 1555 1.33
LINK C MSE B 32 N HIS B 33 1555 1555 1.33
LINK C GLY B 78 N AMSE B 79 1555 1555 1.33
LINK C GLY B 78 N BMSE B 79 1555 1555 1.34
LINK C AMSE B 79 N GLY B 80 1555 1555 1.32
LINK C BMSE B 79 N GLY B 80 1555 1555 1.33
LINK C PHE B 97 N MSE B 98 1555 1555 1.33
LINK C MSE B 98 N ASP B 99 1555 1555 1.33
LINK C PHE B 138 N MSE B 139 1555 1555 1.32
LINK C MSE B 139 N GLU B 140 1555 1555 1.33
LINK C PRO B 184 N MSE B 185 1555 1555 1.32
LINK C MSE B 185 N GLY B 186 1555 1555 1.33
LINK C GLU B 195 N MSE B 196 1555 1555 1.33
LINK C MSE B 196 N ASP B 197 1555 1555 1.33
LINK C TYR B 235 N MSE B 236 1555 1555 1.33
LINK C MSE B 236 N ASP B 237 1555 1555 1.33
LINK OE2 GLU A 224 NA NA A 402 1555 1555 2.19
LINK OE2 GLU B 224 NA NA B 402 1555 1555 2.20
LINK OD2BASP A 21 NA NA A 404 1555 1555 2.24
LINK OD1BASP A 21 NA NA A 404 1555 1555 2.29
LINK NA NA B 403 O HOH B 590 1555 1555 2.65
LINK O PRO A 184 NA NA A 403 1555 1555 2.69
LINK NA NA B 402 O HOH A 592 1555 1555 2.73
LINK NA NA A 402 O HOH B 581 1555 1555 2.76
LINK O ARG A 189 NA NA A 403 1555 1555 2.78
LINK O ASP A 36 NA NA A 404 1555 1555 2.78
LINK NA NA A 402 O HOH A 715 1555 1555 2.79
LINK NA NA B 403 O HOH B 792 1555 1555 2.83
LINK NA NA B 402 O HOH B 736 1555 1555 2.86
LINK NA NA A 404 O HOH A 523 1555 1555 2.97
LINK O VAL A 187 NA NA A 403 1555 1555 3.12
LINK NA NA A 402 O HOH A 536 1555 1555 3.19
LINK NA NA B 402 O HOH B 540 1555 1555 3.19
CISPEP 1 ASN A 51 PRO A 52 0 -1.10
CISPEP 2 GLU A 224 PRO A 225 0 -5.59
CISPEP 3 THR A 252 PRO A 253 0 6.05
CISPEP 4 SER A 306 GLY A 307 0 -8.34
CISPEP 5 ASN B 51 PRO B 52 0 1.84
CISPEP 6 GLU B 224 PRO B 225 0 -6.15
CISPEP 7 THR B 252 PRO B 253 0 3.29
SITE 1 AC1 4 ASN A 51 ASP A 116 TRP A 117 PRO A 216
SITE 1 AC2 4 GLU A 224 ALA A 226 HOH A 715 HOH B 581
SITE 1 AC3 5 ARG A 40 PRO A 184 VAL A 187 ARG A 189
SITE 2 AC3 5 HOH A 534
SITE 1 AC4 6 ASP A 21 HIS A 23 ASP A 36 MSE A 185
SITE 2 AC4 6 NA A 405 HOH A 523
SITE 1 AC5 4 ASP A 21 VAL A 37 MSE A 185 NA A 404
SITE 1 AC6 5 ASN B 51 ASP B 116 TRP B 117 PHE B 215
SITE 2 AC6 5 PRO B 216
SITE 1 AC7 4 HOH A 592 GLU B 224 ALA B 226 HOH B 736
SITE 1 AC8 3 GLU B 153 HOH B 590 HOH B 792
SITE 1 AC9 7 PHE B 18 SER B 55 ASP B 75 LYS B 81
SITE 2 AC9 7 EDO B 405 HOH B 557 HOH B 744
SITE 1 BC1 7 PHE B 18 PHE B 20 PRO B 22 HIS B 33
SITE 2 BC1 7 LYS B 81 EDO B 404 HOH B 644
SITE 1 BC2 10 HOH A 595 PHE B 91 ASP B 92 ASN B 227
SITE 2 BC2 10 ILE B 228 LEU B 231 HOH B 522 HOH B 582
SITE 3 BC2 10 HOH B 589 HOH B 761
CRYST1 68.930 94.800 100.502 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014507 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010549 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009950 0.00000
TER 4786 GLY A 307
TER 9587 GLY B 307
MASTER 406 0 26 34 16 0 18 6 5477 2 384 48
END |