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HEADER HYDROLASE 20-NOV-12 4I19
TITLE THE CRYSTAL STRUCTURE OF AN EPOXIDE HYDROLASEN FROM STREPTOMYCES
TITLE 2 CARZINOSTATICUS SUBSP. NEOCARZINOSTATICUS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CARZINOSTATICUS SUBSP.
SOURCE 3 NEOCARZINOSTATICUS;
SOURCE 4 ORGANISM_TAXID: 167636;
SOURCE 5 STRAIN: SUBSP. NEOCARZINOSTATICUS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, ENZYME DISCOVERY FOR
KEYWDS 3 NATURAL PRODUCT BIOSYNTHESI, NATPRO, ENZYME DISCOVERY FOR NATURAL
KEYWDS 4 PRODUCT BIOSYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,L.BIGELOW,S.CLANCY,G.BABNIGG,C.A.BINGMAN,R.YENNAMALLI,J.LOHMAN,
AUTHOR 2 M.MA,B.SHEN,G.N.JR.PHILLIPS,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS (MCSG),ENZYME DISCOVERY FOR NATURAL PRODUCT
AUTHOR 4 BIOSYNTHESIS (NATPRO)
REVDAT 1 05-DEC-12 4I19 0
JRNL AUTH K.TAN,L.BIGELOW,S.CLANCY,G.BABNIGG,C.A.BINGMAN,R.YENNAMALLI,
JRNL AUTH 2 J.LOHMAN,M.MA,B.SHEN,G.N.JR.PHILLIPS,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF AN EPOXIDE HYDROLASEN FROM
JRNL TITL 2 STREPTOMYCES CARZINOSTATICUS SUBSP. NEOCARZINOSTATICUS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 26457
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1335
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 33.2662 - 4.6245 1.00 2735 133 0.1522 0.1749
REMARK 3 2 4.6245 - 3.6721 0.99 2566 131 0.1263 0.1459
REMARK 3 3 3.6721 - 3.2084 1.00 2508 146 0.1622 0.2131
REMARK 3 4 3.2084 - 2.9152 1.00 2487 146 0.1936 0.2613
REMARK 3 5 2.9152 - 2.7064 1.00 2499 144 0.1933 0.3006
REMARK 3 6 2.7064 - 2.5469 1.00 2475 135 0.1807 0.2369
REMARK 3 7 2.5469 - 2.4194 1.00 2519 128 0.1744 0.2105
REMARK 3 8 2.4194 - 2.3141 1.00 2473 118 0.1714 0.2363
REMARK 3 9 2.3141 - 2.2250 1.00 2457 138 0.1881 0.2747
REMARK 3 10 2.2250 - 2.1482 0.97 2403 116 0.1889 0.2325
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 34.85
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.75380
REMARK 3 B22 (A**2) : -7.75380
REMARK 3 B33 (A**2) : 15.50750
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 : 0.007 3145
REMARK 3 ANGLE : 1.040 4269
REMARK 3 CHIRALITY : 0.066 460
REMARK 3 PLANARITY : 0.005 558
REMARK 3 DIHEDRAL : 13.685 1134
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 0:21)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0171 -7.5907 51.1158
REMARK 3 T TENSOR
REMARK 3 T11: 0.3062 T22: 0.3663
REMARK 3 T33: 0.4822 T12: 0.0565
REMARK 3 T13: -0.0747 T23: -0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 1.6819 L22: 5.9088
REMARK 3 L33: 6.8951 L12: 0.3821
REMARK 3 L13: 1.3260 L23: 6.1366
REMARK 3 S TENSOR
REMARK 3 S11: 0.1554 S12: 0.2361 S13: -0.2985
REMARK 3 S21: 0.6337 S22: 0.4670 S23: -0.5294
REMARK 3 S31: 0.8212 S32: 0.8157 S33: -0.6489
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 22:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5161 -5.7175 29.5548
REMARK 3 T TENSOR
REMARK 3 T11: 0.3052 T22: 0.3783
REMARK 3 T33: 0.2966 T12: -0.0127
REMARK 3 T13: 0.0427 T23: -0.0949
REMARK 3 L TENSOR
REMARK 3 L11: 3.7415 L22: 2.3844
REMARK 3 L33: 2.5176 L12: 0.6833
REMARK 3 L13: 2.2674 L23: 0.4165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0769 S12: 0.5173 S13: -0.1786
REMARK 3 S21: -0.1819 S22: 0.0738 S23: -0.4061
REMARK 3 S31: 0.0694 S32: 0.5207 S33: -0.2201
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 52:162)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0125 10.4304 56.5378
REMARK 3 T TENSOR
REMARK 3 T11: 0.1846 T22: 0.2660
REMARK 3 T33: 0.2309 T12: 0.0087
REMARK 3 T13: -0.0201 T23: -0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 1.6274 L22: 2.1630
REMARK 3 L33: 0.9129 L12: 0.5339
REMARK 3 L13: 0.7590 L23: 0.4961
REMARK 3 S TENSOR
REMARK 3 S11: 0.0715 S12: -0.0123 S13: -0.0898
REMARK 3 S21: 0.1344 S22: -0.0234 S23: -0.0845
REMARK 3 S31: 0.0336 S32: 0.0341 S33: -0.0318
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resseq 163:230)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0107 20.9202 50.2570
REMARK 3 T TENSOR
REMARK 3 T11: 0.2140 T22: 0.1913
REMARK 3 T33: 0.3008 T12: -0.0099
REMARK 3 T13: 0.0213 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 2.8158 L22: 1.8846
REMARK 3 L33: 3.1736 L12: -0.2511
REMARK 3 L13: 1.2648 L23: -0.5440
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: -0.0560 S13: 0.1612
REMARK 3 S21: -0.0985 S22: 0.1012 S23: 0.1126
REMARK 3 S31: -0.1648 S32: -0.1096 S33: -0.0253
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resseq 231:339)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2374 6.1107 44.3114
REMARK 3 T TENSOR
REMARK 3 T11: 0.2646 T22: 0.2809
REMARK 3 T33: 0.2251 T12: -0.0055
REMARK 3 T13: -0.0349 T23: -0.0567
REMARK 3 L TENSOR
REMARK 3 L11: 1.2200 L22: 0.9240
REMARK 3 L33: 0.1711 L12: -0.0295
REMARK 3 L13: 0.1125 L23: -0.0954
REMARK 3 S TENSOR
REMARK 3 S11: 0.0266 S12: 0.0547 S13: -0.0360
REMARK 3 S21: -0.0495 S22: 0.0489 S23: -0.0808
REMARK 3 S31: 0.0263 S32: 0.0397 S33: -0.0843
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resseq 340:385)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6199 26.1218 47.9677
REMARK 3 T TENSOR
REMARK 3 T11: 0.2733 T22: 0.2559
REMARK 3 T33: 0.3319 T12: -0.0473
REMARK 3 T13: 0.0128 T23: -0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 3.6493 L22: 2.0816
REMARK 3 L33: 1.3731 L12: -0.6412
REMARK 3 L13: 0.1575 L23: 0.3642
REMARK 3 S TENSOR
REMARK 3 S11: 0.0659 S12: 0.0428 S13: 0.4137
REMARK 3 S21: -0.0844 S22: -0.0463 S23: -0.1229
REMARK 3 S31: -0.2477 S32: 0.0764 S33: -0.0308
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 4I19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-12.
REMARK 100 THE RCSB ID CODE IS RCSB076177.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26537
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.148
REMARK 200 RESOLUTION RANGE LOW (A) : 33.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 0.60400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/ARP/WARP/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM MALONATE, 0.1M BIS-TRIS
REMARK 280 PROPANE:NAOH, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 80.63150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.00550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.00550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.31575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.00550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.00550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 120.94725
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.00550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.00550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.31575
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.00550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.00550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 120.94725
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 80.63150
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 300 REMARK: EXPERIMENTALLY UNKNONW. THE CHAIN A MAY FORM A DIMER WITH
REMARK 300 IT SYMMETRY-RELATED MOLECULE THORUGH THE OPERATOR (-Y,-X,-Z+1/2).
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 80.63150
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 523 LIES ON A SPECIAL POSITION.
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 SER A -2
REMARK 465 ASN A -1
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 LYS A 143 NZ
REMARK 470 LYS A 158 NZ
REMARK 470 GLU A 211 CG CD OE1 OE2
REMARK 470 GLU A 271 CD OE1 OE2
REMARK 470 LYS A 307 NZ
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 ALA A 145 -155.36 -97.14
REMARK 500 ASP A 174 -125.49 61.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC109144 RELATED DB: TARGETTRACK
DBREF 4I19 A 1 385 UNP Q84HB8 Q84HB8_STRCZ 1 385
SEQADV 4I19 SER A -2 UNP Q84HB8 EXPRESSION TAG
SEQADV 4I19 ASN A -1 UNP Q84HB8 EXPRESSION TAG
SEQADV 4I19 ALA A 0 UNP Q84HB8 EXPRESSION TAG
SEQRES 1 A 388 SER ASN ALA MSE ARG PRO PHE GLN VAL GLN ILE PRO GLN
SEQRES 2 A 388 ALA ASP ILE ASP ASP LEU LYS ARG ARG LEU SER GLU THR
SEQRES 3 A 388 ARG TRP PRO GLU LEU VAL ASP VAL GLY TRP SER ARG GLY
SEQRES 4 A 388 ALA PRO LEU SER TYR ILE LYS GLU LEU ALA GLU TYR TRP
SEQRES 5 A 388 ARG ASP GLY PHE ASP TRP ARG ALA ALA GLU ARG ARG ILE
SEQRES 6 A 388 ASN GLN TYR PRO GLN PHE THR THR GLU ILE ASP GLY ALA
SEQRES 7 A 388 THR ILE HIS PHE LEU HIS VAL ARG SER PRO GLU PRO ASP
SEQRES 8 A 388 ALA THR PRO MSE VAL ILE THR HIS GLY TRP PRO GLY THR
SEQRES 9 A 388 PRO VAL GLU PHE LEU ASP ILE ILE GLY PRO LEU THR ASP
SEQRES 10 A 388 PRO ARG ALA HIS GLY GLY ASP PRO ALA ASP ALA PHE HIS
SEQRES 11 A 388 LEU VAL ILE PRO SER LEU PRO GLY PHE GLY LEU SER GLY
SEQRES 12 A 388 PRO LEU LYS SER ALA GLY TRP GLU LEU GLY ARG ILE ALA
SEQRES 13 A 388 MSE ALA TRP SER LYS LEU MSE ALA SER LEU GLY TYR GLU
SEQRES 14 A 388 ARG TYR ILE ALA GLN GLY GLY ASP ILE GLY ALA PHE THR
SEQRES 15 A 388 SER LEU LEU LEU GLY ALA ILE ASP PRO SER HIS LEU ALA
SEQRES 16 A 388 GLY ILE HIS VAL ASN LEU LEU GLN THR ASN LEU SER GLY
SEQRES 17 A 388 GLU PRO GLY GLU LEU GLU THR LEU SER ASP ALA ASP LYS
SEQRES 18 A 388 ALA ARG LEU ALA VAL SER GLU ARG PHE LEU ASP ASP LEU
SEQRES 19 A 388 SER GLY PRO MSE LYS MSE GLN SER THR ARG PRO HIS THR
SEQRES 20 A 388 ILE GLY TYR MSE LEU ASN ASP SER PRO VAL ALA GLN LEU
SEQRES 21 A 388 ALA TYR LEU LEU GLU MSE PHE LYS HIS TRP ALA GLN THR
SEQRES 22 A 388 GLU ASN VAL PRO GLU ASP ALA VAL ASP ARG ASP LEU MSE
SEQRES 23 A 388 LEU THR HIS ILE SER LEU PHE TRP PHE THR ALA THR GLY
SEQRES 24 A 388 GLY SER ALA ALA GLN ALA HIS TYR GLU LEU LYS PRO PHE
SEQRES 25 A 388 LEU PRO ILE THR SER LEU ILE GLY ARG SER PRO THR LEU
SEQRES 26 A 388 ASP VAL PRO MSE GLY VAL ALA VAL TYR PRO GLY ALA LEU
SEQRES 27 A 388 PHE GLN PRO VAL ARG SER LEU ALA GLU ARG ASP PHE LYS
SEQRES 28 A 388 GLN ILE VAL HIS TRP ALA GLU LEU ASP ARG GLY GLY HIS
SEQRES 29 A 388 PHE SER ALA MSE GLU GLU PRO ASP LEU PHE VAL ASP ASP
SEQRES 30 A 388 LEU ARG THR PHE ASN ARG THR LEU LYS LYS LEU
MODRES 4I19 MSE A 1 MET SELENOMETHIONINE
MODRES 4I19 MSE A 92 MET SELENOMETHIONINE
MODRES 4I19 MSE A 154 MET SELENOMETHIONINE
MODRES 4I19 MSE A 160 MET SELENOMETHIONINE
MODRES 4I19 MSE A 235 MET SELENOMETHIONINE
MODRES 4I19 MSE A 237 MET SELENOMETHIONINE
MODRES 4I19 MSE A 248 MET SELENOMETHIONINE
MODRES 4I19 MSE A 263 MET SELENOMETHIONINE
MODRES 4I19 MSE A 283 MET SELENOMETHIONINE
MODRES 4I19 MSE A 326 MET SELENOMETHIONINE
MODRES 4I19 MSE A 365 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 92 8
HET MSE A 154 8
HET MSE A 160 8
HET MSE A 235 8
HET MSE A 237 8
HET MSE A 248 8
HET MSE A 263 8
HET MSE A 283 8
HET MSE A 326 8
HET MSE A 365 8
HET ACT A 401 4
HET ACT A 402 4
HET FMT A 403 3
HET FMT A 404 3
HET FMT A 405 3
HET FMT A 406 3
HET FMT A 407 3
HET FMT A 408 3
HET FMT A 409 3
HET FMT A 410 3
HET FMT A 411 3
HET FMT A 412 3
HETNAM MSE SELENOMETHIONINE
HETNAM ACT ACETATE ION
HETNAM FMT FORMIC ACID
FORMUL 1 MSE 11(C5 H11 N O2 SE)
FORMUL 2 ACT 2(C2 H3 O2 1-)
FORMUL 4 FMT 10(C H2 O2)
FORMUL 14 HOH *191(H2 O)
HELIX 1 1 PRO A 9 GLU A 22 1 14
HELIX 2 2 PRO A 38 GLY A 52 1 15
HELIX 3 3 ASP A 54 GLN A 64 1 11
HELIX 4 4 THR A 101 GLU A 104 5 4
HELIX 5 5 PHE A 105 ASP A 114 1 10
HELIX 6 6 PRO A 115 GLY A 119 5 5
HELIX 7 7 ASP A 121 ASP A 124 5 4
HELIX 8 8 PHE A 136 GLY A 140 5 5
HELIX 9 9 GLU A 148 LEU A 163 1 16
HELIX 10 10 ASP A 174 ASP A 187 1 14
HELIX 11 11 GLU A 206 LEU A 213 5 8
HELIX 12 12 SER A 214 VAL A 223 1 10
HELIX 13 13 VAL A 223 LEU A 231 1 9
HELIX 14 14 SER A 232 SER A 239 1 8
HELIX 15 15 ARG A 241 ASP A 251 1 11
HELIX 16 16 SER A 252 TRP A 267 1 16
HELIX 17 17 VAL A 273 ALA A 277 5 5
HELIX 18 18 ASP A 279 ALA A 294 1 16
HELIX 19 19 THR A 295 LEU A 306 1 12
HELIX 20 20 LYS A 307 LEU A 310 5 4
HELIX 21 21 VAL A 339 PHE A 347 1 9
HELIX 22 22 PHE A 362 GLU A 367 1 6
HELIX 23 23 GLU A 367 LEU A 385 1 19
SHEET 1 A 9 ARG A 2 PHE A 4 0
SHEET 2 A 9 GLN A 67 ILE A 72 -1 O THR A 69 N ARG A 2
SHEET 3 A 9 ALA A 75 VAL A 82 -1 O ILE A 77 N THR A 70
SHEET 4 A 9 PHE A 126 PRO A 131 -1 O LEU A 128 N VAL A 82
SHEET 5 A 9 THR A 90 THR A 95 1 N MSE A 92 O VAL A 129
SHEET 6 A 9 TYR A 168 GLY A 172 1 O GLN A 171 N VAL A 93
SHEET 7 A 9 LEU A 191 VAL A 196 1 O ALA A 192 N TYR A 168
SHEET 8 A 9 MSE A 326 VAL A 330 1 O GLY A 327 N ILE A 194
SHEET 9 A 9 ILE A 350 GLU A 355 1 O ALA A 354 N VAL A 328
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N ARG A 2 1555 1555 1.33
LINK C PRO A 91 N MSE A 92 1555 1555 1.33
LINK C MSE A 92 N VAL A 93 1555 1555 1.32
LINK C ALA A 153 N MSE A 154 1555 1555 1.33
LINK C MSE A 154 N ALA A 155 1555 1555 1.33
LINK C LEU A 159 N MSE A 160 1555 1555 1.33
LINK C MSE A 160 N ALA A 161 1555 1555 1.33
LINK C PRO A 234 N MSE A 235 1555 1555 1.33
LINK C MSE A 235 N LYS A 236 1555 1555 1.33
LINK C LYS A 236 N MSE A 237 1555 1555 1.33
LINK C MSE A 237 N GLN A 238 1555 1555 1.33
LINK C TYR A 247 N MSE A 248 1555 1555 1.33
LINK C MSE A 248 N LEU A 249 1555 1555 1.33
LINK C GLU A 262 N MSE A 263 1555 1555 1.32
LINK C MSE A 263 N PHE A 264 1555 1555 1.34
LINK C LEU A 282 N MSE A 283 1555 1555 1.33
LINK C MSE A 283 N LEU A 284 1555 1555 1.33
LINK C PRO A 325 N MSE A 326 1555 1555 1.33
LINK C MSE A 326 N GLY A 327 1555 1555 1.33
LINK C ALA A 364 N MSE A 365 1555 1555 1.33
LINK C MSE A 365 N GLU A 366 1555 1555 1.33
CISPEP 1 TRP A 98 PRO A 99 0 -2.23
SITE 1 AC1 6 ASP A 174 ILE A 175 PHE A 178 MSE A 235
SITE 2 AC1 6 HIS A 303 PRO A 311
SITE 1 AC2 6 ALA A 177 PHE A 178 LEU A 198 GLN A 200
SITE 2 AC2 6 FMT A 405 HOH A 667
SITE 1 AC3 2 PRO A 85 ASP A 114
SITE 1 AC4 3 SER A 319 FMT A 405 HOH A 600
SITE 1 AC5 5 GLN A 200 SER A 319 ACT A 402 FMT A 404
SITE 2 AC5 5 FMT A 406
SITE 1 AC6 5 ASN A 202 ARG A 345 ASP A 346 FMT A 405
SITE 2 AC6 5 HOH A 590
SITE 1 AC7 4 ASP A 174 MSE A 235 HIS A 361 HOH A 620
SITE 1 AC8 4 ARG A 60 SER A 214 ASP A 215 HOH A 618
SITE 1 AC9 3 ASP A 276 ALA A 277 FMT A 410
SITE 1 BC1 7 ASP A 276 ALA A 277 GLU A 366 GLU A 367
SITE 2 BC1 7 FMT A 409 HOH A 506 HOH A 572
SITE 1 BC2 3 LYS A 17 TRP A 49 ARG A 50
SITE 1 BC3 2 PRO A 311 THR A 313
CRYST1 76.011 76.011 161.263 90.00 90.00 90.00 P 41 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 0.013156 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013156 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006201 0.00000
TER 3031 LEU A 385
MASTER 412 0 23 23 9 0 17 6 3256 1 148 30
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