| 5h3b-pdb | HEADER HYDROLASE 21-OCT-16 5H3B
TITLE CRYSTAL STRUCTURE OF SEMET-BIOG FROM HAEMOPHILUS INFLUENZAE AT 1.49
TITLE 2 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN HI_1552;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE RD KW20;
SOURCE 3 ORGANISM_TAXID: 71421;
SOURCE 4 STRAIN: KW20;
SOURCE 5 GENE: HI_1552;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA/BETA-HYDROLASE FOLD, PIMELOYL-ACP METHYL ESTERASE, BIOTIN
KEYWDS 2 BIOSYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SHI,Z.GUO
REVDAT 1 07-DEC-16 5H3B 0
JRNL AUTH J.SHI,X.CAO,Y.CHEN,J.E.CRONAN,Z.GUO
JRNL TITL AN ATYPICAL ALPHA/BETA HYDROLASE FOLD REVEALED IN THE
JRNL TITL 2 CRYSTAL STRUCTURE OF PIMELOYL-ACYL CARRIER PROTEIN METHYL
JRNL TITL 3 ESTERASE BIOG FROM HAEMOPHILUS INFLUENZAE
JRNL REF BIOCHEMISTRY 2016
JRNL REFN ISSN 0006-2960
JRNL DOI 10.1021/ACS.BIOCHEM.6B00818
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 68819
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.840
REMARK 3 FREE R VALUE TEST SET COUNT : 1954
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 32.4577 - 3.5945 1.00 4995 144 0.1439 0.1606
REMARK 3 2 3.5945 - 2.8536 1.00 4936 144 0.1485 0.1794
REMARK 3 3 2.8536 - 2.4930 1.00 4892 152 0.1544 0.1588
REMARK 3 4 2.4930 - 2.2652 1.00 4929 133 0.1366 0.1927
REMARK 3 5 2.2652 - 2.1028 1.00 4861 141 0.1277 0.1569
REMARK 3 6 2.1028 - 1.9789 0.99 4909 145 0.1280 0.1763
REMARK 3 7 1.9789 - 1.8798 0.99 4807 146 0.1256 0.1713
REMARK 3 8 1.8798 - 1.7980 0.98 4782 138 0.1394 0.1974
REMARK 3 9 1.7980 - 1.7288 0.98 4795 151 0.1455 0.2058
REMARK 3 10 1.7288 - 1.6691 0.97 4767 124 0.1569 0.1955
REMARK 3 11 1.6691 - 1.6169 0.96 4675 151 0.1671 0.2292
REMARK 3 12 1.6169 - 1.5707 0.96 4665 134 0.1778 0.2690
REMARK 3 13 1.5707 - 1.5293 0.94 4607 129 0.2054 0.2594
REMARK 3 14 1.5293 - 1.4920 0.87 4245 122 0.2297 0.3163
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.32
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 3636
REMARK 3 ANGLE : 1.126 4954
REMARK 3 CHIRALITY : 0.044 523
REMARK 3 PLANARITY : 0.005 630
REMARK 3 DIHEDRAL : 13.427 1277
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5H3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1300001937.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, HKL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70407
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 32.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
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: SAD
REMARK 200 SOFTWARE USED: PHENIX 1.8.4_1496
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10%(V/V) ISO-PROPANOL, 0.1M CITRIC
REMARK 280 ACID/SODIUM CITRATE PH 5.6, 22% PEG 4000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 289K
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 34.73550
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 TOTAL BURIED SURFACE AREA: 240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 HIS A 215
REMARK 465 LEU A 216
REMARK 465 GLU A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 HIS A 223
REMARK 465 HIS B 215
REMARK 465 LEU B 216
REMARK 465 GLU B 217
REMARK 465 HIS B 218
REMARK 465 HIS B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
REMARK 465 HIS B 223
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 GLU A 34 CG CD OE1 OE2
REMARK 470 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 146 OE1
REMARK 470 GLU A 195 CD OE1 OE2
REMARK 470 ASP A 214 OD1 OD2
REMARK 470 LYS B 2 NZ
REMARK 470 LYS B 4 CE NZ
REMARK 470 TYR B 8 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 9 OE1 NE2
REMARK 470 ASN B 28 OD1
REMARK 470 GLU B 34 CB CG CD OE1 OE2
REMARK 470 ASN B 48 CG OD1 ND2
REMARK 470 ASP B 50 CG OD1 OD2
REMARK 470 ARG B 57 CG CD
REMARK 470 ILE B 78 CD1
REMARK 470 ARG B 79 CD NE CZ NH1 NH2
REMARK 470 GLU B 113 CG CD OE1 OE2
REMARK 470 ASN B 114 CG OD1 ND2
REMARK 470 ARG B 116 CG CD
REMARK 470 LYS B 118 CG CD CE NZ
REMARK 470 LYS B 127 CG CD CE NZ
REMARK 470 ASP B 142 CB CG OD1 OD2
REMARK 470 GLN B 146 CD OE1 NE2
REMARK 470 GLU B 197 OE1 OE2
REMARK 470 ASP B 214 O OD1 OD2
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 HOH A 441 O HOH A 621 1.48
REMARK 500 O HOH A 453 O HOH A 626 1.55
REMARK 500 O HOH B 326 O HOH B 409 1.59
REMARK 500 O HOH A 415 O HOH A 647 1.68
REMARK 500 O HOH A 693 O HOH A 725 1.75
REMARK 500 O HOH B 339 O HOH B 417 1.76
REMARK 500 O HOH A 676 O HOH A 732 1.82
REMARK 500 O HOH A 567 O HOH A 654 1.83
REMARK 500 O HOH A 659 O HOH A 728 1.99
REMARK 500 O HOH A 626 O HOH A 665 2.00
REMARK 500 O HOH A 403 O HOH A 625 2.01
REMARK 500 O HOH A 641 O HOH A 647 2.01
REMARK 500 O HOH A 559 O HOH A 651 2.02
REMARK 500 O HOH A 425 O HOH A 508 2.03
REMARK 500 O HOH A 402 O HOH A 645 2.03
REMARK 500 O HOH B 362 O HOH B 419 2.04
REMARK 500 O HOH A 561 O HOH A 661 2.09
REMARK 500 O HOH A 555 O HOH A 684 2.10
REMARK 500 O HOH A 662 O HOH A 668 2.11
REMARK 500 O HOH A 473 O HOH A 619 2.11
REMARK 500 O HOH B 412 O HOH B 432 2.14
REMARK 500 O HOH A 462 O HOH A 699 2.14
REMARK 500 O HOH A 695 O HOH B 417 2.16
REMARK 500 O HOH A 653 O HOH A 693 2.18
REMARK 500 O HOH A 540 O HOH A 600 2.19
REMARK 500 O HOH A 441 O HOH A 549 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 455 O HOH A 615 1655 1.71
REMARK 500 O HOH A 447 O HOH A 504 2546 1.75
REMARK 500 O HOH A 621 O HOH A 651 1655 1.93
REMARK 500 O HOH A 559 O HOH A 621 1455 1.94
REMARK 500 O HOH A 441 O HOH A 651 1655 2.11
REMARK 500 O HOH A 723 O HOH A 730 1655 2.13
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 ARG A 57 -77.12 -80.43
REMARK 500 SER A 65 -128.34 63.53
REMARK 500 SER B 65 -129.76 63.80
REMARK 500 ILE B 177 -65.18 -104.32
REMARK 500 LEU B 189 -2.40 70.98
REMARK 500 ARG B 190 -80.14 -100.65
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 302
DBREF 5H3B A 1 215 UNP P44251 Y1552_HAEIN 1 215
DBREF 5H3B B 1 215 UNP P44251 Y1552_HAEIN 1 215
SEQADV 5H3B LEU A 216 UNP P44251 EXPRESSION TAG
SEQADV 5H3B GLU A 217 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS A 218 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS A 219 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS A 220 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS A 221 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS A 222 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS A 223 UNP P44251 EXPRESSION TAG
SEQADV 5H3B LEU B 216 UNP P44251 EXPRESSION TAG
SEQADV 5H3B GLU B 217 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS B 218 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS B 219 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS B 220 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS B 221 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS B 222 UNP P44251 EXPRESSION TAG
SEQADV 5H3B HIS B 223 UNP P44251 EXPRESSION TAG
SEQRES 1 A 223 MSE LYS THR LYS PHE TYR ASP TYR GLN GLY GLU HIS LEU
SEQRES 2 A 223 ILE LEU TYR PHE ALA GLY TRP GLY THR PRO PRO ASP ALA
SEQRES 3 A 223 VAL ASN HIS LEU ILE LEU PRO GLU ASN HIS ASP LEU LEU
SEQRES 4 A 223 ILE CYS TYR ASP TYR GLN ASP LEU ASN LEU ASP PHE ASP
SEQRES 5 A 223 LEU SER ALA TYR ARG HIS ILE ARG LEU VAL ALA TRP SER
SEQRES 6 A 223 MSE GLY VAL TRP VAL ALA GLU ARG VAL LEU GLN GLY ILE
SEQRES 7 A 223 ARG LEU LYS SER ALA THR ALA VAL ASN GLY THR GLY LEU
SEQRES 8 A 223 PRO CYS ASP ASP SER PHE GLY ILE PRO TYR ALA ILE PHE
SEQRES 9 A 223 LYS GLY THR LEU GLU ASN LEU THR GLU ASN THR ARG LEU
SEQRES 10 A 223 LYS PHE GLU ARG ARG ILE CYS GLY ASP LYS ALA SER PHE
SEQRES 11 A 223 GLU ARG TYR GLN LEU PHE PRO ALA ARG PRO PHE ASP GLU
SEQRES 12 A 223 ILE HIS GLN GLU LEU THR ALA LEU PHE ALA MSE ILE GLN
SEQRES 13 A 223 GLN ASP LYS ARG ILE ASP LEU ILE HIS TRP ALA ASN ALA
SEQRES 14 A 223 TRP VAL SER SER ARG ASP LYS ILE PHE THR PRO ALA ASN
SEQRES 15 A 223 GLN HIS GLN TYR TRP ALA LEU ARG CYS ALA VAL GLN GLU
SEQRES 16 A 223 ILE GLU GLY GLU HIS TYR VAL PHE SER ARG PHE THR HIS
SEQRES 17 A 223 TRP SER ALA LEU TRP ASP HIS LEU GLU HIS HIS HIS HIS
SEQRES 18 A 223 HIS HIS
SEQRES 1 B 223 MSE LYS THR LYS PHE TYR ASP TYR GLN GLY GLU HIS LEU
SEQRES 2 B 223 ILE LEU TYR PHE ALA GLY TRP GLY THR PRO PRO ASP ALA
SEQRES 3 B 223 VAL ASN HIS LEU ILE LEU PRO GLU ASN HIS ASP LEU LEU
SEQRES 4 B 223 ILE CYS TYR ASP TYR GLN ASP LEU ASN LEU ASP PHE ASP
SEQRES 5 B 223 LEU SER ALA TYR ARG HIS ILE ARG LEU VAL ALA TRP SER
SEQRES 6 B 223 MSE GLY VAL TRP VAL ALA GLU ARG VAL LEU GLN GLY ILE
SEQRES 7 B 223 ARG LEU LYS SER ALA THR ALA VAL ASN GLY THR GLY LEU
SEQRES 8 B 223 PRO CYS ASP ASP SER PHE GLY ILE PRO TYR ALA ILE PHE
SEQRES 9 B 223 LYS GLY THR LEU GLU ASN LEU THR GLU ASN THR ARG LEU
SEQRES 10 B 223 LYS PHE GLU ARG ARG ILE CYS GLY ASP LYS ALA SER PHE
SEQRES 11 B 223 GLU ARG TYR GLN LEU PHE PRO ALA ARG PRO PHE ASP GLU
SEQRES 12 B 223 ILE HIS GLN GLU LEU THR ALA LEU PHE ALA MSE ILE GLN
SEQRES 13 B 223 GLN ASP LYS ARG ILE ASP LEU ILE HIS TRP ALA ASN ALA
SEQRES 14 B 223 TRP VAL SER SER ARG ASP LYS ILE PHE THR PRO ALA ASN
SEQRES 15 B 223 GLN HIS GLN TYR TRP ALA LEU ARG CYS ALA VAL GLN GLU
SEQRES 16 B 223 ILE GLU GLY GLU HIS TYR VAL PHE SER ARG PHE THR HIS
SEQRES 17 B 223 TRP SER ALA LEU TRP ASP HIS LEU GLU HIS HIS HIS HIS
SEQRES 18 B 223 HIS HIS
MODRES 5H3B MSE A 1 MET MODIFIED RESIDUE
MODRES 5H3B MSE A 66 MET MODIFIED RESIDUE
MODRES 5H3B MSE A 154 MET MODIFIED RESIDUE
MODRES 5H3B MSE B 1 MET MODIFIED RESIDUE
MODRES 5H3B MSE B 66 MET MODIFIED RESIDUE
MODRES 5H3B MSE B 154 MET MODIFIED RESIDUE
HET MSE A 1 8
HET MSE A 66 8
HET MSE A 154 13
HET MSE B 1 13
HET MSE B 66 13
HET MSE B 154 13
HET GOL A 301 6
HET IPA A 302 4
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN IPA 2-PROPANOL
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 GOL C3 H8 O3
FORMUL 4 IPA C3 H8 O
FORMUL 5 HOH *470(H2 O)
HELIX 1 AA1 PRO A 23 ASN A 28 5 6
HELIX 2 AA2 MSE A 66 LEU A 75 1 10
HELIX 3 AA3 PRO A 100 ASN A 110 1 11
HELIX 4 AA4 THR A 112 GLY A 125 1 14
HELIX 5 AA5 ASP A 126 GLN A 134 1 9
HELIX 6 AA6 PRO A 140 ASP A 158 1 19
HELIX 7 AA7 THR A 179 ALA A 188 1 10
HELIX 8 AA8 VAL A 202 PHE A 206 5 5
HELIX 9 AA9 HIS A 208 TRP A 213 5 6
HELIX 10 AB1 PRO B 23 ASN B 28 5 6
HELIX 11 AB2 ASP B 52 TYR B 56 5 5
HELIX 12 AB3 MSE B 66 LEU B 75 1 10
HELIX 13 AB4 PRO B 100 ASN B 110 1 11
HELIX 14 AB5 THR B 112 GLY B 125 1 14
HELIX 15 AB6 ASP B 126 GLN B 134 1 9
HELIX 16 AB7 PRO B 140 ASP B 158 1 19
HELIX 17 AB8 THR B 179 ALA B 188 1 10
HELIX 18 AB9 VAL B 202 PHE B 206 5 5
HELIX 19 AC1 HIS B 208 ASP B 214 1 7
SHEET 1 AA1 7 LYS A 2 TYR A 6 0
SHEET 2 AA1 7 HIS A 36 TYR A 42 -1 O LEU A 38 N TYR A 6
SHEET 3 AA1 7 HIS A 12 PHE A 17 1 N TYR A 16 O CYS A 41
SHEET 4 AA1 7 ILE A 59 TRP A 64 1 O ARG A 60 N LEU A 15
SHEET 5 AA1 7 SER A 82 VAL A 86 1 O VAL A 86 N ALA A 63
SHEET 6 AA1 7 ASN A 168 SER A 172 1 O TRP A 170 N ALA A 85
SHEET 7 AA1 7 ALA A 192 ILE A 196 1 O GLN A 194 N ALA A 169
SHEET 1 AA2 7 LYS B 2 TYR B 6 0
SHEET 2 AA2 7 HIS B 36 TYR B 42 -1 O LEU B 38 N TYR B 6
SHEET 3 AA2 7 HIS B 12 PHE B 17 1 N TYR B 16 O CYS B 41
SHEET 4 AA2 7 ILE B 59 TRP B 64 1 O ARG B 60 N LEU B 15
SHEET 5 AA2 7 SER B 82 VAL B 86 1 O SER B 82 N LEU B 61
SHEET 6 AA2 7 ASN B 168 SER B 172 1 O TRP B 170 N ALA B 85
SHEET 7 AA2 7 ALA B 192 ILE B 196 1 O GLN B 194 N ALA B 169
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C SER A 65 N MSE A 66 1555 1555 1.31
LINK C MSE A 66 N GLY A 67 1555 1555 1.31
LINK C ALA A 153 N MSE A 154 1555 1555 1.33
LINK C MSE A 154 N ILE A 155 1555 1555 1.34
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C SER B 65 N MSE B 66 1555 1555 1.33
LINK C MSE B 66 N GLY B 67 1555 1555 1.33
LINK C ALA B 153 N MSE B 154 1555 1555 1.33
LINK C MSE B 154 N ILE B 155 1555 1555 1.33
SITE 1 AC1 8 TYR A 6 TYR A 8 ASN A 28 LEU A 30
SITE 2 AC1 8 LEU A 32 HOH A 425 HOH A 442 HOH A 514
SITE 1 AC2 4 GLY A 19 TRP A 20 THR A 22 SER A 65
CRYST1 44.154 69.471 72.034 90.00 93.15 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 0.022648 0.000000 0.001247 0.00000
SCALE2 0.000000 0.014394 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013903 0.00000
TER 1786 ASP A 214
TER 3517 ASP B 214
MASTER 357 0 8 19 14 0 3 6 3954 2 88 36
END
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