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HEADER LYASE 27-SEP-13 4MYD
TITLE 1.37 ANGSTROM CRYSTAL STRUCTURE OF E. COLI 2-SUCCINYL-6-HYDROXY-2,4-
TITLE 2 CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE (MENH) IN COMPLEX WITH SHCHC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE
COMPND 3 SYNTHASE;
COMPND 4 CHAIN: A, B, C;
COMPND 5 SYNONYM: SHCHC SYNTHASE;
COMPND 6 EC: 4.2.99.20;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B2263, JW2258, MENH, YFBB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM
KEYWDS ALPHA/BETA HYDROLASE FOLD, 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-
KEYWDS 2 CARBOXYLATE SYNTHASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SUN,S.YIN,Y.FENG,J.LI,J.ZHOU,C.LIU,G.ZHU,Z.GUO
REVDAT 1 23-APR-14 4MYD 0
JRNL AUTH Y.SUN,S.YIN,Y.FENG,J.LI,J.ZHOU,C.LIU,G.ZHU,Z.GUO
JRNL TITL MOLECULAR BASIS OF THE GENERAL BASE CATALYSIS OF AN
JRNL TITL 2 ALPHA/BETA HYDROLASE CATALYTIC TRIAD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 161886
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.130
REMARK 3 R VALUE (WORKING SET) : 0.128
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 8106
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 42.8406 - 4.2680 0.98 5020 291 0.1623 0.1812
REMARK 3 2 4.2680 - 3.3881 1.00 5125 277 0.1141 0.1520
REMARK 3 3 3.3881 - 2.9599 1.00 5077 301 0.1332 0.1694
REMARK 3 4 2.9599 - 2.6893 1.00 5149 274 0.1292 0.1506
REMARK 3 5 2.6893 - 2.4966 1.00 5110 295 0.1249 0.1815
REMARK 3 6 2.4966 - 2.3494 1.00 5083 264 0.1152 0.1447
REMARK 3 7 2.3494 - 2.2318 1.00 5150 269 0.1098 0.1470
REMARK 3 8 2.2318 - 2.1346 1.00 5138 245 0.1156 0.1498
REMARK 3 9 2.1346 - 2.0524 1.00 5209 243 0.1105 0.1425
REMARK 3 10 2.0524 - 1.9816 1.00 5081 287 0.1145 0.1527
REMARK 3 11 1.9816 - 1.9197 1.00 5129 260 0.1132 0.1480
REMARK 3 12 1.9197 - 1.8648 1.00 5126 270 0.1089 0.1522
REMARK 3 13 1.8648 - 1.8157 1.00 5153 285 0.1106 0.1654
REMARK 3 14 1.8157 - 1.7714 1.00 5059 307 0.1105 0.1549
REMARK 3 15 1.7714 - 1.7311 1.00 5146 286 0.1063 0.1481
REMARK 3 16 1.7311 - 1.6943 1.00 5139 270 0.1095 0.1608
REMARK 3 17 1.6943 - 1.6604 1.00 5140 262 0.1086 0.1562
REMARK 3 18 1.6604 - 1.6291 1.00 5126 273 0.1146 0.1629
REMARK 3 19 1.6291 - 1.6000 1.00 5089 289 0.1195 0.1792
REMARK 3 20 1.6000 - 1.5728 1.00 5139 275 0.1172 0.1500
REMARK 3 21 1.5728 - 1.5475 1.00 5157 283 0.1265 0.1825
REMARK 3 22 1.5475 - 1.5237 1.00 5148 246 0.1365 0.1973
REMARK 3 23 1.5237 - 1.5012 1.00 5062 270 0.1389 0.1792
REMARK 3 24 1.5012 - 1.4801 1.00 5194 267 0.1414 0.2054
REMARK 3 25 1.4801 - 1.4601 1.00 5149 255 0.1552 0.1941
REMARK 3 26 1.4601 - 1.4411 1.00 5156 257 0.1677 0.2113
REMARK 3 27 1.4411 - 1.4231 1.00 5069 273 0.1786 0.2265
REMARK 3 28 1.4231 - 1.4060 1.00 5259 237 0.1984 0.2685
REMARK 3 29 1.4060 - 1.3896 1.00 5102 242 0.2123 0.2405
REMARK 3 30 1.3896 - 1.3740 0.99 5096 253 0.2350 0.2904
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.86
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 : 0.009 7966
REMARK 3 ANGLE : 1.191 10827
REMARK 3 CHIRALITY : 0.052 1167
REMARK 3 PLANARITY : 0.006 1444
REMARK 3 DIHEDRAL : 14.526 2810
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 4MYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB082520.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
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) : 0.97
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 161905
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 46.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.77600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M NA/K PHOSPHATE PH 6.9, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 15.61667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.23333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
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: C
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 MET C 1
REMARK 465 ALA C 221
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 ARG A 129 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 PHE A 252 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 198 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 119 CG CD OE1 OE2
REMARK 470 GLU C 123 CG CD OE1 OE2
REMARK 470 ARG C 126 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 149 CG CD OE1 NE2
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 H SER C 196 O HOH C 307 1.47
REMARK 500 HH22 ARG C 192 O HOH C 312 1.53
REMARK 500 HH11 ARG B 209 O HOH B 685 1.57
REMARK 500 HZ1 LYS A 11 O ARG C 251 1.58
REMARK 500 O LEU C 115 O HOH C 338 1.87
REMARK 500 O ARG C 192 O HOH C 307 1.93
REMARK 500 OD1 ASP B 158 O HOH B 711 1.95
REMARK 500 OG SER A 169 O HOH A 606 2.03
REMARK 500 O HOH B 590 O HOH B 618 2.03
REMARK 500 OD1 ASP A 158 O HOH A 599 2.05
REMARK 500 OE1 GLN B 133 O HOH B 609 2.05
REMARK 500 OE1 GLU C 208 O HOH C 354 2.08
REMARK 500 O HOH B 546 O HOH B 689 2.09
REMARK 500 O HOH B 604 O HOH B 621 2.10
REMARK 500 O HOH A 541 O HOH A 593 2.10
REMARK 500 O GLY C 114 O HOH C 312 2.10
REMARK 500 OD2 ASP B 66 O HOH B 657 2.11
REMARK 500 OG SER C 196 O HOH C 319 2.11
REMARK 500 O HOH A 536 O HOH A 619 2.12
REMARK 500 O HOH B 626 O HOH B 644 2.15
REMARK 500 O HOH A 543 O HOH A 737 2.17
REMARK 500 O HOH A 603 O HOH A 655 2.17
REMARK 500 OE1 GLN B 130 O HOH B 578 2.17
REMARK 500 O HOH B 638 O HOH B 661 2.18
REMARK 500 O HOH A 592 O HOH A 647 2.18
REMARK 500 O HOH A 528 O HOH A 744 2.19
REMARK 500 OD2 ASP A 79 O HOH A 464 2.19
REMARK 500 O HOH A 726 O HOH A 735 2.19
REMARK 500 O HOH B 603 O HOH B 697 2.19
REMARK 500 O HOH B 704 O HOH B 705 2.19
REMARK 500 O HOH A 508 O HOH A 689 2.19
REMARK 500 O HOH B 501 O HOH B 680 2.19
REMARK 500 O HOH B 543 O HOH B 566 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 104 CB CYS A 104 SG -0.125
REMARK 500 CYS B 104 CB CYS B 104 SG -0.099
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 124 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 124 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG B 124 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 124 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
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 SER A 24 -0.52 76.07
REMARK 500 PHE A 37 56.37 -98.90
REMARK 500 SER A 86 -119.20 58.66
REMARK 500 ALA A 221 42.74 -89.45
REMARK 500 SER B 24 -1.37 76.79
REMARK 500 PHE B 37 55.96 -98.99
REMARK 500 SER B 86 -119.57 59.19
REMARK 500 SER C 24 -2.01 79.52
REMARK 500 SER C 86 -120.15 60.66
REMARK 500 LEU C 115 172.36 -59.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 708 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH B 707 DISTANCE = 6.76 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 164 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 164 B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MXD RELATED DB: PDB
REMARK 900 RELATED ID: 4MYS RELATED DB: PDB
DBREF 4MYD A 1 252 UNP P37355 MENH_ECOLI 1 252
DBREF 4MYD B 1 252 UNP P37355 MENH_ECOLI 1 252
DBREF 4MYD C 1 252 UNP P37355 MENH_ECOLI 1 252
SEQRES 1 A 252 MET ILE LEU HIS ALA GLN ALA LYS HIS GLY LYS PRO GLY
SEQRES 2 A 252 LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE SER GLY ASP
SEQRES 3 A 252 CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA PHE ALA ASP
SEQRES 4 A 252 TYR SER ARG LEU TYR VAL ASP LEU PRO GLY HIS GLY GLY
SEQRES 5 A 252 SER ALA ALA ILE SER VAL ASP GLY PHE ASP ASP VAL THR
SEQRES 6 A 252 ASP LEU LEU ARG LYS THR LEU VAL SER TYR ASN ILE LEU
SEQRES 7 A 252 ASP PHE TRP LEU VAL GLY TYR SER LEU GLY GLY ARG VAL
SEQRES 8 A 252 ALA MET MET ALA ALA CYS GLN GLY LEU ALA GLY LEU CYS
SEQRES 9 A 252 GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY LEU GLN ASN
SEQRES 10 A 252 ALA GLU GLN ARG ALA GLU ARG GLN ARG SER ASP ARG GLN
SEQRES 11 A 252 TRP VAL GLN ARG PHE LEU THR GLU PRO LEU THR ALA VAL
SEQRES 12 A 252 PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE ALA SER LEU
SEQRES 13 A 252 ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA LEU ARG SER
SEQRES 14 A 252 ASN ASN ASN GLY ALA THR LEU ALA ALA MET LEU GLU ALA
SEQRES 15 A 252 THR SER LEU ALA VAL GLN PRO ASP LEU ARG ALA ASN LEU
SEQRES 16 A 252 SER ALA ARG THR PHE ALA PHE TYR TYR LEU CYS GLY GLU
SEQRES 17 A 252 ARG ASP SER LYS PHE ARG ALA LEU ALA ALA GLU LEU ALA
SEQRES 18 A 252 ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY HIS ASN ALA
SEQRES 19 A 252 HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA SER LEU ALA
SEQRES 20 A 252 GLN ILE LEU ARG PHE
SEQRES 1 B 252 MET ILE LEU HIS ALA GLN ALA LYS HIS GLY LYS PRO GLY
SEQRES 2 B 252 LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE SER GLY ASP
SEQRES 3 B 252 CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA PHE ALA ASP
SEQRES 4 B 252 TYR SER ARG LEU TYR VAL ASP LEU PRO GLY HIS GLY GLY
SEQRES 5 B 252 SER ALA ALA ILE SER VAL ASP GLY PHE ASP ASP VAL THR
SEQRES 6 B 252 ASP LEU LEU ARG LYS THR LEU VAL SER TYR ASN ILE LEU
SEQRES 7 B 252 ASP PHE TRP LEU VAL GLY TYR SER LEU GLY GLY ARG VAL
SEQRES 8 B 252 ALA MET MET ALA ALA CYS GLN GLY LEU ALA GLY LEU CYS
SEQRES 9 B 252 GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY LEU GLN ASN
SEQRES 10 B 252 ALA GLU GLN ARG ALA GLU ARG GLN ARG SER ASP ARG GLN
SEQRES 11 B 252 TRP VAL GLN ARG PHE LEU THR GLU PRO LEU THR ALA VAL
SEQRES 12 B 252 PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE ALA SER LEU
SEQRES 13 B 252 ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA LEU ARG SER
SEQRES 14 B 252 ASN ASN ASN GLY ALA THR LEU ALA ALA MET LEU GLU ALA
SEQRES 15 B 252 THR SER LEU ALA VAL GLN PRO ASP LEU ARG ALA ASN LEU
SEQRES 16 B 252 SER ALA ARG THR PHE ALA PHE TYR TYR LEU CYS GLY GLU
SEQRES 17 B 252 ARG ASP SER LYS PHE ARG ALA LEU ALA ALA GLU LEU ALA
SEQRES 18 B 252 ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY HIS ASN ALA
SEQRES 19 B 252 HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA SER LEU ALA
SEQRES 20 B 252 GLN ILE LEU ARG PHE
SEQRES 1 C 252 MET ILE LEU HIS ALA GLN ALA LYS HIS GLY LYS PRO GLY
SEQRES 2 C 252 LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE SER GLY ASP
SEQRES 3 C 252 CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA PHE ALA ASP
SEQRES 4 C 252 TYR SER ARG LEU TYR VAL ASP LEU PRO GLY HIS GLY GLY
SEQRES 5 C 252 SER ALA ALA ILE SER VAL ASP GLY PHE ASP ASP VAL THR
SEQRES 6 C 252 ASP LEU LEU ARG LYS THR LEU VAL SER TYR ASN ILE LEU
SEQRES 7 C 252 ASP PHE TRP LEU VAL GLY TYR SER LEU GLY GLY ARG VAL
SEQRES 8 C 252 ALA MET MET ALA ALA CYS GLN GLY LEU ALA GLY LEU CYS
SEQRES 9 C 252 GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY LEU GLN ASN
SEQRES 10 C 252 ALA GLU GLN ARG ALA GLU ARG GLN ARG SER ASP ARG GLN
SEQRES 11 C 252 TRP VAL GLN ARG PHE LEU THR GLU PRO LEU THR ALA VAL
SEQRES 12 C 252 PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE ALA SER LEU
SEQRES 13 C 252 ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA LEU ARG SER
SEQRES 14 C 252 ASN ASN ASN GLY ALA THR LEU ALA ALA MET LEU GLU ALA
SEQRES 15 C 252 THR SER LEU ALA VAL GLN PRO ASP LEU ARG ALA ASN LEU
SEQRES 16 C 252 SER ALA ARG THR PHE ALA PHE TYR TYR LEU CYS GLY GLU
SEQRES 17 C 252 ARG ASP SER LYS PHE ARG ALA LEU ALA ALA GLU LEU ALA
SEQRES 18 C 252 ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY HIS ASN ALA
SEQRES 19 C 252 HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA SER LEU ALA
SEQRES 20 C 252 GLN ILE LEU ARG PHE
HET 164 A 301 27
HET 164 B 301 27
HETNAM 164 2-(3-CARBOXYPROPIONYL)-6-HYDROXY-CYCLOHEXA-2,4-DIENE
HETNAM 2 164 CARBOXYLIC ACID
FORMUL 4 164 2(C11 H12 O6)
FORMUL 6 HOH *797(H2 O)
HELIX 1 1 TRP A 30 GLU A 35 1 6
HELIX 2 2 HIS A 50 ALA A 54 5 5
HELIX 3 3 GLY A 60 TYR A 75 1 16
HELIX 4 4 SER A 86 GLY A 99 1 14
HELIX 5 5 ASN A 117 GLU A 138 1 22
HELIX 6 6 PRO A 139 TYR A 148 1 10
HELIX 7 7 GLN A 149 ALA A 154 5 6
HELIX 8 8 ASN A 157 SER A 169 1 13
HELIX 9 9 ASN A 172 THR A 183 1 12
HELIX 10 10 SER A 184 GLN A 188 5 5
HELIX 11 11 LEU A 191 ALA A 197 1 7
HELIX 12 12 ASP A 210 GLU A 219 1 10
HELIX 13 13 ASN A 233 ASN A 238 1 6
HELIX 14 14 ASN A 238 ARG A 251 1 14
HELIX 15 15 TRP B 30 GLU B 35 1 6
HELIX 16 16 HIS B 50 ALA B 54 5 5
HELIX 17 17 GLY B 60 TYR B 75 1 16
HELIX 18 18 SER B 86 GLY B 99 1 14
HELIX 19 19 ASN B 117 GLU B 138 1 22
HELIX 20 20 PRO B 139 TYR B 148 1 10
HELIX 21 21 GLN B 149 ALA B 154 5 6
HELIX 22 22 ASN B 157 SER B 169 1 13
HELIX 23 23 ASN B 172 THR B 183 1 12
HELIX 24 24 SER B 184 GLN B 188 5 5
HELIX 25 25 LEU B 191 ALA B 197 1 7
HELIX 26 26 ASP B 210 GLU B 219 1 10
HELIX 27 27 ASN B 233 ASN B 238 1 6
HELIX 28 28 ASN B 238 ARG B 251 1 14
HELIX 29 29 TRP C 30 GLU C 35 1 6
HELIX 30 30 HIS C 50 ALA C 54 5 5
HELIX 31 31 GLY C 60 TYR C 75 1 16
HELIX 32 32 SER C 86 GLY C 99 1 14
HELIX 33 33 ASN C 117 GLU C 138 1 22
HELIX 34 34 PRO C 139 TYR C 148 1 10
HELIX 35 35 GLN C 149 ALA C 154 5 6
HELIX 36 36 ASN C 157 SER C 169 1 13
HELIX 37 37 ASN C 172 THR C 183 1 12
HELIX 38 38 SER C 184 GLN C 188 5 5
HELIX 39 39 LEU C 191 ALA C 197 1 7
HELIX 40 40 ASP C 210 GLU C 219 1 10
HELIX 41 41 ASN C 233 ASN C 238 1 6
HELIX 42 42 ASN C 238 ARG C 251 1 14
SHEET 1 A 7 ALA A 5 LYS A 8 0
SHEET 2 A 7 SER A 41 VAL A 45 -1 O TYR A 44 N GLN A 6
SHEET 3 A 7 TRP A 16 LEU A 20 1 N LEU A 17 O SER A 41
SHEET 4 A 7 PHE A 80 TYR A 85 1 O TRP A 81 N VAL A 18
SHEET 5 A 7 LEU A 103 GLU A 109 1 O CYS A 104 N PHE A 80
SHEET 6 A 7 ALA A 201 GLY A 207 1 O LEU A 205 N VAL A 108
SHEET 7 A 7 ASP A 223 ILE A 227 1 O HIS A 225 N TYR A 204
SHEET 1 B 7 ALA B 5 LYS B 8 0
SHEET 2 B 7 SER B 41 VAL B 45 -1 O TYR B 44 N GLN B 6
SHEET 3 B 7 TRP B 16 LEU B 20 1 N PHE B 19 O LEU B 43
SHEET 4 B 7 PHE B 80 TYR B 85 1 O VAL B 83 N VAL B 18
SHEET 5 B 7 LEU B 103 GLU B 109 1 O CYS B 104 N PHE B 80
SHEET 6 B 7 ALA B 201 GLY B 207 1 O LEU B 205 N VAL B 108
SHEET 7 B 7 ASP B 223 ILE B 227 1 O HIS B 225 N TYR B 204
SHEET 1 C 7 ALA C 5 LYS C 8 0
SHEET 2 C 7 SER C 41 VAL C 45 -1 O ARG C 42 N LYS C 8
SHEET 3 C 7 TRP C 16 LEU C 20 1 N LEU C 17 O LEU C 43
SHEET 4 C 7 PHE C 80 TYR C 85 1 O VAL C 83 N LEU C 20
SHEET 5 C 7 LEU C 103 GLU C 109 1 O CYS C 104 N PHE C 80
SHEET 6 C 7 PHE C 202 GLY C 207 1 O LEU C 205 N VAL C 108
SHEET 7 C 7 ASP C 223 ILE C 227 1 O HIS C 225 N TYR C 204
SITE 1 AC1 15 GLY A 22 PHE A 23 TYR A 85 SER A 86
SITE 2 AC1 15 LEU A 87 ARG A 90 ARG A 124 TRP A 147
SITE 3 AC1 15 TYR A 148 PHE A 153 HOH A 412 HOH A 418
SITE 4 AC1 15 HOH A 424 HOH A 440 HOH A 627
SITE 1 AC2 15 GLY B 22 PHE B 23 TYR B 85 SER B 86
SITE 2 AC2 15 LEU B 87 ARG B 90 TRP B 147 TYR B 148
SITE 3 AC2 15 PHE B 153 HOH B 411 HOH B 420 HOH B 422
SITE 4 AC2 15 HOH B 430 HOH B 433 HOH B 459
CRYST1 121.850 121.850 46.850 90.00 90.00 120.00 P 31 9
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 0.008207 0.004738 0.000000 0.00000
SCALE2 0.000000 0.009476 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021345 0.00000
TER 3820 PHE A 252
TER 7666 PHE B 252
TER 15218 PHE C 252
MASTER 394 0 2 42 21 0 8 6 6637 3 54 60
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