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HEADER HYDROLASE 10-AUG-22 8E18
TITLE CRYSTAL STRUCTURE OF APO TNMK1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SECRETED HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. CB03234;
SOURCE 3 ORGANISM_TAXID: 1703937;
SOURCE 4 GENE: TNMK1, AMK26_32035;
SOURCE 5 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1916
KEYWDS BIOSYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-C.LIU,C.GUI,B.SHEN
REVDAT 1 09-NOV-22 8E18 0
JRNL AUTH C.GUI,E.KALKREUTER,Y.C.LIU,A.ADHIKARI,C.N.TEIJARO,D.YANG,
JRNL AUTH 2 C.CHANG,B.SHEN
JRNL TITL INTRAMOLECULAR C-C BOND FORMATION LINKS ANTHRAQUINONE AND
JRNL TITL 2 ENEDIYNE SCAFFOLDS IN TIANCIMYCIN BIOSYNTHESIS.
JRNL REF J.AM.CHEM.SOC. 2022
JRNL REFN ESSN 1520-5126
JRNL PMID 36279548
JRNL DOI 10.1021/JACS.2C08957
REMARK 2
REMARK 2 RESOLUTION. 1.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 172050
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.134
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.153
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 8587
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.14
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 345
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 6.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 15
REMARK 3 BIN FREE R VALUE : 0.3567
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3545
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 772
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.58
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.11
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8E18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1000266442.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-19
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) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 172050
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.130
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 56.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.15
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: MRBUMP
REMARK 200 STARTING MODEL: 5UNO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.0, 1.0 M SUCCINIC
REMARK 280 ACID, PH 7.0, AND 1% W/V PEG 2000 MME, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
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 66.19600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.00300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.00300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.09800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.00300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.00300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 99.29400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.00300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.00300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.09800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.00300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.00300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 99.29400
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 66.19600
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 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 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 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 A1008 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1152 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1264 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 MET A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 HIS A 4
REMARK 465 ARG A 5
REMARK 465 SER A 6
REMARK 465 VAL A 7
REMARK 465 ALA A 473
REMARK 465 ASP A 474
REMARK 465 GLY A 475
REMARK 465 GLY A 476
REMARK 465 PRO A 477
REMARK 465 ALA A 478
REMARK 465 GLY A 479
REMARK 465 GLU A 480
REMARK 465 GLY A 481
REMARK 465 SER A 482
REMARK 465 PRO A 483
REMARK 465 SER A 484
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 751 O HOH A 1063 1.71
REMARK 500 O HOH A 911 O HOH A 981 1.73
REMARK 500 O HOH A 1063 O HOH A 1328 1.78
REMARK 500 O HOH A 1027 O HOH A 1100 1.85
REMARK 500 O HOH A 672 O HOH A 1007 1.86
REMARK 500 O HOH A 919 O HOH A 1257 1.87
REMARK 500 O HOH A 1078 O HOH A 1105 1.88
REMARK 500 O HOH A 673 O HOH A 983 1.89
REMARK 500 O HOH A 732 O HOH A 1078 1.91
REMARK 500 O HOH A 1196 O HOH A 1311 1.92
REMARK 500 O1S EPE A 502 O HOH A 601 1.94
REMARK 500 O HOH A 1088 O HOH A 1091 1.95
REMARK 500 O HOH A 817 O HOH A 1031 1.98
REMARK 500 OD2 ASP A 72 O HOH A 602 1.99
REMARK 500 O HOH A 870 O HOH A 988 2.01
REMARK 500 O HOH A 1045 O HOH A 1091 2.03
REMARK 500 O HOH A 1043 O HOH A 1324 2.03
REMARK 500 O HOH A 613 O HOH A 1120 2.03
REMARK 500 O HOH A 831 O HOH A 996 2.04
REMARK 500 O HOH A 956 O HOH A 975 2.04
REMARK 500 O HOH A 609 O HOH A 646 2.04
REMARK 500 O HOH A 1022 O HOH A 1043 2.06
REMARK 500 O HOH A 911 O HOH A 1284 2.07
REMARK 500 O HOH A 637 O HOH A 923 2.07
REMARK 500 O HOH A 912 O HOH A 1190 2.08
REMARK 500 O HOH A 634 O HOH A 988 2.08
REMARK 500 O HOH A 1081 O HOH A 1121 2.08
REMARK 500 O HOH A 783 O HOH A 890 2.10
REMARK 500 O HOH A 1215 O HOH A 1222 2.10
REMARK 500 O HOH A 1097 O HOH A 1196 2.10
REMARK 500 O HOH A 647 O HOH A 1020 2.10
REMARK 500 O HOH A 1023 O HOH A 1274 2.11
REMARK 500 O HOH A 601 O HOH A 984 2.11
REMARK 500 O8 EPE A 501 O HOH A 603 2.11
REMARK 500 O HOH A 629 O HOH A 869 2.12
REMARK 500 O HOH A 1072 O HOH A 1093 2.12
REMARK 500 O HOH A 1308 O HOH A 1323 2.12
REMARK 500 O HOH A 807 O HOH A 1236 2.13
REMARK 500 O HOH A 1022 O HOH A 1081 2.14
REMARK 500 O HOH A 668 O HOH A 1247 2.14
REMARK 500 O HOH A 621 O HOH A 1100 2.15
REMARK 500 O HOH A 1354 O HOH A 1356 2.15
REMARK 500 O HOH A 1037 O HOH A 1227 2.16
REMARK 500 O HOH A 625 O HOH A 975 2.16
REMARK 500 O HOH A 1226 O HOH A 1300 2.16
REMARK 500 O HOH A 1109 O HOH A 1248 2.16
REMARK 500 O HOH A 1274 O HOH A 1283 2.17
REMARK 500 O HOH A 674 O HOH A 839 2.17
REMARK 500 O HOH A 645 O HOH A 1057 2.17
REMARK 500 O HOH A 952 O HOH A 1170 2.18
REMARK 500
REMARK 500 THIS ENTRY HAS 51 CLOSE CONTACTS
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 963 O HOH A 983 6444 2.01
REMARK 500 O HOH A 763 O HOH A 1099 6444 2.09
REMARK 500 O HOH A 1198 O HOH A 1365 7645 2.16
REMARK 500 O HOH A 850 O HOH A 1059 3545 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 109 79.71 -106.15
REMARK 500 LEU A 122 35.89 -96.13
REMARK 500 ALA A 149 22.68 -141.96
REMARK 500 SER A 183 -119.35 62.93
REMARK 500 PHE A 196 20.46 -140.44
REMARK 500 ASP A 201 -86.37 -93.35
REMARK 500 SER A 207 78.43 63.85
REMARK 500 LEU A 422 43.40 -108.01
REMARK 500 ARG A 438 96.50 77.08
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 A1354 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A1355 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A1356 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A1357 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A1358 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A1359 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1360 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH A1361 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A1362 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A1363 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A1364 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A1365 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A1366 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A1367 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A1368 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A1369 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH A1370 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH A1371 DISTANCE = 7.95 ANGSTROMS
REMARK 525 HOH A1372 DISTANCE = 8.47 ANGSTROMS
DBREF1 8E18 A 1 484 UNP A0A125SA14_9ACTN
DBREF2 8E18 A A0A125SA14 1 484
SEQRES 1 A 484 MET THR GLU HIS ARG SER VAL ARG PHE SER ALA PRO ARG
SEQRES 2 A 484 PRO SER TRP ARG PRO ALA GLY ASP ASP THR PRO LEU ALA
SEQRES 3 A 484 GLY LEU GLU CYS ALA THR VAL THR VAL PRO VAL ASP HIS
SEQRES 4 A 484 ALA ARG PRO ASP GLY PRO THR LEU GLU VAL ALA LEU ALA
SEQRES 5 A 484 ARG HIS PRO ALA ARG SER ALA GLY ARG ARG ARG GLY VAL
SEQRES 6 A 484 LEU LEU VAL GLY PRO ASP ASP PRO GLY ASN PRO GLY THR
SEQRES 7 A 484 LEU LEU VAL PRO GLN LEU VAL ARG ASP LEU PRO ALA ASP
SEQRES 8 A 484 VAL LEU ASP GLY TYR ASP VAL VAL GLY PHE ASP HIS ARG
SEQRES 9 A 484 PHE SER GLY GLY SER ALA PRO LEU SER CYS GLY LEU THR
SEQRES 10 A 484 PRO ASP GLN TRP LEU TRP ILE PHE HIS ARG PRO GLN ASP
SEQRES 11 A 484 VAL GLU SER GLU ALA ARG PHE GLN ARG ALA VAL VAL GLU
SEQRES 12 A 484 ARG CYS PHE ASP ALA ALA GLY ASP VAL LEU PRO TYR LEU
SEQRES 13 A 484 THR SER ARG ASP ILE ALA ARG ASP MET ASP VAL ILE ARG
SEQRES 14 A 484 ARG ALA LEU GLY GLU ASP ARG ILE SER TYR LEU GLY HIS
SEQRES 15 A 484 SER TYR GLY SER TYR LEU GLY ALA VAL TRP THR GLN MET
SEQRES 16 A 484 PHE GLY GLU HIS ALA ASP ARG VAL VAL LEU ASP SER VAL
SEQRES 17 A 484 ILE ASP PRO SER SER VAL TRP ARG ARG MET PHE LEU ASP
SEQRES 18 A 484 TYR ALA VAL SER CYS GLU ALA ALA LEU GLU ARG TRP ALA
SEQRES 19 A 484 HIS TRP ALA ALA GLU ARG ASP GLY GLU LEU ASP LEU GLY
SEQRES 20 A 484 ARG ASP ALA PRO THR VAL ARG ALA ALA LEU ASP ALA LEU
SEQRES 21 A 484 ALA GLY ARG ALA ASP ARG GLU PRO LEU PRO VAL ALA GLY
SEQRES 22 A 484 MET PRO VAL ASP GLY THR MET LEU ARG LEU PHE THR MET
SEQRES 23 A 484 VAL LEU LEU SER SER ASP ARG ALA TRP GLY PHE LEU GLY
SEQRES 24 A 484 ASP ILE VAL ARG ALA ALA VAL HIS GLY ASP GLU ALA ALA
SEQRES 25 A 484 PRO SER THR LEU ARG ALA LEU GLY ALA MET PHE GLY ARG
SEQRES 26 A 484 GLY LYS GLU GLU SER GLY ALA VAL ALA GLN LEU GLY VAL
SEQRES 27 A 484 LEU CYS GLY ASP ALA ALA TRP PRO ARG ASP MET GLU VAL
SEQRES 28 A 484 TYR ARG ARG ASP LEU ALA GLY HIS GLY ALA ARG HIS PRO
SEQRES 29 A 484 PHE ILE GLY PRO ALA MET ALA GLY PRO LYS ALA GLY ALA
SEQRES 30 A 484 PHE TRP PRO VAL PRO PRO ALA GLU PRO VAL THR VAL LEU
SEQRES 31 A 484 GLY ALA ASP ASN ARG ALA GLU SER VAL LEU LEU VAL GLN
SEQRES 32 A 484 SER GLU GLN ASP MET PHE THR PRO ALA ARG GLY ALA ARG
SEQRES 33 A 484 ARG MET ARG GLU LEU LEU ALA HIS ASN THR ARG LEU VAL
SEQRES 34 A 484 THR LEU ALA GLY ALA VAL GLN HIS ARG VAL PHE PRO PHE
SEQRES 35 A 484 HIS GLY ASP PRO GLY VAL ASN ARG ALA ALA ALA ALA TYR
SEQRES 36 A 484 LEU LEU THR GLY LYS LEU PRO ASP THR ASP LEU THR LEU
SEQRES 37 A 484 ARG ALA ALA ALA ALA ASP GLY GLY PRO ALA GLY GLU GLY
SEQRES 38 A 484 SER PRO SER
HET EPE A 501 15
HET EPE A 502 15
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 2 EPE 2(C8 H18 N2 O4 S)
FORMUL 4 HOH *772(H2 O)
HELIX 1 AA1 PRO A 76 THR A 78 5 3
HELIX 2 AA2 LEU A 79 LEU A 88 1 10
HELIX 3 AA3 PRO A 89 GLY A 95 1 7
HELIX 4 AA4 THR A 117 LEU A 122 1 6
HELIX 5 AA5 ASP A 130 GLY A 150 1 21
HELIX 6 AA6 VAL A 152 LEU A 156 5 5
HELIX 7 AA7 THR A 157 GLY A 173 1 17
HELIX 8 AA8 SER A 183 GLY A 197 1 15
HELIX 9 AA9 ASP A 210 VAL A 214 5 5
HELIX 10 AB1 TRP A 215 GLU A 239 1 25
HELIX 11 AB2 ARG A 240 ASP A 245 1 6
HELIX 12 AB3 ASP A 249 GLU A 267 1 19
HELIX 13 AB4 ASP A 277 SER A 290 1 14
HELIX 14 AB5 SER A 291 ARG A 293 5 3
HELIX 15 AB6 ALA A 294 GLY A 308 1 15
HELIX 16 AB7 ALA A 312 GLY A 324 1 13
HELIX 17 AB8 GLU A 328 ASP A 342 1 15
HELIX 18 AB9 ASP A 348 GLY A 358 1 11
HELIX 19 AC1 GLY A 358 HIS A 363 1 6
HELIX 20 AC2 ILE A 366 GLY A 372 1 7
HELIX 21 AC3 LYS A 374 TRP A 379 5 6
HELIX 22 AC4 PRO A 411 LEU A 422 1 12
HELIX 23 AC5 ASP A 445 GLY A 459 1 15
SHEET 1 AA110 ARG A 17 PRO A 18 0
SHEET 2 AA110 GLU A 29 PRO A 36 -1 O CYS A 30 N ARG A 17
SHEET 3 AA110 THR A 46 HIS A 54 -1 O LEU A 51 N ALA A 31
SHEET 4 AA110 TYR A 96 PHE A 101 -1 O VAL A 98 N HIS A 54
SHEET 5 AA110 GLY A 64 VAL A 68 1 N LEU A 66 O ASP A 97
SHEET 6 AA110 ILE A 177 HIS A 182 1 O SER A 178 N LEU A 67
SHEET 7 AA110 ALA A 200 ASP A 206 1 O VAL A 204 N TYR A 179
SHEET 8 AA110 VAL A 399 GLN A 406 1 O LEU A 400 N VAL A 203
SHEET 9 AA110 THR A 426 VAL A 435 1 O ARG A 427 N LEU A 401
SHEET 10 AA110 LEU A 466 ARG A 469 1 O LEU A 468 N ALA A 432
SHEET 1 AA2 2 LEU A 269 VAL A 271 0
SHEET 2 AA2 2 MET A 274 VAL A 276 -1 O VAL A 276 N LEU A 269
CISPEP 1 VAL A 214 TRP A 215 0 -22.09
CISPEP 2 PHE A 440 PRO A 441 0 0.14
CRYST1 86.006 86.006 132.392 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 0.011627 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011627 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007553 0.00000
TER 3633 ALA A 472
MASTER 426 0 2 23 12 0 0 6 4347 1 30 38
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