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HEADER HYDROLASE 20-FEB-24 8W2D
TITLE HOLO-PCP-THIOESTERASE DI-DOMAIN STRUCTURE FROM THE SULFAZECIN
TITLE 2 BIOSYNTHETIC NONRIBOSOMAL PEPTIDE SYNTHETASE, SULM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-RIBOSOMAL PEPTIDE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: THIOESTERASE DIDOMAIN;
COMPND 5 SYNONYM: SULM;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THE PROTEIN WAS EXPRESSED AND CRYSTALLIZED WITH HIS-
COMPND 8 TAG FROM EXPRESSION VECTOR.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARABURKHOLDERIA ACIDICOLA;
SOURCE 3 ORGANISM_TAXID: 1912599;
SOURCE 4 STRAIN: ATCC 31363;
SOURCE 5 GENE: SULM, BWP39_23695;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS THIOESTERASE DOMAIN, NRPS, PCP DOMAIN, NONRIBOSOMAL PEPTIDE
KEYWDS 2 SYNTHETASE, SULFAZECIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.D.PATEL,A.M.GULICK
REVDAT 1 07-AUG-24 8W2D 0
JRNL AUTH K.D.PATEL,R.A.OLIVER,M.S.LICHSTRAHL,R.LI,C.A.TOWNSEND,
JRNL AUTH 2 A.M.GULICK
JRNL TITL THE STRUCTURE OF THE MONOBACTAM-PRODUCING THIOESTERASE
JRNL TITL 2 DOMAIN OF SULM FORMS A UNIQUE COMPLEX WITH THE UPSTREAM
JRNL TITL 3 CARRIER PROTEIN DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : GEOSTD + MONOMER LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 17786
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1768
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 40.4700 - 6.3300 0.97 1269 140 0.1996 0.2108
REMARK 3 2 6.3300 - 5.0300 0.99 1253 140 0.2122 0.2599
REMARK 3 3 5.0300 - 4.4000 0.96 1236 138 0.1844 0.1997
REMARK 3 4 4.4000 - 3.9900 0.99 1247 139 0.1788 0.2220
REMARK 3 5 3.9900 - 3.7100 0.98 1252 140 0.2120 0.2690
REMARK 3 6 3.7100 - 3.4900 0.96 1211 133 0.2371 0.2661
REMARK 3 7 3.4900 - 3.3100 0.98 1227 134 0.2457 0.2746
REMARK 3 8 3.3100 - 3.1700 1.00 1266 147 0.2307 0.2649
REMARK 3 9 3.1700 - 3.0500 0.99 1250 138 0.2505 0.3088
REMARK 3 10 3.0500 - 2.9400 0.98 1223 132 0.2713 0.3412
REMARK 3 11 2.9400 - 2.8500 0.98 1235 134 0.3062 0.3700
REMARK 3 12 2.8500 - 2.7700 0.99 1259 142 0.2912 0.3145
REMARK 3 13 2.7700 - 2.7000 0.87 1090 111 0.2855 0.3374
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) : 0.383
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.367
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.96
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 : 0.004 4924
REMARK 3 ANGLE : 0.801 6703
REMARK 3 CHIRALITY : 0.047 772
REMARK 3 PLANARITY : 0.004 871
REMARK 3 DIHEDRAL : 9.765 2899
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'A' AND ((RESID 2659 THROUGH 2660
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 2661 OR (RESID
REMARK 3 2662 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 2663
REMARK 3 THROUGH 2665 OR (RESID 2666 THROUGH 2667
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 2668 THROUGH
REMARK 3 2708 OR (RESID 2709 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 2710 THROUGH 2713 OR (RESID 2714
REMARK 3 THROUGH 2715 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 2716 THROUGH 2720 OR RESID 2727 THROUGH
REMARK 3 2735 OR (RESID 2736 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 2737 THROUGH 2740 OR (RESID 2741
REMARK 3 THROUGH 2742 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 2743 THROUGH 2765 OR (RESID 2766 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 2767 THROUGH 2876 OR
REMARK 3 (RESID 2877 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 2878 OR (RESID 2879 THROUGH 2880 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 2881 THROUGH 2934 OR
REMARK 3 (RESID 2935 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 2936 THROUGH 2979 OR RESID 3040 OR RESID
REMARK 3 3041 OR RESID 3042))
REMARK 3 SELECTION : (CHAIN 'B' AND ((RESID 2659 THROUGH 2660
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 2661 THROUGH
REMARK 3 2678 OR (RESID 2679 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 2680 THROUGH 2682 OR (RESID 2683
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 2684 THROUGH
REMARK 3 2720 OR RESID 2727 THROUGH 2769 OR (RESID
REMARK 3 2770 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 2771
REMARK 3 THROUGH 2783 OR (RESID 2784 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 2785 THROUGH 2790 OR (RESID
REMARK 3 2791 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 2792
REMARK 3 THROUGH 2808 OR (RESID 2809 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 2810 THROUGH 2853 OR (RESID
REMARK 3 2854 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 2855
REMARK 3 THROUGH 2911 OR (RESID 2912 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 2913 THROUGH 2943 OR (RESID
REMARK 3 2944 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 2945
REMARK 3 THROUGH 2963 OR (RESID 2964 THROUGH 2965
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 2966 THROUGH
REMARK 3 2979 OR RESID 3040 OR RESID 3041 THROUGH
REMARK 3 3042))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8W2D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-24.
REMARK 100 THE DEPOSITION ID IS D_1000281587.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7.0-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17876
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THIN RODS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M TRIBASIC AMMONIUM CITRATE,
REMARK 280 MICROBATCH, TEMPERATURE 293K
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 39.53600
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 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 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 GLY A 2640
REMARK 465 SER A 2641
REMARK 465 SER A 2642
REMARK 465 HIS A 2643
REMARK 465 HIS A 2644
REMARK 465 HIS A 2645
REMARK 465 HIS A 2646
REMARK 465 HIS A 2647
REMARK 465 HIS A 2648
REMARK 465 SER A 2649
REMARK 465 SER A 2650
REMARK 465 GLY A 2651
REMARK 465 LEU A 2652
REMARK 465 VAL A 2653
REMARK 465 PRO A 2654
REMARK 465 ARG A 2655
REMARK 465 GLU A 2725
REMARK 465 GLU A 2726
REMARK 465 LYS A 2980
REMARK 465 GLY A 2981
REMARK 465 VAL A 2982
REMARK 465 THR A 2983
REMARK 465 ALA A 2984
REMARK 465 GLY B 2640
REMARK 465 SER B 2641
REMARK 465 SER B 2642
REMARK 465 HIS B 2643
REMARK 465 HIS B 2644
REMARK 465 HIS B 2645
REMARK 465 HIS B 2646
REMARK 465 HIS B 2647
REMARK 465 HIS B 2648
REMARK 465 SER B 2649
REMARK 465 SER B 2650
REMARK 465 GLY B 2651
REMARK 465 LEU B 2652
REMARK 465 VAL B 2653
REMARK 465 PRO B 2654
REMARK 465 ARG B 2655
REMARK 465 GLY B 2656
REMARK 465 SER B 2657
REMARK 465 HIS B 2658
REMARK 465 GLU B 2721
REMARK 465 LYS B 2980
REMARK 465 GLY B 2981
REMARK 465 VAL B 2982
REMARK 465 THR B 2983
REMARK 465 ALA B 2984
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 A2660 CG CD OE1 OE2
REMARK 470 GLU A2664 CG CD OE1 OE2
REMARK 470 ASP A2679 CG OD1 OD2
REMARK 470 ASP A2683 CG OD1 OD2
REMARK 470 GLU A2718 CG CD OE1 OE2
REMARK 470 ASP A2770 CG OD1 OD2
REMARK 470 GLU A2782 CG CD OE1 OE2
REMARK 470 ASP A2784 CG OD1 OD2
REMARK 470 GLU A2791 CG CD OE1 OE2
REMARK 470 ASP A2809 CG OD1 OD2
REMARK 470 LYS A2854 CG CD CE NZ
REMARK 470 GLU A2912 CG CD OE1 OE2
REMARK 470 ARG A2944 CG CD NE CZ NH1 NH2
REMARK 470 GLU A2964 CG CD OE1 OE2
REMARK 470 MET B2659 CG SD CE
REMARK 470 LEU B2662 CG CD1 CD2
REMARK 470 GLU B2664 CG CD OE1 OE2
REMARK 470 PHE B2666 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B2667 CG CD NE CZ NH1 NH2
REMARK 470 ASP B2709 CG OD1 OD2
REMARK 470 GLU B2714 CG CD OE1 OE2
REMARK 470 GLU B2718 CG CD OE1 OE2
REMARK 470 HIS B2722 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B2725 CG CD OE1 OE2
REMARK 470 GLU B2726 CG CD OE1 OE2
REMARK 470 ASP B2736 CG OD1 OD2
REMARK 470 LYS B2741 CG CD CE NZ
REMARK 470 GLU B2766 CG CD OE1 OE2
REMARK 470 GLU B2782 CG CD OE1 OE2
REMARK 470 GLN B2877 CG CD OE1 NE2
REMARK 470 ASP B2879 CG OD1 OD2
REMARK 470 GLU B2880 CG CD OE1 OE2
REMARK 470 ARG B2935 CG CD NE CZ NH1 NH2
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 GLY A 2656 NH1 ARG A 2661 2.19
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 LEU A2684 39.36 -143.35
REMARK 500 HIS A2710 74.92 -155.24
REMARK 500 HIS A2722 33.19 -89.91
REMARK 500 ALA A2768 74.06 -155.08
REMARK 500 ALA A2818 -113.07 52.09
REMARK 500 ALA A2840 148.46 -170.53
REMARK 500 CYS A2962 57.61 -145.53
REMARK 500 SER B2688 -69.03 -29.43
REMARK 500 LYS B2690 -11.08 93.58
REMARK 500 ALA B2768 75.36 -153.65
REMARK 500 ALA B2818 -113.78 55.95
REMARK 500 ALA B2822 -70.73 -44.88
REMARK 500 CYS B2962 57.09 -144.38
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8W2D A 2660 2984 UNP A0A1I9RH13_9BURK
DBREF2 8W2D A A0A1I9RH13 2660 2984
DBREF1 8W2D B 2660 2984 UNP A0A1I9RH13_9BURK
DBREF2 8W2D B A0A1I9RH13 2660 2984
SEQADV 8W2D GLY A 2640 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER A 2641 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER A 2642 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS A 2643 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS A 2644 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS A 2645 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS A 2646 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS A 2647 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS A 2648 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER A 2649 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER A 2650 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D GLY A 2651 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D LEU A 2652 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D VAL A 2653 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D PRO A 2654 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D ARG A 2655 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D GLY A 2656 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER A 2657 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS A 2658 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D MET A 2659 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D ALA A 2818 UNP A0A1I9RH1 CYS 2818 CONFLICT
SEQADV 8W2D GLY B 2640 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER B 2641 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER B 2642 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS B 2643 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS B 2644 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS B 2645 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS B 2646 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS B 2647 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS B 2648 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER B 2649 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER B 2650 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D GLY B 2651 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D LEU B 2652 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D VAL B 2653 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D PRO B 2654 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D ARG B 2655 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D GLY B 2656 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D SER B 2657 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D HIS B 2658 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D MET B 2659 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2D ALA B 2818 UNP A0A1I9RH1 CYS 2818 CONFLICT
SEQRES 1 A 345 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 345 VAL PRO ARG GLY SER HIS MET GLU ARG LEU THR GLU ILE
SEQRES 3 A 345 PHE ARG GLY VAL LEU GLY HIS ALA ALA PHE GLY ILE ARG
SEQRES 4 A 345 ASP ASP PHE PHE ASP LEU GLY GLY ASP SER PHE LYS ALA
SEQRES 5 A 345 ILE ARG ILE ALA ALA LYS TYR GLY PRO PRO LEU GLU VAL
SEQRES 6 A 345 THR ASP ILE TYR ASP HIS PRO THR ILE GLU ALA LEU ALA
SEQRES 7 A 345 GLU HIS LEU GLU HIS ALA SER GLU GLU SER SER SER ILE
SEQRES 8 A 345 VAL LEU MET ALA GLY ASP PRO ALA THR ALA LYS ALA VAL
SEQRES 9 A 345 VAL VAL CYS VAL ALA ASN ALA ALA GLY GLY PRO VAL ASN
SEQRES 10 A 345 PHE VAL ASP MET SER ARG ALA MET PRO GLU GLN ALA SER
SEQRES 11 A 345 ASP VAL ALA MET PHE GLY VAL LYS LEU PRO ARG THR GLU
SEQRES 12 A 345 VAL ASP SER ASP GLY ALA MET LEU GLU GLU VAL ARG ARG
SEQRES 13 A 345 LEU SER ASN ALA VAL CYS ASP ASP LEU LEU ALA ALA THR
SEQRES 14 A 345 ASP LEU PRO ALA ILE VAL PHE ALA GLN ALA ASN GLY SER
SEQRES 15 A 345 ALA LEU ALA LEU ALA ILE THR ARG GLU LEU VAL ARG ARG
SEQRES 16 A 345 SER ALA ASP VAL ARG ALA LEU CYS ILE GLY GLY ALA LEU
SEQRES 17 A 345 MET ARG THR VAL THR GLY LYS ARG ASP THR ARG THR ASP
SEQRES 18 A 345 ASP GLU ILE LEU ALA PHE LEU GLY LYS ALA GLY SER THR
SEQRES 19 A 345 LEU PRO ALA GLN PRO ASP GLU GLN ALA PHE PHE LEU HIS
SEQRES 20 A 345 ASP PHE ARG TYR ASP GLY TRP LEU ALA ASP VAL TYR TYR
SEQRES 21 A 345 ASN HIS LEU VAL ASP LEU MET SER ARG GLY ALA LEU GLU
SEQRES 22 A 345 VAL VAL ASP ILE PRO VAL TRP CYS LEU VAL GLY SER GLU
SEQRES 23 A 345 ASP PRO LEU VAL PRO ASN TYR PRO VAL ARG PHE GLN ASP
SEQRES 24 A 345 TRP SER HIS ILE GLY ARG PRO VAL GLN LEU VAL GLU TYR
SEQRES 25 A 345 ALA GLY ILE GLY HIS TYR LEU LEU ARG ASP CYS PRO GLU
SEQRES 26 A 345 ALA ILE ALA ARG ALA VAL GLY SER VAL TRP GLU HIS VAL
SEQRES 27 A 345 SER CYS LYS GLY VAL THR ALA
SEQRES 1 B 345 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 345 VAL PRO ARG GLY SER HIS MET GLU ARG LEU THR GLU ILE
SEQRES 3 B 345 PHE ARG GLY VAL LEU GLY HIS ALA ALA PHE GLY ILE ARG
SEQRES 4 B 345 ASP ASP PHE PHE ASP LEU GLY GLY ASP SER PHE LYS ALA
SEQRES 5 B 345 ILE ARG ILE ALA ALA LYS TYR GLY PRO PRO LEU GLU VAL
SEQRES 6 B 345 THR ASP ILE TYR ASP HIS PRO THR ILE GLU ALA LEU ALA
SEQRES 7 B 345 GLU HIS LEU GLU HIS ALA SER GLU GLU SER SER SER ILE
SEQRES 8 B 345 VAL LEU MET ALA GLY ASP PRO ALA THR ALA LYS ALA VAL
SEQRES 9 B 345 VAL VAL CYS VAL ALA ASN ALA ALA GLY GLY PRO VAL ASN
SEQRES 10 B 345 PHE VAL ASP MET SER ARG ALA MET PRO GLU GLN ALA SER
SEQRES 11 B 345 ASP VAL ALA MET PHE GLY VAL LYS LEU PRO ARG THR GLU
SEQRES 12 B 345 VAL ASP SER ASP GLY ALA MET LEU GLU GLU VAL ARG ARG
SEQRES 13 B 345 LEU SER ASN ALA VAL CYS ASP ASP LEU LEU ALA ALA THR
SEQRES 14 B 345 ASP LEU PRO ALA ILE VAL PHE ALA GLN ALA ASN GLY SER
SEQRES 15 B 345 ALA LEU ALA LEU ALA ILE THR ARG GLU LEU VAL ARG ARG
SEQRES 16 B 345 SER ALA ASP VAL ARG ALA LEU CYS ILE GLY GLY ALA LEU
SEQRES 17 B 345 MET ARG THR VAL THR GLY LYS ARG ASP THR ARG THR ASP
SEQRES 18 B 345 ASP GLU ILE LEU ALA PHE LEU GLY LYS ALA GLY SER THR
SEQRES 19 B 345 LEU PRO ALA GLN PRO ASP GLU GLN ALA PHE PHE LEU HIS
SEQRES 20 B 345 ASP PHE ARG TYR ASP GLY TRP LEU ALA ASP VAL TYR TYR
SEQRES 21 B 345 ASN HIS LEU VAL ASP LEU MET SER ARG GLY ALA LEU GLU
SEQRES 22 B 345 VAL VAL ASP ILE PRO VAL TRP CYS LEU VAL GLY SER GLU
SEQRES 23 B 345 ASP PRO LEU VAL PRO ASN TYR PRO VAL ARG PHE GLN ASP
SEQRES 24 B 345 TRP SER HIS ILE GLY ARG PRO VAL GLN LEU VAL GLU TYR
SEQRES 25 B 345 ALA GLY ILE GLY HIS TYR LEU LEU ARG ASP CYS PRO GLU
SEQRES 26 B 345 ALA ILE ALA ARG ALA VAL GLY SER VAL TRP GLU HIS VAL
SEQRES 27 B 345 SER CYS LYS GLY VAL THR ALA
HET PNS A3001 42
HET EDO A3002 10
HET EDO A3003 10
HET EDO A3004 10
HET PNS B3001 42
HET EDO B3002 10
HET EDO B3003 10
HETNAM PNS 4'-PHOSPHOPANTETHEINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PNS 2(C11 H23 N2 O7 P S)
FORMUL 4 EDO 5(C2 H6 O2)
FORMUL 10 HOH *28(H2 O)
HELIX 1 AA1 SER A 2657 GLY A 2671 1 15
HELIX 2 AA2 ASP A 2687 GLY A 2699 1 13
HELIX 3 AA3 GLU A 2703 ASP A 2709 1 7
HELIX 4 AA4 THR A 2712 HIS A 2722 1 11
HELIX 5 AA5 GLY A 2753 ASN A 2756 5 4
HELIX 6 AA6 PHE A 2757 ALA A 2768 1 12
HELIX 7 AA7 SER A 2785 THR A 2808 1 24
HELIX 8 AA8 GLY A 2820 ARG A 2834 1 15
HELIX 9 AA9 THR A 2859 GLY A 2871 1 13
HELIX 10 AB1 GLN A 2877 ARG A 2908 1 32
HELIX 11 AB2 ASN A 2931 PHE A 2936 1 6
HELIX 12 AB3 GLN A 2937 ILE A 2942 5 6
HELIX 13 AB4 TYR A 2957 CYS A 2962 1 6
HELIX 14 AB5 CYS A 2962 VAL A 2977 1 16
HELIX 15 AB6 GLU B 2660 LEU B 2670 1 11
HELIX 16 AB7 PHE B 2681 GLY B 2685 5 5
HELIX 17 AB8 ALA B 2691 GLY B 2699 1 9
HELIX 18 AB9 VAL B 2704 ASP B 2709 1 6
HELIX 19 AC1 THR B 2712 LEU B 2720 1 9
HELIX 20 AC2 GLY B 2753 ASN B 2756 5 4
HELIX 21 AC3 PHE B 2757 ALA B 2768 1 12
HELIX 22 AC4 SER B 2785 THR B 2808 1 24
HELIX 23 AC5 GLY B 2820 ARG B 2834 1 15
HELIX 24 AC6 THR B 2859 GLY B 2871 1 13
HELIX 25 AC7 GLN B 2877 ARG B 2908 1 32
HELIX 26 AC8 ASN B 2931 PHE B 2936 1 6
HELIX 27 AC9 GLN B 2937 ILE B 2942 5 6
HELIX 28 AD1 TYR B 2957 CYS B 2962 1 6
HELIX 29 AD2 CYS B 2962 VAL B 2977 1 16
SHEET 1 AA1 7 ILE A2730 ALA A2734 0
SHEET 2 AA1 7 VAL A2771 VAL A2776 -1 O MET A2773 N MET A2733
SHEET 3 AA1 7 ALA A2742 VAL A2747 1 N CYS A2746 O VAL A2776
SHEET 4 AA1 7 ALA A2812 GLN A2817 1 O ILE A2813 N VAL A2745
SHEET 5 AA1 7 VAL A2838 GLY A2844 1 O CYS A2842 N VAL A2814
SHEET 6 AA1 7 VAL A2918 GLY A2923 1 O TRP A2919 N ILE A2843
SHEET 7 AA1 7 VAL A2946 TYR A2951 1 O GLN A2947 N VAL A2918
SHEET 1 AA2 7 ILE B2730 ALA B2734 0
SHEET 2 AA2 7 VAL B2771 VAL B2776 -1 O MET B2773 N MET B2733
SHEET 3 AA2 7 ALA B2742 VAL B2747 1 N CYS B2746 O VAL B2776
SHEET 4 AA2 7 ALA B2812 GLN B2817 1 O ILE B2813 N VAL B2745
SHEET 5 AA2 7 VAL B2838 GLY B2844 1 O CYS B2842 N VAL B2814
SHEET 6 AA2 7 VAL B2918 GLY B2923 1 O TRP B2919 N LEU B2841
SHEET 7 AA2 7 VAL B2946 TYR B2951 1 O GLN B2947 N CYS B2920
LINK OG SER A2688 P24 PNS A3001 1555 1555 1.60
LINK OG SER B2688 P24 PNS B3001 1555 1555 1.60
CISPEP 1 ARG A 2944 PRO A 2945 0 -2.13
CISPEP 2 PRO B 2700 PRO B 2701 0 -2.13
CISPEP 3 ARG B 2944 PRO B 2945 0 0.27
CRYST1 60.116 79.072 70.484 90.00 93.52 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 0.016635 0.000000 0.001022 0.00000
SCALE2 0.000000 0.012647 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014214 0.00000
TER 4727 CYS A2979
TER 9376 CYS B2979
MASTER 398 0 7 29 14 0 0 6 4856 2 136 54
END |