HEADER ISOMERASE 11-JUL-16 5LHE
TITLE PHOSPHORIBOSYL ANTHRANILATE ISOMERASE FROM THERMOCOCCUS KODAKARAENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PRAI;
COMPND 5 EC: 5.3.1.24;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARENSIS (STRAIN ATCC BAA-918
SOURCE 3 / JCM 12380 / KOD1);
SOURCE 4 ORGANISM_TAXID: 69014;
SOURCE 5 GENE: TRPF, TK0256;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-28A;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: TKTRPF-PET-28
KEYWDS TRYPTOPHAN BIOSYNTHESIS, TIM BARREL, PROTEIN STABILITY, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PERVEEN,N.RASHID,A.C.PAPAGEORGIOU
REVDAT 3 10-JAN-24 5LHE 1 LINK
REVDAT 2 28-DEC-16 5LHE 1 JRNL
REVDAT 1 09-NOV-16 5LHE 0
JRNL AUTH S.PERVEEN,N.RASHID,A.C.PAPAGEORGIOU
JRNL TITL CRYSTAL STRUCTURE OF A PHOSPHORIBOSYL ANTHRANILATE ISOMERASE
JRNL TITL 2 FROM THE HYPERTHERMOPHILIC ARCHAEON THERMOCOCCUS
JRNL TITL 3 KODAKARAENSIS.
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 72 804 2016
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 2053-230X
JRNL PMID 27827353
JRNL DOI 10.1107/S2053230X16015223
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 15340
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 754
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 24.7225 - 3.1617 0.91 3050 178 0.1896 0.2016
REMARK 3 2 3.1617 - 2.5103 0.91 2969 158 0.2362 0.2999
REMARK 3 3 2.5103 - 2.1932 0.90 2899 149 0.2452 0.3417
REMARK 3 4 2.1932 - 1.9928 0.88 2846 142 0.2446 0.3368
REMARK 3 5 1.9928 - 1.8500 0.88 2822 127 0.2519 0.3029
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.590
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) : 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 1640
REMARK 3 ANGLE : 1.128 2219
REMARK 3 CHIRALITY : 0.042 255
REMARK 3 PLANARITY : 0.005 286
REMARK 3 DIHEDRAL : 13.719 625
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 2:34)
REMARK 3 ORIGIN FOR THE GROUP (A): 97.8051 21.5467 8.8010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1495 T22: 0.2092
REMARK 3 T33: 0.1977 T12: -0.0632
REMARK 3 T13: -0.0554 T23: 0.0684
REMARK 3 L TENSOR
REMARK 3 L11: 1.5547 L22: 1.4026
REMARK 3 L33: 0.8872 L12: -0.1311
REMARK 3 L13: 0.0387 L23: -0.3489
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: -0.1814 S13: -0.0575
REMARK 3 S21: -0.2717 S22: 0.2702 S23: 0.2476
REMARK 3 S31: 0.1104 S32: -0.3390 S33: -0.0736
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 35:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 107.2581 16.9867 3.6473
REMARK 3 T TENSOR
REMARK 3 T11: 0.1721 T22: 0.1647
REMARK 3 T33: 0.1687 T12: -0.0317
REMARK 3 T13: 0.0284 T23: -0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 3.8338 L22: 6.5576
REMARK 3 L33: 5.2103 L12: 2.2722
REMARK 3 L13: -2.3096 L23: -3.5264
REMARK 3 S TENSOR
REMARK 3 S11: -0.1202 S12: 0.0012 S13: 0.0509
REMARK 3 S21: -0.5338 S22: -0.1376 S23: -0.3814
REMARK 3 S31: 0.3256 S32: 0.1755 S33: -0.0714
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 46:78)
REMARK 3 ORIGIN FOR THE GROUP (A): 109.8207 26.0226 7.5998
REMARK 3 T TENSOR
REMARK 3 T11: 0.1199 T22: 0.1248
REMARK 3 T33: 0.2059 T12: -0.0106
REMARK 3 T13: 0.0201 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.2765 L22: 1.5402
REMARK 3 L33: 1.5297 L12: 0.3408
REMARK 3 L13: -0.4269 L23: 0.4807
REMARK 3 S TENSOR
REMARK 3 S11: 0.2601 S12: 0.0736 S13: 0.1244
REMARK 3 S21: -0.3574 S22: -0.1470 S23: -0.4906
REMARK 3 S31: -0.1679 S32: 0.0360 S33: -0.0351
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 79:107)
REMARK 3 ORIGIN FOR THE GROUP (A): 112.8949 28.9212 18.5957
REMARK 3 T TENSOR
REMARK 3 T11: 0.1773 T22: 0.1370
REMARK 3 T33: 0.2390 T12: -0.0332
REMARK 3 T13: -0.0347 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.2430 L22: 0.3123
REMARK 3 L33: 1.4655 L12: 0.2402
REMARK 3 L13: -0.6963 L23: -0.2553
REMARK 3 S TENSOR
REMARK 3 S11: 0.1860 S12: -0.1190 S13: 0.1915
REMARK 3 S21: 0.2674 S22: -0.1534 S23: -0.2562
REMARK 3 S31: -0.3657 S32: 0.0339 S33: 0.0105
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 108:115)
REMARK 3 ORIGIN FOR THE GROUP (A): 104.8289 18.5574 39.6037
REMARK 3 T TENSOR
REMARK 3 T11: 0.5698 T22: 0.3395
REMARK 3 T33: 0.3507 T12: 0.0139
REMARK 3 T13: -0.0961 T23: 0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 0.8839 L22: 0.3980
REMARK 3 L33: 0.9915 L12: 0.3410
REMARK 3 L13: 0.2653 L23: 0.5929
REMARK 3 S TENSOR
REMARK 3 S11: 0.2518 S12: -0.5302 S13: -0.5532
REMARK 3 S21: 0.1038 S22: -0.0442 S23: -0.3896
REMARK 3 S31: 0.6413 S32: 0.6112 S33: -0.0652
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 116:135)
REMARK 3 ORIGIN FOR THE GROUP (A): 107.6728 28.6811 28.4491
REMARK 3 T TENSOR
REMARK 3 T11: 0.3413 T22: 0.3158
REMARK 3 T33: 0.0753 T12: -0.1451
REMARK 3 T13: -0.0913 T23: -0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 1.2611 L22: 0.9865
REMARK 3 L33: 1.5198 L12: 0.6316
REMARK 3 L13: -0.0741 L23: 0.3202
REMARK 3 S TENSOR
REMARK 3 S11: 0.2103 S12: -0.4724 S13: -0.1291
REMARK 3 S21: 0.3247 S22: -0.0019 S23: -0.0921
REMARK 3 S31: 0.0180 S32: 0.2864 S33: 0.0122
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 136:201)
REMARK 3 ORIGIN FOR THE GROUP (A): 93.6300 19.5211 23.4727
REMARK 3 T TENSOR
REMARK 3 T11: 0.2435 T22: 0.2248
REMARK 3 T33: 0.1490 T12: -0.0750
REMARK 3 T13: 0.0552 T23: -0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 0.4659 L22: 1.4971
REMARK 3 L33: 1.3547 L12: -0.0193
REMARK 3 L13: 0.1850 L23: -0.1458
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: -0.0138 S13: 0.0221
REMARK 3 S21: 0.3904 S22: 0.0898 S23: 0.4065
REMARK 3 S31: 0.0198 S32: -0.3741 S33: -0.0393
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 202:208)
REMARK 3 ORIGIN FOR THE GROUP (A): 83.9856 24.9881 18.1924
REMARK 3 T TENSOR
REMARK 3 T11: 0.0377 T22: 0.2877
REMARK 3 T33: 0.8458 T12: -0.0590
REMARK 3 T13: 0.1484 T23: 0.1656
REMARK 3 L TENSOR
REMARK 3 L11: 1.9997 L22: 0.2740
REMARK 3 L33: 1.1960 L12: 0.6867
REMARK 3 L13: 0.1160 L23: 0.2510
REMARK 3 S TENSOR
REMARK 3 S11: 0.0820 S12: -0.0837 S13: 0.5975
REMARK 3 S21: -0.0423 S22: -0.0777 S23: 0.2787
REMARK 3 S31: -0.2369 S32: -0.2517 S33: -0.2557
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 5LHE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000591.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96598
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15362
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 38.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.41400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: 4AAJ
REMARK 200
REMARK 200 REMARK: RODS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8, 0.2 M SODIUM
REMARK 280 FORMATE, 12% PEG 4000, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 44.34800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 14.54800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.34800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 14.54800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 NA NA A 302 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 424 LIES ON A SPECIAL POSITION.
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 563 O HOH A 569 1.80
REMARK 500 O HOH A 518 O HOH A 530 1.86
REMARK 500 O HOH A 552 O HOH A 566 2.03
REMARK 500 O HOH A 498 O HOH A 537 2.03
REMARK 500 OE2 GLU A 109 O HOH A 401 2.06
REMARK 500 O ARG A 108 O HOH A 402 2.07
REMARK 500 O HOH A 495 O HOH A 499 2.07
REMARK 500 O HOH A 433 O HOH A 569 2.09
REMARK 500 O HOH A 405 O HOH A 466 2.11
REMARK 500 OE2 GLU A 45 O HOH A 403 2.12
REMARK 500 OD2 ASP A 130 O HOH A 404 2.12
REMARK 500 O VAL A 2 O HOH A 405 2.13
REMARK 500 O HOH A 450 O HOH A 488 2.13
REMARK 500 O HOH A 519 O HOH A 574 2.15
REMARK 500 OE1 GLU A 71 O HOH A 406 2.16
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 403 O HOH A 472 4745 2.19
REMARK 500 O HOH A 520 O HOH A 546 4755 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 GLU A 3 -153.04 -119.12
REMARK 500 ASP A 83 47.57 -81.89
REMARK 500 SER A 184 -86.94 -125.99
REMARK 500 ARG A 206 68.26 -54.19
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 582 DISTANCE = 6.14 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 417 O
REMARK 620 2 HOH A 498 O 64.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 476 O
REMARK 620 2 HOH A 476 O 99.6
REMARK 620 3 HOH A 544 O 64.1 134.5
REMARK 620 4 HOH A 544 O 136.3 63.4 155.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 302
DBREF 5LHE A 2 208 UNP Q9YGB1 TRPF_THEKO 2 208
SEQRES 1 A 207 VAL GLU PHE VAL LYS ILE CYS GLY VAL LYS THR MET ASP
SEQRES 2 A 207 GLU LEU ARG LEU VAL GLU ARG TYR ALA ASP ALA THR GLY
SEQRES 3 A 207 VAL VAL VAL ASN SER ARG SER LYS ARG LYS VAL PRO LEU
SEQRES 4 A 207 LYS THR ALA ALA GLU LEU ILE GLU MET ALA GLU ILE PRO
SEQRES 5 A 207 ILE TYR LEU VAL SER THR MET LYS THR PHE PRO GLU TRP
SEQRES 6 A 207 ALA ASN ALA VAL GLU LYS THR GLY ALA GLU TYR ILE GLN
SEQRES 7 A 207 VAL HIS SER ASP MET HIS PRO LYS ALA VAL ASN ARG LEU
SEQRES 8 A 207 LYS ASP GLU TYR GLY VAL SER VAL MET LYS ALA PHE MET
SEQRES 9 A 207 VAL PRO ARG GLU SER ASP ASP PRO ALA GLU ASP ALA GLU
SEQRES 10 A 207 ARG LEU LEU GLU LEU ILE GLY GLN TYR GLU VAL ASP LYS
SEQRES 11 A 207 ILE LEU LEU ASP THR GLY VAL GLY SER GLY ARG ARG HIS
SEQRES 12 A 207 ASP TYR ARG VAL SER ALA ILE ILE ALA LYS GLU TYR PRO
SEQRES 13 A 207 ILE VAL LEU ALA GLY GLY LEU THR PRO GLU ASN VAL GLY
SEQRES 14 A 207 GLU ALA ILE ARG TRP VAL LYS PRO ALA GLY VAL ASP VAL
SEQRES 15 A 207 SER SER GLY VAL GLU ARG ASN GLY VAL LYS ASP ARG VAL
SEQRES 16 A 207 LEU ILE GLU ALA PHE MET ALA VAL VAL ARG ASN GLY
HET NA A 301 1
HET NA A 302 1
HETNAM NA SODIUM ION
FORMUL 2 NA 2(NA 1+)
FORMUL 4 HOH *182(H2 O)
HELIX 1 AA1 THR A 12 GLU A 20 1 9
HELIX 2 AA2 PRO A 39 ALA A 50 1 12
HELIX 3 AA3 THR A 62 GLY A 74 1 13
HELIX 4 AA4 HIS A 85 GLY A 97 1 13
HELIX 5 AA5 ASP A 112 GLY A 125 1 14
HELIX 6 AA6 SER A 140 ALA A 153 1 14
HELIX 7 AA7 ASN A 168 LYS A 177 1 10
HELIX 8 AA8 SER A 184 GLY A 186 5 3
HELIX 9 AA9 ASP A 194 ARG A 206 1 13
SHEET 1 AA1 9 PHE A 4 CYS A 8 0
SHEET 2 AA1 9 ALA A 25 VAL A 29 1 O ALA A 25 N ILE A 7
SHEET 3 AA1 9 ILE A 54 SER A 58 1 O TYR A 55 N THR A 26
SHEET 4 AA1 9 TYR A 77 VAL A 80 1 O GLN A 79 N LEU A 56
SHEET 5 AA1 9 SER A 99 MET A 105 1 O MET A 101 N ILE A 78
SHEET 6 AA1 9 LYS A 131 ASP A 135 1 O LEU A 133 N PHE A 104
SHEET 7 AA1 9 VAL A 159 ALA A 161 1 O ALA A 161 N LEU A 134
SHEET 8 AA1 9 GLY A 180 VAL A 183 1 O GLY A 180 N LEU A 160
SHEET 9 AA1 9 PHE A 4 CYS A 8 1 N LYS A 6 O VAL A 181
SHEET 1 AA2 2 GLU A 188 ARG A 189 0
SHEET 2 AA2 2 VAL A 192 LYS A 193 -1 O VAL A 192 N ARG A 189
LINK NA NA A 301 O HOH A 417 1555 1555 2.42
LINK NA NA A 301 O HOH A 498 1555 2755 3.13
LINK NA NA A 302 O HOH A 476 1555 1555 2.91
LINK NA NA A 302 O HOH A 476 1555 2755 2.96
LINK NA NA A 302 O HOH A 544 1555 1555 2.55
LINK NA NA A 302 O HOH A 544 1555 2755 2.56
CISPEP 1 GLU A 109 SER A 110 0 -1.30
CISPEP 2 SER A 110 ASP A 111 0 -16.68
SITE 1 AC1 5 MET A 13 TYR A 22 MET A 49 GLU A 199
SITE 2 AC1 5 HOH A 417
SITE 1 AC2 2 HOH A 476 HOH A 544
CRYST1 88.696 29.096 83.946 90.00 114.16 90.00 C 1 2 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 0.011274 0.000000 0.005057 0.00000
SCALE2 0.000000 0.034369 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013056 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
