HEADER TRANSCRIPTION 03-APR-09 3GXX
TITLE STRUCTURE OF THE SH2 DOMAIN OF THE CANDIDA GLABRATA TRANSCRIPTION
TITLE 2 ELONGATION FACTOR SPT6, CRYSTAL FORM B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION ELONGATION FACTOR SPT6;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: CHROMATIN ELONGATION FACTOR SPT6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA GLABRATA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 5478;
SOURCE 5 GENE: CAGL0L04774G, SPT6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL23 (DE3) CODONPLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS SH2-FOLD, THREE STRANDED ANTI-PARALLEL BETA SHEET, N-TERMINAL ALPHA
KEYWDS 2 HELIX, C-TERMINAL ALPHA HELIX, NUCLEUS, SH2 DOMAIN, TRANSCRIPTION,
KEYWDS 3 TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DENGL,A.MAYER,M.SUN,P.CRAMER
REVDAT 4 22-NOV-23 3GXX 1 REMARK
REVDAT 3 06-SEP-23 3GXX 1 REMARK
REVDAT 2 13-OCT-21 3GXX 1 SEQADV LINK
REVDAT 1 26-MAY-09 3GXX 0
JRNL AUTH S.DENGL,A.MAYER,M.SUN,P.CRAMER
JRNL TITL STRUCTURE AND IN VIVO REQUIREMENT OF THE YEAST SPT6 SH2
JRNL TITL 2 DOMAIN
JRNL REF J.MOL.BIOL. V. 389 211 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19371747
JRNL DOI 10.1016/J.JMB.2009.04.016
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 18513
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 999
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3146
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 73
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 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): NULL
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3GXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052444.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-07
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 : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97971
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18513
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 45.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.19000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.700
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: PDB ENTRY 3GXW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BICINE PH 8.0, 4,3 M NACL AND 5
REMARK 280 MM TRIS(2-CARBOXYETHYL) PHOSPHINE HYDRO-CHLORIDE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 58.40000
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 29.20000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 1
REMARK 465 LEU A 70
REMARK 465 ALA A 71
REMARK 465 MSE A 72
REMARK 465 LEU A 101
REMARK 465 ASN A 102
REMARK 465 GLU A 103
REMARK 465 GLY B 1
REMARK 465 ASN B 68
REMARK 465 PRO B 69
REMARK 465 LEU B 70
REMARK 465 ALA B 71
REMARK 465 GLU B 103
REMARK 465 GLY C 1
REMARK 465 SER C 2
REMARK 465 HIS C 3
REMARK 465 MSE C 4
REMARK 465 HIS C 5
REMARK 465 ARG C 6
REMARK 465 VAL C 7
REMARK 465 GLY C 41
REMARK 465 ASP C 42
REMARK 465 LEU C 70
REMARK 465 ALA C 71
REMARK 465 MSE C 72
REMARK 465 GLY D 1
REMARK 465 SER D 2
REMARK 465 HIS D 3
REMARK 465 MSE D 4
REMARK 465 HIS D 5
REMARK 465 ARG D 6
REMARK 465 ARG D 40
REMARK 465 GLY D 41
REMARK 465 ASP D 42
REMARK 465 ASP D 43
REMARK 465 LYS D 66
REMARK 465 GLU D 67
REMARK 465 ASN D 68
REMARK 465 PRO D 69
REMARK 465 LEU D 70
REMARK 465 ALA D 71
REMARK 465 MSE D 72
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 OD1 ASP C 32 O HOH C 106 2.11
REMARK 500 O TYR C 13 O HOH C 120 2.18
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 40 N - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 PHE B 16 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 PRO C 69 C - N - CD ANGL. DEV. = -15.7 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 39 43.55 -92.87
REMARK 500 ARG A 40 -62.49 -90.87
REMARK 500 ASP A 52 -175.94 -175.27
REMARK 500 GLU A 67 45.60 -154.36
REMARK 500 GLU A 79 35.31 38.47
REMARK 500 LEU B 100 28.97 -78.52
REMARK 500 LEU B 101 84.82 -158.75
REMARK 500 MSE C 64 129.15 -173.29
REMARK 500 ASN C 68 -168.72 -171.83
REMARK 500 GLU C 79 62.34 64.63
REMARK 500 PRO D 15 47.70 -77.30
REMARK 500 ASP D 52 -173.71 -171.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GXW RELATED DB: PDB
DBREF 3GXX A 5 103 UNP Q6FLB1 SPT6_CANGA 1250 1348
DBREF 3GXX B 5 103 UNP Q6FLB1 SPT6_CANGA 1250 1348
DBREF 3GXX C 5 103 UNP Q6FLB1 SPT6_CANGA 1250 1348
DBREF 3GXX D 5 103 UNP Q6FLB1 SPT6_CANGA 1250 1348
SEQADV 3GXX GLY A 1 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX SER A 2 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX HIS A 3 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX MSE A 4 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX MSE A 64 UNP Q6FLB1 LEU 1309 ENGINEERED MUTATION
SEQADV 3GXX MSE A 72 UNP Q6FLB1 LEU 1317 ENGINEERED MUTATION
SEQADV 3GXX GLY B 1 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX SER B 2 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX HIS B 3 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX MSE B 4 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX MSE B 64 UNP Q6FLB1 LEU 1309 ENGINEERED MUTATION
SEQADV 3GXX MSE B 72 UNP Q6FLB1 LEU 1317 ENGINEERED MUTATION
SEQADV 3GXX GLY C 1 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX SER C 2 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX HIS C 3 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX MSE C 4 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX MSE C 64 UNP Q6FLB1 LEU 1309 ENGINEERED MUTATION
SEQADV 3GXX MSE C 72 UNP Q6FLB1 LEU 1317 ENGINEERED MUTATION
SEQADV 3GXX GLY D 1 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX SER D 2 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX HIS D 3 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX MSE D 4 UNP Q6FLB1 EXPRESSION TAG
SEQADV 3GXX MSE D 64 UNP Q6FLB1 LEU 1309 ENGINEERED MUTATION
SEQADV 3GXX MSE D 72 UNP Q6FLB1 LEU 1317 ENGINEERED MUTATION
SEQRES 1 A 103 GLY SER HIS MSE HIS ARG VAL ILE ASN HIS PRO TYR TYR
SEQRES 2 A 103 PHE PRO PHE ASN GLY LYS GLN ALA GLU ASP TYR LEU ARG
SEQRES 3 A 103 SER LYS GLU ARG GLY ASP PHE VAL ILE ARG GLN SER SER
SEQRES 4 A 103 ARG GLY ASP ASP HIS LEU ALA ILE THR TRP LYS LEU ASP
SEQRES 5 A 103 LYS ASP LEU PHE GLN HIS VAL ASP ILE GLN GLU MSE GLU
SEQRES 6 A 103 LYS GLU ASN PRO LEU ALA MSE GLY LYS VAL LEU VAL VAL
SEQRES 7 A 103 GLU GLY GLN ARG TYR HIS ASP LEU ASP GLN ILE ILE VAL
SEQRES 8 A 103 GLU TYR LEU GLN ASN LYS ILE ARG LEU LEU ASN GLU
SEQRES 1 B 103 GLY SER HIS MSE HIS ARG VAL ILE ASN HIS PRO TYR TYR
SEQRES 2 B 103 PHE PRO PHE ASN GLY LYS GLN ALA GLU ASP TYR LEU ARG
SEQRES 3 B 103 SER LYS GLU ARG GLY ASP PHE VAL ILE ARG GLN SER SER
SEQRES 4 B 103 ARG GLY ASP ASP HIS LEU ALA ILE THR TRP LYS LEU ASP
SEQRES 5 B 103 LYS ASP LEU PHE GLN HIS VAL ASP ILE GLN GLU MSE GLU
SEQRES 6 B 103 LYS GLU ASN PRO LEU ALA MSE GLY LYS VAL LEU VAL VAL
SEQRES 7 B 103 GLU GLY GLN ARG TYR HIS ASP LEU ASP GLN ILE ILE VAL
SEQRES 8 B 103 GLU TYR LEU GLN ASN LYS ILE ARG LEU LEU ASN GLU
SEQRES 1 C 103 GLY SER HIS MSE HIS ARG VAL ILE ASN HIS PRO TYR TYR
SEQRES 2 C 103 PHE PRO PHE ASN GLY LYS GLN ALA GLU ASP TYR LEU ARG
SEQRES 3 C 103 SER LYS GLU ARG GLY ASP PHE VAL ILE ARG GLN SER SER
SEQRES 4 C 103 ARG GLY ASP ASP HIS LEU ALA ILE THR TRP LYS LEU ASP
SEQRES 5 C 103 LYS ASP LEU PHE GLN HIS VAL ASP ILE GLN GLU MSE GLU
SEQRES 6 C 103 LYS GLU ASN PRO LEU ALA MSE GLY LYS VAL LEU VAL VAL
SEQRES 7 C 103 GLU GLY GLN ARG TYR HIS ASP LEU ASP GLN ILE ILE VAL
SEQRES 8 C 103 GLU TYR LEU GLN ASN LYS ILE ARG LEU LEU ASN GLU
SEQRES 1 D 103 GLY SER HIS MSE HIS ARG VAL ILE ASN HIS PRO TYR TYR
SEQRES 2 D 103 PHE PRO PHE ASN GLY LYS GLN ALA GLU ASP TYR LEU ARG
SEQRES 3 D 103 SER LYS GLU ARG GLY ASP PHE VAL ILE ARG GLN SER SER
SEQRES 4 D 103 ARG GLY ASP ASP HIS LEU ALA ILE THR TRP LYS LEU ASP
SEQRES 5 D 103 LYS ASP LEU PHE GLN HIS VAL ASP ILE GLN GLU MSE GLU
SEQRES 6 D 103 LYS GLU ASN PRO LEU ALA MSE GLY LYS VAL LEU VAL VAL
SEQRES 7 D 103 GLU GLY GLN ARG TYR HIS ASP LEU ASP GLN ILE ILE VAL
SEQRES 8 D 103 GLU TYR LEU GLN ASN LYS ILE ARG LEU LEU ASN GLU
MODRES 3GXX MSE A 4 MET SELENOMETHIONINE
MODRES 3GXX MSE A 64 MET SELENOMETHIONINE
MODRES 3GXX MSE B 4 MET SELENOMETHIONINE
MODRES 3GXX MSE B 64 MET SELENOMETHIONINE
MODRES 3GXX MSE B 72 MET SELENOMETHIONINE
MODRES 3GXX MSE C 64 MET SELENOMETHIONINE
MODRES 3GXX MSE D 64 MET SELENOMETHIONINE
HET MSE A 4 8
HET MSE A 64 8
HET MSE B 4 8
HET MSE B 64 8
HET MSE B 72 8
HET MSE C 64 8
HET MSE D 64 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 5 HOH *73(H2 O)
HELIX 1 1 SER A 2 ASN A 9 1 8
HELIX 2 2 ASN A 17 SER A 27 1 11
HELIX 3 3 ASP A 85 ARG A 99 1 15
HELIX 4 4 HIS B 3 ASN B 9 1 7
HELIX 5 5 ASN B 17 ARG B 26 1 10
HELIX 6 6 ASP B 85 LEU B 100 1 16
HELIX 7 7 ASN C 17 SER C 27 1 11
HELIX 8 8 ASP C 85 ASN C 102 1 18
HELIX 9 9 ASN D 17 SER D 27 1 11
HELIX 10 10 ASP D 85 GLU D 103 1 19
SHEET 1 A 5 PHE A 33 GLN A 37 0
SHEET 2 A 5 LEU A 45 ASP A 52 -1 O ALA A 46 N ARG A 36
SHEET 3 A 5 LEU A 55 GLU A 65 -1 O VAL A 59 N ILE A 47
SHEET 4 A 5 LYS A 74 VAL A 78 -1 O VAL A 75 N MSE A 64
SHEET 5 A 5 GLN A 81 TYR A 83 -1 O TYR A 83 N LEU A 76
SHEET 1 B 5 PHE B 33 GLN B 37 0
SHEET 2 B 5 LEU B 45 ASP B 52 -1 O ALA B 46 N ARG B 36
SHEET 3 B 5 LEU B 55 MSE B 64 -1 O VAL B 59 N ILE B 47
SHEET 4 B 5 VAL B 75 VAL B 77 -1 O VAL B 77 N GLN B 62
SHEET 5 B 5 ARG B 82 TYR B 83 -1 O TYR B 83 N LEU B 76
SHEET 1 C 6 TYR C 13 PHE C 14 0
SHEET 2 C 6 PHE C 33 GLN C 37 1 O ILE C 35 N PHE C 14
SHEET 3 C 6 LEU C 45 ASP C 52 -1 O THR C 48 N VAL C 34
SHEET 4 C 6 LEU C 55 MSE C 64 -1 O VAL C 59 N ILE C 47
SHEET 5 C 6 VAL C 75 VAL C 77 -1 O VAL C 77 N GLN C 62
SHEET 6 C 6 ARG C 82 TYR C 83 -1 O TYR C 83 N LEU C 76
SHEET 1 D 5 PHE D 33 GLN D 37 0
SHEET 2 D 5 LEU D 45 ASP D 52 -1 O ALA D 46 N ARG D 36
SHEET 3 D 5 LEU D 55 GLU D 63 -1 O LEU D 55 N LEU D 51
SHEET 4 D 5 LEU D 76 VAL D 78 -1 O VAL D 77 N GLN D 62
SHEET 5 D 5 GLN D 81 TYR D 83 -1 O GLN D 81 N VAL D 78
LINK C HIS A 3 N MSE A 4 1555 1555 1.34
LINK C MSE A 4 N HIS A 5 1555 1555 1.32
LINK C GLU A 63 N MSE A 64 1555 1555 1.33
LINK C MSE A 64 N GLU A 65 1555 1555 1.34
LINK C HIS B 3 N MSE B 4 1555 1555 1.33
LINK C MSE B 4 N HIS B 5 1555 1555 1.33
LINK C GLU B 63 N MSE B 64 1555 1555 1.33
LINK C MSE B 64 N GLU B 65 1555 1555 1.33
LINK C MSE B 72 N GLY B 73 1555 1555 1.34
LINK C GLU C 63 N MSE C 64 1555 1555 1.33
LINK C MSE C 64 N GLU C 65 1555 1555 1.33
LINK C GLU D 63 N MSE D 64 1555 1555 1.33
LINK C MSE D 64 N GLU D 65 1555 1555 1.33
CISPEP 1 ARG A 40 GLY A 41 0 -22.54
CISPEP 2 GLY A 41 ASP A 42 0 12.93
CISPEP 3 LEU B 101 ASN B 102 0 -0.02
CISPEP 4 ILE C 8 ASN C 9 0 -3.95
CRYST1 71.600 71.600 87.600 90.00 90.00 120.00 P 32 12
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 0.013966 0.008064 0.000000 0.00000
SCALE2 0.000000 0.016127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011416 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
