HEADER ISOMERASE 14-JAN-02 1KT1
TITLE STRUCTURE OF THE LARGE FKBP-LIKE PROTEIN, FKBP51, INVOLVED IN STEROID
TITLE 2 RECEPTOR COMPLEXES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FK506-BINDING PROTEIN FKBP51;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.2.1.8;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SAIMIRI BOLIVIENSIS;
SOURCE 3 ORGANISM_COMMON: BOLIVIAN SQUIRREL MONKEY;
SOURCE 4 ORGANISM_TAXID: 27679;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS FKBP-LIKE PPIASE, TPR REPEATS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.SINARS,J.CHEUNG-FLYNN,R.A.RIMERMAN,J.G.SCAMMELL,D.F.SMITH,
AUTHOR 2 J.C.CLARDY
REVDAT 3 14-FEB-24 1KT1 1 REMARK
REVDAT 2 24-FEB-09 1KT1 1 VERSN
REVDAT 1 04-FEB-03 1KT1 0
JRNL AUTH C.R.SINARS,J.CHEUNG-FLYNN,R.A.RIMERMAN,J.G.SCAMMELL,
JRNL AUTH 2 D.F.SMITH,J.C.CLARDY
JRNL TITL STRUCTURE OF THE LARGE FK506-BINDING PROTEIN FKBP51, AN
JRNL TITL 2 HSP90-BINDING PROTEIN AND A COMPONENT OF STEROID RECEPTOR
JRNL TITL 3 COMPLEXES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 868 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 12538866
JRNL DOI 10.1073/PNAS.0231020100
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1287156.860
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 16179
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.314
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 812
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2525
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE : 0.4220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2961
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 31
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 13.07000
REMARK 3 B22 (A**2) : 13.07000
REMARK 3 B33 (A**2) : -26.15000
REMARK 3 B12 (A**2) : 11.28000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.34
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.54
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.600 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.520 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.390 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.350 ; 4.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 69.49
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015311.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9251
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16210
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEGMME 5000, AMMONIUM SULFATE, PH 5.8,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 88.43200
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 44.21600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.21600
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 88.43200
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 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 THR A 3
REMARK 465 ASP A 4
REMARK 465 GLU A 5
REMARK 465 GLY A 6
REMARK 465 ALA A 7
REMARK 465 LYS A 8
REMARK 465 ASN A 9
REMARK 465 SER A 10
REMARK 465 ARG A 11
REMARK 465 GLY A 12
REMARK 465 ASN A 13
REMARK 465 PRO A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 THR A 17
REMARK 465 VAL A 18
REMARK 465 ALA A 19
REMARK 465 GLU A 20
REMARK 465 GLN A 21
REMARK 465 GLY A 22
REMARK 465 GLU A 23
REMARK 465 ASP A 24
REMARK 465 VAL A 25
REMARK 465 THR A 26
REMARK 465 SER A 27
REMARK 465 LYS A 38
REMARK 465 ARG A 39
REMARK 465 VAL A 40
REMARK 465 GLY A 41
REMARK 465 GLY A 64
REMARK 465 LYS A 65
REMARK 465 LYS A 66
REMARK 465 PHE A 67
REMARK 465 ASP A 68
REMARK 465 SER A 69
REMARK 465 SER A 70
REMARK 465 HIS A 71
REMARK 465 ASP A 72
REMARK 465 ARG A 73
REMARK 465 ASN A 74
REMARK 465 GLU A 75
REMARK 465 LYS A 108
REMARK 465 PRO A 109
REMARK 465 GLU A 110
REMARK 465 TYR A 111
REMARK 465 LYS A 422
REMARK 465 GLU A 423
REMARK 465 GLU A 424
REMARK 465 ALA A 425
REMARK 465 ASN A 426
REMARK 465 LYS A 427
REMARK 465 ALA A 428
REMARK 465 MET A 429
REMARK 465 SER A 430
REMARK 465 LYS A 431
REMARK 465 LYS A 432
REMARK 465 THR A 433
REMARK 465 SER A 434
REMARK 465 GLU A 435
REMARK 465 GLY A 436
REMARK 465 VAL A 437
REMARK 465 THR A 438
REMARK 465 ASN A 439
REMARK 465 GLU A 440
REMARK 465 LYS A 441
REMARK 465 LEU A 442
REMARK 465 THR A 443
REMARK 465 ALA A 444
REMARK 465 SER A 445
REMARK 465 HIS A 446
REMARK 465 ALA A 447
REMARK 465 VAL A 448
REMARK 465 GLU A 449
REMARK 465 GLU A 450
REMARK 465 GLU A 451
REMARK 465 LYS A 452
REMARK 465 PRO A 453
REMARK 465 GLU A 454
REMARK 465 GLY A 455
REMARK 465 HIS A 456
REMARK 465 VAL A 457
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 THR A 116 OG1 CG2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 28 CG CD CE NZ
REMARK 480 LYS A 29 CG CD CE NZ
REMARK 480 LYS A 35 CG CD CE NZ
REMARK 480 GLU A 44 CG CD OE1 OE2
REMARK 480 LYS A 60 CG CD CE NZ
REMARK 480 LYS A 88 CG CD CE NZ
REMARK 480 LYS A 121 CG CD CE NZ
REMARK 480 GLU A 131 CG CD OE1 OE2
REMARK 480 ARG A 154 CG CD NE CZ NH1 NH2
REMARK 480 ARG A 222 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 251 CG CD OE1 OE2
REMARK 480 GLU A 306 CG CD OE1 OE2
REMARK 480 LYS A 385 CG CD CE NZ
REMARK 480 GLN A 395 CD OE1 NE2
REMARK 480 LYS A 399 CG CD CE NZ
REMARK 480 GLU A 403 CG CD OE1 OE2
REMARK 480 LYS A 414 CG CD CE NZ
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 OE1 GLU A 44 CD2 LEU A 346 2664 2.12
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 LYS A 29 CB LYS A 29 CG 0.241
REMARK 500 GLU A 44 CB GLU A 44 CG 0.119
REMARK 500 LYS A 88 CB LYS A 88 CG 0.258
REMARK 500 GLU A 131 CB GLU A 131 CG -0.364
REMARK 500 GLU A 251 CB GLU A 251 CG -0.126
REMARK 500 GLN A 395 CG GLN A 395 CD -0.366
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 LYS A 28 CA - CB - CG ANGL. DEV. = 32.5 DEGREES
REMARK 500 LYS A 28 CB - CG - CD ANGL. DEV. = 17.4 DEGREES
REMARK 500 ALA A 62 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 GLU A 251 CA - CB - CG ANGL. DEV. = 13.5 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 LYS A 29 -29.54 -32.16
REMARK 500 ARG A 31 37.12 -61.63
REMARK 500 GLU A 44 31.29 -83.67
REMARK 500 PRO A 47 131.60 -38.01
REMARK 500 ILE A 49 136.77 -38.38
REMARK 500 ASN A 58 131.20 -172.56
REMARK 500 LYS A 60 102.38 -174.10
REMARK 500 LEU A 61 -104.93 -52.51
REMARK 500 ILE A 87 155.82 -41.09
REMARK 500 THR A 96 -14.49 -142.36
REMARK 500 LEU A 119 173.30 -51.72
REMARK 500 PRO A 123 121.86 -27.33
REMARK 500 SER A 124 -118.72 -12.82
REMARK 500 ASN A 125 35.18 -86.25
REMARK 500 ALA A 126 175.44 -47.72
REMARK 500 THR A 127 75.10 -151.58
REMARK 500 GLU A 144 62.85 31.07
REMARK 500 ASP A 145 19.94 -170.74
REMARK 500 ARG A 155 151.33 -36.18
REMARK 500 SER A 256 -39.75 -39.35
REMARK 500 LYS A 283 58.99 -92.20
REMARK 500 GLU A 332 72.84 -109.44
REMARK 500 ASN A 381 84.13 -173.11
REMARK 500 LYS A 385 -77.89 -51.07
REMARK 500 ALA A 387 -74.00 -50.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KT0 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE LARGE FKBP-LIKE PROTEIN, FKBP51, INVOLVED IN
REMARK 900 STEROID RECEPTOR COMPLEXES
DBREF 1KT1 A 1 457 UNP Q9XSH5 FKBP5_SAIBB 1 457
SEQRES 1 A 457 MET THR THR ASP GLU GLY ALA LYS ASN SER ARG GLY ASN
SEQRES 2 A 457 PRO ALA ALA THR VAL ALA GLU GLN GLY GLU ASP VAL THR
SEQRES 3 A 457 SER LYS LYS ASP ARG GLY VAL LEU LYS ILE VAL LYS ARG
SEQRES 4 A 457 VAL GLY HIS GLY GLU GLU THR PRO MET ILE GLY ASP ARG
SEQRES 5 A 457 VAL TYR VAL HIS TYR ASN GLY LYS LEU ALA ASN GLY LYS
SEQRES 6 A 457 LYS PHE ASP SER SER HIS ASP ARG ASN GLU PRO PHE VAL
SEQRES 7 A 457 PHE SER ILE GLY LYS GLY GLN VAL ILE LYS ALA TRP ASP
SEQRES 8 A 457 ILE GLY VAL ALA THR MET LYS LYS GLY GLU ILE CYS HIS
SEQRES 9 A 457 LEU LEU CYS LYS PRO GLU TYR ALA TYR GLY ALA THR GLY
SEQRES 10 A 457 SER LEU PRO LYS ILE PRO SER ASN ALA THR LEU PHE PHE
SEQRES 11 A 457 GLU VAL GLU LEU LEU ASP PHE LYS GLY GLU ASP LEU LEU
SEQRES 12 A 457 GLU ASP GLY GLY ILE ILE ARG ARG THR LYS ARG ARG GLY
SEQRES 13 A 457 GLU GLY TYR SER ASN PRO ASN GLU GLY ALA ARG VAL GLN
SEQRES 14 A 457 ILE HIS LEU GLU GLY ARG CYS GLY GLY ARG VAL PHE ASP
SEQRES 15 A 457 CYS ARG ASP VAL ALA PHE THR VAL GLY GLU GLY GLU ASP
SEQRES 16 A 457 HIS ASP ILE PRO ILE GLY ILE ASP LYS ALA LEU GLU LYS
SEQRES 17 A 457 MET GLN ARG GLU GLU GLN CYS ILE LEU HIS LEU GLY PRO
SEQRES 18 A 457 ARG TYR GLY PHE GLY GLU ALA GLY LYS PRO LYS PHE GLY
SEQRES 19 A 457 ILE GLU PRO ASN ALA GLU LEU ILE TYR GLU VAL THR LEU
SEQRES 20 A 457 LYS SER PHE GLU LYS ALA LYS GLU SER TRP GLU MET ASP
SEQRES 21 A 457 THR LYS GLU LYS LEU GLU GLN ALA ALA ILE VAL LYS GLU
SEQRES 22 A 457 LYS GLY THR VAL TYR PHE LYS GLY GLY LYS TYR VAL GLN
SEQRES 23 A 457 ALA VAL ILE GLN TYR GLY LYS ILE VAL SER TRP LEU GLU
SEQRES 24 A 457 MET GLU TYR GLY LEU SER GLU LYS GLU SER LYS ALA SER
SEQRES 25 A 457 GLU SER PHE LEU LEU ALA ALA PHE LEU ASN LEU ALA MET
SEQRES 26 A 457 CYS TYR LEU LYS LEU ARG GLU TYR THR LYS ALA VAL GLU
SEQRES 27 A 457 CYS CYS ASP LYS ALA LEU GLY LEU ASP SER ALA ASN GLU
SEQRES 28 A 457 LYS GLY LEU TYR ARG ARG GLY GLU ALA GLN LEU LEU MET
SEQRES 29 A 457 ASN GLU PHE GLU SER ALA LYS GLY ASP PHE GLU LYS VAL
SEQRES 30 A 457 LEU GLU VAL ASN PRO GLN ASN LYS ALA ALA ARG LEU GLN
SEQRES 31 A 457 ILE PHE MET CYS GLN LYS LYS ALA LYS GLU HIS ASN GLU
SEQRES 32 A 457 ARG ASP ARG ARG THR TYR ALA ASN MET PHE LYS LYS PHE
SEQRES 33 A 457 ALA GLU GLN ASP ALA LYS GLU GLU ALA ASN LYS ALA MET
SEQRES 34 A 457 SER LYS LYS THR SER GLU GLY VAL THR ASN GLU LYS LEU
SEQRES 35 A 457 THR ALA SER HIS ALA VAL GLU GLU GLU LYS PRO GLU GLY
SEQRES 36 A 457 HIS VAL
HET SO4 A 601 5
HET SO4 A 602 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 HOH *31(H2 O)
HELIX 1 1 ILE A 87 GLY A 93 1 7
HELIX 2 2 GLU A 192 ASP A 197 5 6
HELIX 3 3 PRO A 199 GLU A 207 1 9
HELIX 4 4 PRO A 221 GLY A 224 5 4
HELIX 5 5 GLU A 255 MET A 259 5 5
HELIX 6 6 ASP A 260 GLY A 281 1 22
HELIX 7 7 LYS A 283 GLU A 299 1 17
HELIX 8 8 SER A 305 LEU A 330 1 26
HELIX 9 9 GLU A 332 ASP A 347 1 16
HELIX 10 10 ASN A 350 MET A 364 1 15
HELIX 11 11 GLU A 366 VAL A 380 1 15
HELIX 12 12 ASN A 384 GLU A 418 1 35
SHEET 1 A 5 LEU A 34 ILE A 36 0
SHEET 2 A 5 CYS A 103 LEU A 106 -1 O HIS A 104 N ILE A 36
SHEET 3 A 5 PHE A 129 LYS A 138 -1 O PHE A 130 N LEU A 105
SHEET 4 A 5 ARG A 52 HIS A 56 -1 N ARG A 52 O LYS A 138
SHEET 5 A 5 PHE A 77 SER A 80 -1 O PHE A 79 N VAL A 53
SHEET 1 B 6 GLU A 140 ASP A 141 0
SHEET 2 B 6 ILE A 148 ARG A 154 -1 O ARG A 150 N GLU A 140
SHEET 3 B 6 GLN A 214 LEU A 219 -1 O HIS A 218 N ILE A 149
SHEET 4 B 6 LEU A 241 GLU A 251 -1 O TYR A 243 N LEU A 217
SHEET 5 B 6 ARG A 167 CYS A 176 -1 N ARG A 175 O ILE A 242
SHEET 6 B 6 ARG A 179 THR A 189 -1 O PHE A 181 N GLY A 174
CISPEP 1 LEU A 119 PRO A 120 0 1.30
SITE 1 AC1 3 LYS A 230 PRO A 231 LYS A 232
SITE 1 AC2 3 ARG A 184 VAL A 186 HIS A 196
CRYST1 91.035 91.035 132.648 90.00 90.00 120.00 P 32 2 1 6
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 0.010985 0.006342 0.000000 0.00000
SCALE2 0.000000 0.012684 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007539 0.00000
(ATOM LINES ARE NOT SHOWN.)
END