HEADER CHAPERONE 04-DEC-15 5F5R
TITLE TRAP1N-ADPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 60-294;
COMPND 5 SYNONYM: HSP 75,TNFR-ASSOCIATED PROTEIN 1,TUMOR NECROSIS FACTOR TYPE
COMPND 6 1 RECEPTOR-ASSOCIATED PROTEIN,TRAP-1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TRAP1, HSP75;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTYB12
KEYWDS CHAPERONE, ATPASE, GHKL ATPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.T.F.TSAI,S.LEE,N.SUNG,J.LEE,C.CHANG,A.JOACHIMIAK
REVDAT 6 27-SEP-23 5F5R 1 LINK
REVDAT 5 25-DEC-19 5F5R 1 REMARK
REVDAT 4 13-SEP-17 5F5R 1 JRNL REMARK
REVDAT 3 22-JUN-16 5F5R 1 JRNL
REVDAT 2 23-MAR-16 5F5R 1 JRNL
REVDAT 1 02-MAR-16 5F5R 0
JRNL AUTH N.SUNG,J.LEE,J.H.KIM,C.CHANG,A.JOACHIMIAK,S.LEE,F.T.TSAI
JRNL TITL MITOCHONDRIAL HSP90 IS A LIGAND-ACTIVATED MOLECULAR
JRNL TITL 2 CHAPERONE COUPLING ATP BINDING TO DIMER CLOSURE THROUGH A
JRNL TITL 3 COILED-COIL INTERMEDIATE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 2952 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 26929380
JRNL DOI 10.1073/PNAS.1516167113
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 54569
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 + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2899
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3803
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 198
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3443
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 508
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.104
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.623
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3560 ; 0.003 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4807 ; 0.656 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 444 ; 8.477 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;35.477 ;24.211
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 633 ;14.973 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;17.116 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 548 ; 0.048 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2592 ; 0.023 ; 0.020
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): 2207 ; 2.072 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3542 ; 3.337 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1353 ; 5.051 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1265 ; 7.861 ; 4.500
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 70 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6152 55.7017 67.8599
REMARK 3 T TENSOR
REMARK 3 T11: 0.1270 T22: 0.1251
REMARK 3 T33: 0.1102 T12: 0.0337
REMARK 3 T13: 0.1128 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 1.1525 L22: 2.8090
REMARK 3 L33: 1.2776 L12: 0.9578
REMARK 3 L13: 0.3595 L23: -0.2533
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: 0.1854 S13: 0.0670
REMARK 3 S21: -0.3726 S22: -0.0751 S23: -0.2397
REMARK 3 S31: 0.0127 S32: 0.2067 S33: 0.0785
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 70 B 294
REMARK 3 ORIGIN FOR THE GROUP (A): -52.4450 15.6452 64.9082
REMARK 3 T TENSOR
REMARK 3 T11: 0.0470 T22: 0.0929
REMARK 3 T33: 0.0662 T12: -0.0059
REMARK 3 T13: -0.0400 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 1.0254 L22: 1.7167
REMARK 3 L33: 1.3488 L12: 0.4577
REMARK 3 L13: -0.1028 L23: 0.3757
REMARK 3 S TENSOR
REMARK 3 S11: -0.0428 S12: 0.1935 S13: -0.1230
REMARK 3 S21: -0.2101 S22: 0.0336 S23: 0.0759
REMARK 3 S31: -0.0380 S32: -0.1251 S33: 0.0092
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5F5R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000215730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : NULL
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) : 0.97926
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54569
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 29.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
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) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.52700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2CG9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE PH 5.6, 22%
REMARK 280 PEG4000, 5% ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 51.50550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.50550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 46.28500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.58400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.28500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.58400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 51.50550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.28500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.58400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 51.50550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.28500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 71.58400
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 A 506 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 590 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 521 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 589 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 652 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 ALA A 57
REMARK 465 GLY A 58
REMARK 465 HIS A 59
REMARK 465 SER A 60
REMARK 465 THR A 61
REMARK 465 GLN A 62
REMARK 465 THR A 63
REMARK 465 ALA A 64
REMARK 465 GLU A 65
REMARK 465 ASP A 66
REMARK 465 LYS A 67
REMARK 465 GLU A 68
REMARK 465 GLU A 69
REMARK 465 ALA B 57
REMARK 465 GLY B 58
REMARK 465 HIS B 59
REMARK 465 SER B 60
REMARK 465 THR B 61
REMARK 465 GLN B 62
REMARK 465 THR B 63
REMARK 465 ALA B 64
REMARK 465 GLU B 65
REMARK 465 ASP B 66
REMARK 465 LYS B 67
REMARK 465 GLU B 68
REMARK 465 GLU B 69
REMARK 465 ASP B 134
REMARK 465 GLY B 135
REMARK 465 GLN B 136
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 442 O HOH A 452 1.93
REMARK 500 O HOH B 609 O HOH B 615 1.93
REMARK 500 O PHE A 90 NZ LYS A 95 1.93
REMARK 500 OE1 GLN A 200 O HOH A 401 2.06
REMARK 500 O HOH B 522 O HOH B 654 2.07
REMARK 500 O HOH B 639 O HOH B 674 2.07
REMARK 500 O HOH B 403 O HOH B 590 2.08
REMARK 500 O HOH A 430 O HOH A 595 2.16
REMARK 500 O ASN B 189 O HOH B 401 2.16
REMARK 500 O HOH A 460 O HOH A 508 2.16
REMARK 500 O HOH B 438 O HOH B 573 2.17
REMARK 500 OE2 GLU A 267 O HOH A 402 2.19
REMARK 500 O HOH B 579 O HOH B 587 2.19
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 B 644 O HOH B 644 3456 1.64
REMARK 500 O HOH A 440 O HOH B 401 5555 2.01
REMARK 500 O HOH A 599 O HOH A 599 3456 2.03
REMARK 500 O HOH A 568 O HOH B 679 5555 2.18
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 108 56.71 -91.55
REMARK 500 ILE A 175 53.79 -114.79
REMARK 500 ASN A 189 45.20 -101.99
REMARK 500 GLU B 108 55.29 -91.52
REMARK 500 ILE B 175 73.31 -107.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 135 GLN A 136 -147.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 177 0.22 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 119 OD1
REMARK 620 2 ANP A 300 O1G 172.4
REMARK 620 3 ANP A 300 O1B 91.4 88.5
REMARK 620 4 ANP A 300 O2A 87.1 100.5 87.1
REMARK 620 5 HOH A 443 O 86.6 94.1 175.4 88.7
REMARK 620 6 HOH A 458 O 81.6 90.8 92.4 168.7 91.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 119 OD1
REMARK 620 2 ANP B 300 O1G 173.7
REMARK 620 3 ANP B 300 O1B 92.9 85.9
REMARK 620 4 ANP B 300 O2A 88.7 97.4 86.8
REMARK 620 5 HOH B 469 O 82.9 90.9 93.1 171.6
REMARK 620 6 HOH B 513 O 87.2 94.4 176.0 89.2 90.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5F3K RELATED DB: PDB
REMARK 900 5F3K CONTAINS THE SAME PROTEIN WITHOUT LIGAND BINDING
DBREF 5F5R A 60 294 UNP Q12931 TRAP1_HUMAN 60 294
DBREF 5F5R B 60 294 UNP Q12931 TRAP1_HUMAN 60 294
SEQADV 5F5R ALA A 57 UNP Q12931 EXPRESSION TAG
SEQADV 5F5R GLY A 58 UNP Q12931 EXPRESSION TAG
SEQADV 5F5R HIS A 59 UNP Q12931 EXPRESSION TAG
SEQADV 5F5R ALA B 57 UNP Q12931 EXPRESSION TAG
SEQADV 5F5R GLY B 58 UNP Q12931 EXPRESSION TAG
SEQADV 5F5R HIS B 59 UNP Q12931 EXPRESSION TAG
SEQRES 1 A 238 ALA GLY HIS SER THR GLN THR ALA GLU ASP LYS GLU GLU
SEQRES 2 A 238 PRO LEU HIS SER ILE ILE SER SER THR GLU SER VAL GLN
SEQRES 3 A 238 GLY SER THR SER LYS HIS GLU PHE GLN ALA GLU THR LYS
SEQRES 4 A 238 LYS LEU LEU ASP ILE VAL ALA ARG SER LEU TYR SER GLU
SEQRES 5 A 238 LYS GLU VAL PHE ILE ARG GLU LEU ILE SER ASN ALA SER
SEQRES 6 A 238 ASP ALA LEU GLU LYS LEU ARG HIS LYS LEU VAL SER ASP
SEQRES 7 A 238 GLY GLN ALA LEU PRO GLU MET GLU ILE HIS LEU GLN THR
SEQRES 8 A 238 ASN ALA GLU LYS GLY THR ILE THR ILE GLN ASP THR GLY
SEQRES 9 A 238 ILE GLY MET THR GLN GLU GLU LEU VAL SER ASN LEU GLY
SEQRES 10 A 238 THR ILE ALA ARG SER GLY SER LYS ALA PHE LEU ASP ALA
SEQRES 11 A 238 LEU GLN ASN GLN ALA GLU ALA SER SER LYS ILE ILE GLY
SEQRES 12 A 238 GLN PHE GLY VAL GLY PHE TYR SER ALA PHE MET VAL ALA
SEQRES 13 A 238 ASP ARG VAL GLU VAL TYR SER ARG SER ALA ALA PRO GLY
SEQRES 14 A 238 SER LEU GLY TYR GLN TRP LEU SER ASP GLY SER GLY VAL
SEQRES 15 A 238 PHE GLU ILE ALA GLU ALA SER GLY VAL ARG THR GLY THR
SEQRES 16 A 238 LYS ILE ILE ILE HIS LEU LYS SER ASP CYS LYS GLU PHE
SEQRES 17 A 238 SER SER GLU ALA ARG VAL ARG ASP VAL VAL THR LYS TYR
SEQRES 18 A 238 SER ASN PHE VAL SER PHE PRO LEU TYR LEU ASN GLY ARG
SEQRES 19 A 238 ARG MET ASN THR
SEQRES 1 B 238 ALA GLY HIS SER THR GLN THR ALA GLU ASP LYS GLU GLU
SEQRES 2 B 238 PRO LEU HIS SER ILE ILE SER SER THR GLU SER VAL GLN
SEQRES 3 B 238 GLY SER THR SER LYS HIS GLU PHE GLN ALA GLU THR LYS
SEQRES 4 B 238 LYS LEU LEU ASP ILE VAL ALA ARG SER LEU TYR SER GLU
SEQRES 5 B 238 LYS GLU VAL PHE ILE ARG GLU LEU ILE SER ASN ALA SER
SEQRES 6 B 238 ASP ALA LEU GLU LYS LEU ARG HIS LYS LEU VAL SER ASP
SEQRES 7 B 238 GLY GLN ALA LEU PRO GLU MET GLU ILE HIS LEU GLN THR
SEQRES 8 B 238 ASN ALA GLU LYS GLY THR ILE THR ILE GLN ASP THR GLY
SEQRES 9 B 238 ILE GLY MET THR GLN GLU GLU LEU VAL SER ASN LEU GLY
SEQRES 10 B 238 THR ILE ALA ARG SER GLY SER LYS ALA PHE LEU ASP ALA
SEQRES 11 B 238 LEU GLN ASN GLN ALA GLU ALA SER SER LYS ILE ILE GLY
SEQRES 12 B 238 GLN PHE GLY VAL GLY PHE TYR SER ALA PHE MET VAL ALA
SEQRES 13 B 238 ASP ARG VAL GLU VAL TYR SER ARG SER ALA ALA PRO GLY
SEQRES 14 B 238 SER LEU GLY TYR GLN TRP LEU SER ASP GLY SER GLY VAL
SEQRES 15 B 238 PHE GLU ILE ALA GLU ALA SER GLY VAL ARG THR GLY THR
SEQRES 16 B 238 LYS ILE ILE ILE HIS LEU LYS SER ASP CYS LYS GLU PHE
SEQRES 17 B 238 SER SER GLU ALA ARG VAL ARG ASP VAL VAL THR LYS TYR
SEQRES 18 B 238 SER ASN PHE VAL SER PHE PRO LEU TYR LEU ASN GLY ARG
SEQRES 19 B 238 ARG MET ASN THR
HET ANP A 300 31
HET MG A 301 1
HET ANP B 300 31
HET MG B 301 1
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 3 ANP 2(C10 H17 N6 O12 P3)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *508(H2 O)
HELIX 1 AA1 GLN A 91 SER A 104 1 14
HELIX 2 AA2 GLU A 110 HIS A 129 1 20
HELIX 3 AA3 THR A 164 LEU A 172 1 9
HELIX 4 AA4 ARG A 177 ASN A 189 1 13
HELIX 5 AA5 ALA A 193 GLY A 202 1 10
HELIX 6 AA6 VAL A 203 MET A 210 5 8
HELIX 7 AA7 SER A 259 SER A 265 5 7
HELIX 8 AA8 SER A 266 THR A 275 1 10
HELIX 9 AA9 LYS A 276 VAL A 281 5 6
HELIX 10 AB1 GLN B 91 SER B 104 1 14
HELIX 11 AB2 GLU B 110 HIS B 129 1 20
HELIX 12 AB3 THR B 164 LEU B 172 1 9
HELIX 13 AB4 ARG B 177 GLN B 190 1 14
HELIX 14 AB5 ALA B 193 GLY B 202 1 10
HELIX 15 AB6 VAL B 203 MET B 210 5 8
HELIX 16 AB7 SER B 259 SER B 265 5 7
HELIX 17 AB8 SER B 266 THR B 275 1 10
HELIX 18 AB9 LYS B 276 VAL B 281 5 6
SHEET 1 AA1 9 SER A 80 GLU A 89 0
SHEET 2 AA1 9 VAL A 238 SER A 245 -1 O SER A 245 N SER A 80
SHEET 3 AA1 9 GLY A 228 SER A 233 -1 N GLN A 230 O ALA A 242
SHEET 4 AA1 9 ALA A 212 ARG A 220 -1 N VAL A 217 O TRP A 231
SHEET 5 AA1 9 GLY A 250 LEU A 257 -1 O ILE A 254 N GLU A 216
SHEET 6 AA1 9 THR A 153 ASP A 158 -1 N ILE A 156 O ILE A 253
SHEET 7 AA1 9 ILE A 143 ASN A 148 -1 N HIS A 144 O GLN A 157
SHEET 8 AA1 9 LEU A 285 LEU A 287 1 O TYR A 286 N ILE A 143
SHEET 9 AA1 9 ARG A 290 ARG A 291 -1 O ARG A 290 N LEU A 287
SHEET 1 AA2 9 SER B 80 GLU B 89 0
SHEET 2 AA2 9 VAL B 238 SER B 245 -1 O ILE B 241 N SER B 86
SHEET 3 AA2 9 GLY B 228 SER B 233 -1 N GLN B 230 O ALA B 242
SHEET 4 AA2 9 ALA B 212 ARG B 220 -1 N VAL B 217 O TRP B 231
SHEET 5 AA2 9 GLY B 250 LEU B 257 -1 O ILE B 254 N GLU B 216
SHEET 6 AA2 9 THR B 153 ASP B 158 -1 N ILE B 156 O ILE B 253
SHEET 7 AA2 9 ILE B 143 ASN B 148 -1 N HIS B 144 O GLN B 157
SHEET 8 AA2 9 LEU B 285 LEU B 287 1 O TYR B 286 N LEU B 145
SHEET 9 AA2 9 ARG B 290 ARG B 291 -1 O ARG B 290 N LEU B 287
LINK OD1 ASN A 119 MG MG A 301 1555 1555 2.01
LINK O1G ANP A 300 MG MG A 301 1555 1555 2.02
LINK O1B ANP A 300 MG MG A 301 1555 1555 2.06
LINK O2A ANP A 300 MG MG A 301 1555 1555 2.01
LINK MG MG A 301 O HOH A 443 1555 1555 2.16
LINK MG MG A 301 O HOH A 458 1555 1555 2.15
LINK OD1 ASN B 119 MG MG B 301 1555 1555 1.98
LINK O1G ANP B 300 MG MG B 301 1555 1555 2.03
LINK O1B ANP B 300 MG MG B 301 1555 1555 2.04
LINK O2A ANP B 300 MG MG B 301 1555 1555 2.02
LINK MG MG B 301 O HOH B 469 1555 1555 2.08
LINK MG MG B 301 O HOH B 513 1555 1555 2.12
SITE 1 AC1 29 ASN A 119 ALA A 123 LYS A 126 ASP A 158
SITE 2 AC1 29 MET A 163 ASN A 171 ARG A 177 GLY A 204
SITE 3 AC1 29 PHE A 205 THR A 251 MG A 301 HOH A 422
SITE 4 AC1 29 HOH A 424 HOH A 429 HOH A 430 HOH A 431
SITE 5 AC1 29 HOH A 433 HOH A 442 HOH A 443 HOH A 447
SITE 6 AC1 29 HOH A 455 HOH A 458 HOH A 468 HOH A 471
SITE 7 AC1 29 HOH A 474 HOH A 478 HOH A 492 HOH A 498
SITE 8 AC1 29 HOH A 523
SITE 1 AC2 4 ASN A 119 ANP A 300 HOH A 443 HOH A 458
SITE 1 AC3 28 ASN B 119 ALA B 123 LYS B 126 ASP B 158
SITE 2 AC3 28 MET B 163 ASN B 171 ARG B 177 GLY B 204
SITE 3 AC3 28 PHE B 205 THR B 251 MG B 301 HOH B 427
SITE 4 AC3 28 HOH B 431 HOH B 440 HOH B 442 HOH B 444
SITE 5 AC3 28 HOH B 449 HOH B 453 HOH B 462 HOH B 469
SITE 6 AC3 28 HOH B 483 HOH B 485 HOH B 496 HOH B 513
SITE 7 AC3 28 HOH B 522 HOH B 533 HOH B 552 HOH B 554
SITE 1 AC4 4 ASN B 119 ANP B 300 HOH B 469 HOH B 513
CRYST1 92.570 143.168 103.011 90.00 90.00 90.00 C 2 2 21 16
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 0.010803 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009708 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
