HEADER TRANSCRIPTION 18-APR-06 2GPP
TITLE ESTROGEN RELATED RECEPTOR-GAMMA LIGAND BINDING DOMAIN COMPLEXED WITH A
TITLE 2 RIP140 PEPTIDE AND SYNTHETIC LIGAND GSK4716
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN-RELATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES (229-458);
COMPND 5 SYNONYM: ESTROGEN RECEPTOR-RELATED PROTEIN 3, ERR GAMMA-2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUCLEAR RECEPTOR-INTERACTING PROTEIN 1;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: RESIDUES (366-390);
COMPND 11 SYNONYM: NUCLEAR FACTOR RIP140, RECEPTOR-INTERACTING PROTEIN 140;
COMPND 12 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: ESRRG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: CHEMICALLY SYNTHESIZED. OCCURS NATURALLY IN HUMANS.
KEYWDS ESTROGEN RELATED RECEPTOR, ERR, ERRG, ESRRG, NUCLEAR RECEPTOR,
KEYWDS 2 STEROID RECEPTOR, RIP140, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR L.WANG,W.J.ZUERCHER,T.G.CONSLER,M.H.LAMBERT,A.B.MILLER,L.A.OSBAND-
AUTHOR 2 MILLER,D.D.MCKEE,T.M.WILLSON,R.T.NOLTE
REVDAT 4 30-AUG-23 2GPP 1 REMARK
REVDAT 3 24-FEB-09 2GPP 1 VERSN
REVDAT 2 30-OCT-07 2GPP 1 JRNL
REVDAT 1 26-SEP-06 2GPP 0
JRNL AUTH L.WANG,W.J.ZUERCHER,T.G.CONSLER,M.H.LAMBERT,A.B.MILLER,
JRNL AUTH 2 L.A.ORBAND-MILLER,D.D.MCKEE,T.M.WILLSON,R.T.NOLTE
JRNL TITL X-RAY CRYSTAL STRUCTURES OF THE ESTROGEN-RELATED
JRNL TITL 2 RECEPTOR-GAMMA LIGAND BINDING DOMAIN IN THREE FUNCTIONAL
JRNL TITL 3 STATES REVEAL THE MOLECULAR BASIS OF SMALL MOLECULE
JRNL TITL 4 REGULATION.
JRNL REF J.BIOL.CHEM. V. 281 37773 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16990259
JRNL DOI 10.1074/JBC.M608410200
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 25065
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 764
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1590
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3745
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 25
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.86000
REMARK 3 B22 (A**2) : -0.86000
REMARK 3 B33 (A**2) : 1.29000
REMARK 3 B12 (A**2) : -0.43000
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): 0.397
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.269
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.198
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.449
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3849 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3619 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5210 ; 1.215 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8455 ; 0.733 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 473 ; 5.576 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;35.503 ;25.849
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 730 ;15.579 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;14.940 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 614 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4176 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 679 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 945 ; 0.230 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3558 ; 0.167 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1914 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2198 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 108 ; 0.149 ; 0.200
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): 6 ; 0.178 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 28 ; 0.198 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.002 ; 0.200
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): 2570 ; 0.609 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 953 ; 0.146 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3843 ; 0.939 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1602 ; 1.222 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1367 ; 1.911 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 233 A 457 5
REMARK 3 1 B 233 B 456 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1316 ; NULL ; NULL
REMARK 3 LOOSE POSITIONAL 1 A (A): 2123 ; NULL ; NULL
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1316 ; NULL ; NULL
REMARK 3 LOOSE THERMAL 1 A (A**2): 2123 ; NULL ; NULL
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 378 C 388 5
REMARK 3 1 D 378 D 390 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 C (A): 65 ; NULL ; NULL
REMARK 3 LOOSE POSITIONAL 2 C (A): 108 ; NULL ; NULL
REMARK 3 MEDIUM THERMAL 2 C (A**2): 65 ; NULL ; NULL
REMARK 3 LOOSE THERMAL 2 C (A**2): 108 ; NULL ; 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 : BABINET MODEL WITH 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 2GPP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25066
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.40300
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: AMORE
REMARK 200 STARTING MODEL: 2GP7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% PEG 20K 0.1M MES BUFFER, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 101.90500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 58.83488
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 17.82000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 101.90500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 58.83488
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.82000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 101.90500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 58.83488
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 17.82000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 117.66976
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 35.64000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 117.66976
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 35.64000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 117.66976
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 35.64000
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 PRO A 229
REMARK 465 ALA A 230
REMARK 465 LYS A 231
REMARK 465 LYS A 232
REMARK 465 VAL A 458
REMARK 465 PRO B 229
REMARK 465 ALA B 230
REMARK 465 LYS B 231
REMARK 465 LYS B 232
REMARK 465 LYS B 457
REMARK 465 VAL B 458
REMARK 465 LEU C 366
REMARK 465 GLU C 367
REMARK 465 ARG C 368
REMARK 465 ASN C 369
REMARK 465 ASN C 370
REMARK 465 ILE C 371
REMARK 465 LYS C 372
REMARK 465 GLN C 373
REMARK 465 ALA C 374
REMARK 465 ALA C 375
REMARK 465 ASN C 376
REMARK 465 ASN C 377
REMARK 465 ILE C 389
REMARK 465 PRO C 390
REMARK 465 LEU D 366
REMARK 465 GLU D 367
REMARK 465 ARG D 368
REMARK 465 ASN D 369
REMARK 465 ASN D 370
REMARK 465 ILE D 371
REMARK 465 LYS D 372
REMARK 465 GLN D 373
REMARK 465 ALA D 374
REMARK 465 ALA D 375
REMARK 465 ASN D 376
REMARK 465 ASN D 377
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 LYS A 338 CD CE NZ
REMARK 470 LYS A 390 CD CE NZ
REMARK 470 LYS A 457 CG CD CE NZ
REMARK 470 LYS C 385 CD CE NZ
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 TYR A 330 86.54 -151.81
REMARK 500 LYS A 363 -52.44 -24.04
REMARK 500 ASN A 376 36.53 -90.74
REMARK 500 ASP B 259 86.82 -61.02
REMARK 500 ASN B 376 34.77 -99.65
REMARK 500 SER C 386 -158.95 -69.23
REMARK 500 GLN C 387 -94.74 -117.91
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 SER C 386 GLN C 387 -144.21
REMARK 500 GLN C 387 THR C 388 -147.94
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 1BA A 459
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GP7 RELATED DB: PDB
REMARK 900 RELATED ID: 2GPO RELATED DB: PDB
REMARK 900 RELATED ID: 2GPU RELATED DB: PDB
REMARK 900 RELATED ID: 2GPV RELATED DB: PDB
DBREF 2GPP A 229 458 UNP P62508 ERR3_HUMAN 229 458
DBREF 2GPP B 229 458 UNP P62508 ERR3_HUMAN 229 458
DBREF 2GPP C 366 390 UNP P48552 NRIP1_HUMAN 366 390
DBREF 2GPP D 366 390 UNP P48552 NRIP1_HUMAN 366 390
SEQRES 1 A 230 PRO ALA LYS LYS PRO TYR ASN LYS ILE VAL SER HIS LEU
SEQRES 2 A 230 LEU VAL ALA GLU PRO GLU LYS ILE TYR ALA MET PRO ASP
SEQRES 3 A 230 PRO THR VAL PRO ASP SER ASP ILE LYS ALA LEU THR THR
SEQRES 4 A 230 LEU CYS ASP LEU ALA ASP ARG GLU LEU VAL VAL ILE ILE
SEQRES 5 A 230 GLY TRP ALA LYS HIS ILE PRO GLY PHE SER THR LEU SER
SEQRES 6 A 230 LEU ALA ASP GLN MET SER LEU LEU GLN SER ALA TRP MET
SEQRES 7 A 230 GLU ILE LEU ILE LEU GLY VAL VAL TYR ARG SER LEU SER
SEQRES 8 A 230 PHE GLU ASP GLU LEU VAL TYR ALA ASP ASP TYR ILE MET
SEQRES 9 A 230 ASP GLU ASP GLN SER LYS LEU ALA GLY LEU LEU ASP LEU
SEQRES 10 A 230 ASN ASN ALA ILE LEU GLN LEU VAL LYS LYS TYR LYS SER
SEQRES 11 A 230 MET LYS LEU GLU LYS GLU GLU PHE VAL THR LEU LYS ALA
SEQRES 12 A 230 ILE ALA LEU ALA ASN SER ASP SER MET HIS ILE GLU ASP
SEQRES 13 A 230 VAL GLU ALA VAL GLN LYS LEU GLN ASP VAL LEU HIS GLU
SEQRES 14 A 230 ALA LEU GLN ASP TYR GLU ALA GLY GLN HIS MET GLU ASP
SEQRES 15 A 230 PRO ARG ARG ALA GLY LYS MET LEU MET THR LEU PRO LEU
SEQRES 16 A 230 LEU ARG GLN THR SER THR LYS ALA VAL GLN HIS PHE TYR
SEQRES 17 A 230 ASN ILE LYS LEU GLU GLY LYS VAL PRO MET HIS LYS LEU
SEQRES 18 A 230 PHE LEU GLU MET LEU GLU ALA LYS VAL
SEQRES 1 B 230 PRO ALA LYS LYS PRO TYR ASN LYS ILE VAL SER HIS LEU
SEQRES 2 B 230 LEU VAL ALA GLU PRO GLU LYS ILE TYR ALA MET PRO ASP
SEQRES 3 B 230 PRO THR VAL PRO ASP SER ASP ILE LYS ALA LEU THR THR
SEQRES 4 B 230 LEU CYS ASP LEU ALA ASP ARG GLU LEU VAL VAL ILE ILE
SEQRES 5 B 230 GLY TRP ALA LYS HIS ILE PRO GLY PHE SER THR LEU SER
SEQRES 6 B 230 LEU ALA ASP GLN MET SER LEU LEU GLN SER ALA TRP MET
SEQRES 7 B 230 GLU ILE LEU ILE LEU GLY VAL VAL TYR ARG SER LEU SER
SEQRES 8 B 230 PHE GLU ASP GLU LEU VAL TYR ALA ASP ASP TYR ILE MET
SEQRES 9 B 230 ASP GLU ASP GLN SER LYS LEU ALA GLY LEU LEU ASP LEU
SEQRES 10 B 230 ASN ASN ALA ILE LEU GLN LEU VAL LYS LYS TYR LYS SER
SEQRES 11 B 230 MET LYS LEU GLU LYS GLU GLU PHE VAL THR LEU LYS ALA
SEQRES 12 B 230 ILE ALA LEU ALA ASN SER ASP SER MET HIS ILE GLU ASP
SEQRES 13 B 230 VAL GLU ALA VAL GLN LYS LEU GLN ASP VAL LEU HIS GLU
SEQRES 14 B 230 ALA LEU GLN ASP TYR GLU ALA GLY GLN HIS MET GLU ASP
SEQRES 15 B 230 PRO ARG ARG ALA GLY LYS MET LEU MET THR LEU PRO LEU
SEQRES 16 B 230 LEU ARG GLN THR SER THR LYS ALA VAL GLN HIS PHE TYR
SEQRES 17 B 230 ASN ILE LYS LEU GLU GLY LYS VAL PRO MET HIS LYS LEU
SEQRES 18 B 230 PHE LEU GLU MET LEU GLU ALA LYS VAL
SEQRES 1 C 25 LEU GLU ARG ASN ASN ILE LYS GLN ALA ALA ASN ASN SER
SEQRES 2 C 25 LEU LEU LEU HIS LEU LEU LYS SER GLN THR ILE PRO
SEQRES 1 D 25 LEU GLU ARG ASN ASN ILE LYS GLN ALA ALA ASN ASN SER
SEQRES 2 D 25 LEU LEU LEU HIS LEU LEU LYS SER GLN THR ILE PRO
HET 1BA A 459 21
HETNAM 1BA 4-HYDROXY-N'-(4-ISOPROPYLBENZYL)BENZOHYDRAZIDE
FORMUL 5 1BA C17 H20 N2 O2
FORMUL 6 HOH *25(H2 O)
HELIX 1 1 ASN A 235 LEU A 242 1 8
HELIX 2 2 SER A 260 HIS A 285 1 26
HELIX 3 3 SER A 293 SER A 317 1 25
HELIX 4 4 ASP A 333 GLY A 341 1 9
HELIX 5 5 LEU A 342 MET A 359 1 18
HELIX 6 6 GLU A 362 ASN A 376 1 15
HELIX 7 7 ASP A 384 HIS A 407 1 24
HELIX 8 8 ARG A 412 MET A 419 1 8
HELIX 9 9 THR A 420 GLY A 442 1 23
HELIX 10 10 HIS A 447 GLU A 455 1 9
HELIX 11 11 ASN B 235 GLU B 245 1 11
HELIX 12 12 SER B 260 HIS B 285 1 26
HELIX 13 13 SER B 293 SER B 317 1 25
HELIX 14 14 LEU B 318 PHE B 320 5 3
HELIX 15 15 GLU B 334 GLY B 341 1 8
HELIX 16 16 LEU B 342 LYS B 360 1 19
HELIX 17 17 GLU B 362 ASN B 376 1 15
HELIX 18 18 ASP B 384 HIS B 407 1 24
HELIX 19 19 ARG B 412 MET B 419 1 8
HELIX 20 20 THR B 420 GLY B 442 1 23
HELIX 21 21 HIS B 447 GLU B 455 1 9
HELIX 22 22 SER C 378 SER C 386 1 9
HELIX 23 23 SER D 378 SER D 386 1 9
SHEET 1 A 2 LEU A 324 ALA A 327 0
SHEET 2 A 2 TYR A 330 MET A 332 -1 O MET A 332 N LEU A 324
SHEET 1 B 2 GLU B 323 ALA B 327 0
SHEET 2 B 2 TYR B 330 ASP B 333 -1 O MET B 332 N LEU B 324
CISPEP 1 GLU A 245 PRO A 246 0 -7.83
SITE 1 AC1 14 HOH A 1 HOH A 23 GLU A 247 LYS A 248
SITE 2 AC1 14 ILE A 249 LEU A 268 ALA A 272 GLU A 275
SITE 3 AC1 14 LEU A 309 VAL A 313 ARG A 316 VAL A 325
SITE 4 AC1 14 TYR A 326 ASP A 328
CRYST1 203.810 203.810 53.460 90.00 90.00 120.00 H 3 18
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 0.004910 0.002830 0.000000 0.00000
SCALE2 0.000000 0.005670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018710 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
