HEADER SIGNALING PROTEIN 28-APR-17 5NTW
TITLE STRUCTURAL STATES OF RORGT: X-RAY ELUCIDATION OF MOLECULAR MECHANISMS
TITLE 2 AND BINDING INTERACTIONS FOR NATURAL AND SYNTHETIC COMPOUNDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: NUCLEAR RECEPTOR RZR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1
COMPND 6 GROUP F MEMBER 3,RAR-RELATED ORPHAN RECEPTOR C,RETINOID-RELATED
COMPND 7 ORPHAN RECEPTOR-GAMMA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: NUCLEAR RECEPTOR-INTERACTING PROTEIN 1;
COMPND 12 CHAIN: P, Q, R, S;
COMPND 13 SYNONYM: NUCLEAR FACTOR RIP140,RECEPTOR-INTERACTING PROTEIN 140
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RORC, NR1F3, RORG, RZRG;
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_PLASMID: PET28-DERIVED VECTOR;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS NUCLEAR HORMONE RECEPTOR, LIGAND-BINDING DOMAIN, INVERSE AGONIST,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KALLEN
REVDAT 3 17-JAN-24 5NTW 1 REMARK
REVDAT 2 19-JUL-17 5NTW 1
REVDAT 1 21-JUN-17 5NTW 0
JRNL AUTH J.KALLEN,A.IZAAC,C.BE,L.ARISTA,D.ORAIN,K.KAUPMANN,
JRNL AUTH 2 C.GUNTERMANN,K.HOEGENAUER,S.HINTERMANN
JRNL TITL STRUCTURAL STATES OF ROR GAMMA T: X-RAY ELUCIDATION OF
JRNL TITL 2 MOLECULAR MECHANISMS AND BINDING INTERACTIONS FOR NATURAL
JRNL TITL 3 AND SYNTHETIC COMPOUNDS.
JRNL REF CHEMMEDCHEM V. 12 1014 2017
JRNL REFN ESSN 1860-7187
JRNL PMID 28590087
JRNL DOI 10.1002/CMDC.201700278
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 121951
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4950
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) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8840
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 359
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8309
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 152
REMARK 3 SOLVENT ATOMS : 1026
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.114
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.031
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8893 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12072 ; 0.977 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1090 ; 4.100 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 427 ;34.899 ;23.162
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1633 ;12.147 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ;18.389 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1342 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6641 ; 0.004 ; 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): 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5NTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004726.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99979
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126901
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 19.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 19.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.50300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: 5NTI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG3350, 0.2M AMMONIUM ACETATE,
REMARK 280 0.1M BIS-TRIS, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.23400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Q
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, R
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, S
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 262
REMARK 465 PRO A 263
REMARK 465 GLU A 509
REMARK 465 THR A 510
REMARK 465 GLU A 511
REMARK 465 SER A 512
REMARK 465 PRO A 513
REMARK 465 VAL A 514
REMARK 465 GLY A 515
REMARK 465 LEU A 516
REMARK 465 SER A 517
REMARK 465 LYS A 518
REMARK 465 GLY B 262
REMARK 465 PRO B 263
REMARK 465 GLU B 509
REMARK 465 THR B 510
REMARK 465 GLU B 511
REMARK 465 SER B 512
REMARK 465 PRO B 513
REMARK 465 VAL B 514
REMARK 465 GLY B 515
REMARK 465 LEU B 516
REMARK 465 SER B 517
REMARK 465 LYS B 518
REMARK 465 GLY C 262
REMARK 465 PRO C 263
REMARK 465 GLU C 509
REMARK 465 THR C 510
REMARK 465 GLU C 511
REMARK 465 SER C 512
REMARK 465 PRO C 513
REMARK 465 VAL C 514
REMARK 465 GLY C 515
REMARK 465 LEU C 516
REMARK 465 SER C 517
REMARK 465 LYS C 518
REMARK 465 GLY D 262
REMARK 465 PRO D 263
REMARK 465 GLU D 509
REMARK 465 THR D 510
REMARK 465 GLU D 511
REMARK 465 SER D 512
REMARK 465 PRO D 513
REMARK 465 VAL D 514
REMARK 465 GLY D 515
REMARK 465 LEU D 516
REMARK 465 SER D 517
REMARK 465 LYS D 518
REMARK 465 ASN P 493
REMARK 465 SER P 494
REMARK 465 HIS P 495
REMARK 465 GLN P 496
REMARK 465 LYS P 497
REMARK 465 VAL P 498
REMARK 465 LYS P 508
REMARK 465 ASN P 509
REMARK 465 GLU P 510
REMARK 465 GLU P 511
REMARK 465 ASN P 512
REMARK 465 ASN Q 493
REMARK 465 SER Q 494
REMARK 465 HIS Q 495
REMARK 465 GLN Q 496
REMARK 465 LYS Q 497
REMARK 465 VAL Q 498
REMARK 465 ASN Q 509
REMARK 465 GLU Q 510
REMARK 465 GLU Q 511
REMARK 465 ASN Q 512
REMARK 465 ASN R 493
REMARK 465 SER R 494
REMARK 465 HIS R 495
REMARK 465 GLN R 496
REMARK 465 LYS R 497
REMARK 465 VAL R 498
REMARK 465 LYS R 508
REMARK 465 ASN R 509
REMARK 465 GLU R 510
REMARK 465 GLU R 511
REMARK 465 ASN R 512
REMARK 465 ASN S 493
REMARK 465 SER S 494
REMARK 465 HIS S 495
REMARK 465 GLN S 496
REMARK 465 LYS S 497
REMARK 465 VAL S 498
REMARK 465 LYS S 508
REMARK 465 ASN S 509
REMARK 465 GLU S 510
REMARK 465 GLU S 511
REMARK 465 ASN S 512
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 864 O HOH A 884 2.00
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 GLN A 286 -72.49 75.41
REMARK 500 GLU A 435 69.01 -111.23
REMARK 500 GLN B 286 -68.71 76.90
REMARK 500 GLN C 286 -74.09 77.34
REMARK 500 GLN D 286 -69.63 73.38
REMARK 500 GLU D 435 66.65 -115.58
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 C 970 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH D 966 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH D 967 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH D 968 DISTANCE = 6.61 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 98N A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 98N B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 98N C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 98N D 601
DBREF 5NTW A 263 518 UNP P51449 RORG_HUMAN 263 518
DBREF 5NTW B 263 518 UNP P51449 RORG_HUMAN 263 518
DBREF 5NTW C 263 518 UNP P51449 RORG_HUMAN 263 518
DBREF 5NTW D 263 518 UNP P51449 RORG_HUMAN 263 518
DBREF 5NTW P 493 512 UNP P48552 NRIP1_HUMAN 493 512
DBREF 5NTW Q 493 512 UNP P48552 NRIP1_HUMAN 493 512
DBREF 5NTW R 493 512 UNP P48552 NRIP1_HUMAN 493 512
DBREF 5NTW S 493 512 UNP P48552 NRIP1_HUMAN 493 512
SEQADV 5NTW GLY A 262 UNP P51449 EXPRESSION TAG
SEQADV 5NTW SER A 455 UNP P51449 CYS 455 ENGINEERED MUTATION
SEQADV 5NTW GLY B 262 UNP P51449 EXPRESSION TAG
SEQADV 5NTW SER B 455 UNP P51449 CYS 455 ENGINEERED MUTATION
SEQADV 5NTW GLY C 262 UNP P51449 EXPRESSION TAG
SEQADV 5NTW SER C 455 UNP P51449 CYS 455 ENGINEERED MUTATION
SEQADV 5NTW GLY D 262 UNP P51449 EXPRESSION TAG
SEQADV 5NTW SER D 455 UNP P51449 CYS 455 ENGINEERED MUTATION
SEQRES 1 A 257 GLY PRO TYR ALA SER LEU THR GLU ILE GLU HIS LEU VAL
SEQRES 2 A 257 GLN SER VAL CYS LYS SER TYR ARG GLU THR CYS GLN LEU
SEQRES 3 A 257 ARG LEU GLU ASP LEU LEU ARG GLN ARG SER ASN ILE PHE
SEQRES 4 A 257 SER ARG GLU GLU VAL THR GLY TYR GLN ARG LYS SER MET
SEQRES 5 A 257 TRP GLU MET TRP GLU ARG CYS ALA HIS HIS LEU THR GLU
SEQRES 6 A 257 ALA ILE GLN TYR VAL VAL GLU PHE ALA LYS ARG LEU SER
SEQRES 7 A 257 GLY PHE MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU
SEQRES 8 A 257 LEU LYS ALA GLY ALA MET GLU VAL VAL LEU VAL ARG MET
SEQRES 9 A 257 CYS ARG ALA TYR ASN ALA ASP ASN ARG THR VAL PHE PHE
SEQRES 10 A 257 GLU GLY LYS TYR GLY GLY MET GLU LEU PHE ARG ALA LEU
SEQRES 11 A 257 GLY CYS SER GLU LEU ILE SER SER ILE PHE ASP PHE SER
SEQRES 12 A 257 HIS SER LEU SER ALA LEU HIS PHE SER GLU ASP GLU ILE
SEQRES 13 A 257 ALA LEU TYR THR ALA LEU VAL LEU ILE ASN ALA HIS ARG
SEQRES 14 A 257 PRO GLY LEU GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN
SEQRES 15 A 257 TYR ASN LEU GLU LEU ALA PHE HIS HIS HIS LEU SER LYS
SEQRES 16 A 257 THR HIS ARG GLN SER ILE LEU ALA LYS LEU PRO PRO LYS
SEQRES 17 A 257 GLY LYS LEU ARG SER LEU CYS SER GLN HIS VAL GLU ARG
SEQRES 18 A 257 LEU GLN ILE PHE GLN HIS LEU HIS PRO ILE VAL VAL GLN
SEQRES 19 A 257 ALA ALA PHE PRO PRO LEU TYR LYS GLU LEU PHE SER THR
SEQRES 20 A 257 GLU THR GLU SER PRO VAL GLY LEU SER LYS
SEQRES 1 B 257 GLY PRO TYR ALA SER LEU THR GLU ILE GLU HIS LEU VAL
SEQRES 2 B 257 GLN SER VAL CYS LYS SER TYR ARG GLU THR CYS GLN LEU
SEQRES 3 B 257 ARG LEU GLU ASP LEU LEU ARG GLN ARG SER ASN ILE PHE
SEQRES 4 B 257 SER ARG GLU GLU VAL THR GLY TYR GLN ARG LYS SER MET
SEQRES 5 B 257 TRP GLU MET TRP GLU ARG CYS ALA HIS HIS LEU THR GLU
SEQRES 6 B 257 ALA ILE GLN TYR VAL VAL GLU PHE ALA LYS ARG LEU SER
SEQRES 7 B 257 GLY PHE MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU
SEQRES 8 B 257 LEU LYS ALA GLY ALA MET GLU VAL VAL LEU VAL ARG MET
SEQRES 9 B 257 CYS ARG ALA TYR ASN ALA ASP ASN ARG THR VAL PHE PHE
SEQRES 10 B 257 GLU GLY LYS TYR GLY GLY MET GLU LEU PHE ARG ALA LEU
SEQRES 11 B 257 GLY CYS SER GLU LEU ILE SER SER ILE PHE ASP PHE SER
SEQRES 12 B 257 HIS SER LEU SER ALA LEU HIS PHE SER GLU ASP GLU ILE
SEQRES 13 B 257 ALA LEU TYR THR ALA LEU VAL LEU ILE ASN ALA HIS ARG
SEQRES 14 B 257 PRO GLY LEU GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN
SEQRES 15 B 257 TYR ASN LEU GLU LEU ALA PHE HIS HIS HIS LEU SER LYS
SEQRES 16 B 257 THR HIS ARG GLN SER ILE LEU ALA LYS LEU PRO PRO LYS
SEQRES 17 B 257 GLY LYS LEU ARG SER LEU CYS SER GLN HIS VAL GLU ARG
SEQRES 18 B 257 LEU GLN ILE PHE GLN HIS LEU HIS PRO ILE VAL VAL GLN
SEQRES 19 B 257 ALA ALA PHE PRO PRO LEU TYR LYS GLU LEU PHE SER THR
SEQRES 20 B 257 GLU THR GLU SER PRO VAL GLY LEU SER LYS
SEQRES 1 C 257 GLY PRO TYR ALA SER LEU THR GLU ILE GLU HIS LEU VAL
SEQRES 2 C 257 GLN SER VAL CYS LYS SER TYR ARG GLU THR CYS GLN LEU
SEQRES 3 C 257 ARG LEU GLU ASP LEU LEU ARG GLN ARG SER ASN ILE PHE
SEQRES 4 C 257 SER ARG GLU GLU VAL THR GLY TYR GLN ARG LYS SER MET
SEQRES 5 C 257 TRP GLU MET TRP GLU ARG CYS ALA HIS HIS LEU THR GLU
SEQRES 6 C 257 ALA ILE GLN TYR VAL VAL GLU PHE ALA LYS ARG LEU SER
SEQRES 7 C 257 GLY PHE MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU
SEQRES 8 C 257 LEU LYS ALA GLY ALA MET GLU VAL VAL LEU VAL ARG MET
SEQRES 9 C 257 CYS ARG ALA TYR ASN ALA ASP ASN ARG THR VAL PHE PHE
SEQRES 10 C 257 GLU GLY LYS TYR GLY GLY MET GLU LEU PHE ARG ALA LEU
SEQRES 11 C 257 GLY CYS SER GLU LEU ILE SER SER ILE PHE ASP PHE SER
SEQRES 12 C 257 HIS SER LEU SER ALA LEU HIS PHE SER GLU ASP GLU ILE
SEQRES 13 C 257 ALA LEU TYR THR ALA LEU VAL LEU ILE ASN ALA HIS ARG
SEQRES 14 C 257 PRO GLY LEU GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN
SEQRES 15 C 257 TYR ASN LEU GLU LEU ALA PHE HIS HIS HIS LEU SER LYS
SEQRES 16 C 257 THR HIS ARG GLN SER ILE LEU ALA LYS LEU PRO PRO LYS
SEQRES 17 C 257 GLY LYS LEU ARG SER LEU CYS SER GLN HIS VAL GLU ARG
SEQRES 18 C 257 LEU GLN ILE PHE GLN HIS LEU HIS PRO ILE VAL VAL GLN
SEQRES 19 C 257 ALA ALA PHE PRO PRO LEU TYR LYS GLU LEU PHE SER THR
SEQRES 20 C 257 GLU THR GLU SER PRO VAL GLY LEU SER LYS
SEQRES 1 D 257 GLY PRO TYR ALA SER LEU THR GLU ILE GLU HIS LEU VAL
SEQRES 2 D 257 GLN SER VAL CYS LYS SER TYR ARG GLU THR CYS GLN LEU
SEQRES 3 D 257 ARG LEU GLU ASP LEU LEU ARG GLN ARG SER ASN ILE PHE
SEQRES 4 D 257 SER ARG GLU GLU VAL THR GLY TYR GLN ARG LYS SER MET
SEQRES 5 D 257 TRP GLU MET TRP GLU ARG CYS ALA HIS HIS LEU THR GLU
SEQRES 6 D 257 ALA ILE GLN TYR VAL VAL GLU PHE ALA LYS ARG LEU SER
SEQRES 7 D 257 GLY PHE MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU
SEQRES 8 D 257 LEU LYS ALA GLY ALA MET GLU VAL VAL LEU VAL ARG MET
SEQRES 9 D 257 CYS ARG ALA TYR ASN ALA ASP ASN ARG THR VAL PHE PHE
SEQRES 10 D 257 GLU GLY LYS TYR GLY GLY MET GLU LEU PHE ARG ALA LEU
SEQRES 11 D 257 GLY CYS SER GLU LEU ILE SER SER ILE PHE ASP PHE SER
SEQRES 12 D 257 HIS SER LEU SER ALA LEU HIS PHE SER GLU ASP GLU ILE
SEQRES 13 D 257 ALA LEU TYR THR ALA LEU VAL LEU ILE ASN ALA HIS ARG
SEQRES 14 D 257 PRO GLY LEU GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN
SEQRES 15 D 257 TYR ASN LEU GLU LEU ALA PHE HIS HIS HIS LEU SER LYS
SEQRES 16 D 257 THR HIS ARG GLN SER ILE LEU ALA LYS LEU PRO PRO LYS
SEQRES 17 D 257 GLY LYS LEU ARG SER LEU CYS SER GLN HIS VAL GLU ARG
SEQRES 18 D 257 LEU GLN ILE PHE GLN HIS LEU HIS PRO ILE VAL VAL GLN
SEQRES 19 D 257 ALA ALA PHE PRO PRO LEU TYR LYS GLU LEU PHE SER THR
SEQRES 20 D 257 GLU THR GLU SER PRO VAL GLY LEU SER LYS
SEQRES 1 P 20 ASN SER HIS GLN LYS VAL THR LEU LEU GLN LEU LEU LEU
SEQRES 2 P 20 GLY HIS LYS ASN GLU GLU ASN
SEQRES 1 Q 20 ASN SER HIS GLN LYS VAL THR LEU LEU GLN LEU LEU LEU
SEQRES 2 Q 20 GLY HIS LYS ASN GLU GLU ASN
SEQRES 1 R 20 ASN SER HIS GLN LYS VAL THR LEU LEU GLN LEU LEU LEU
SEQRES 2 R 20 GLY HIS LYS ASN GLU GLU ASN
SEQRES 1 S 20 ASN SER HIS GLN LYS VAL THR LEU LEU GLN LEU LEU LEU
SEQRES 2 S 20 GLY HIS LYS ASN GLU GLU ASN
HET 98N A 601 38
HET 98N B 601 38
HET 98N C 601 38
HET 98N D 601 38
HETNAM 98N (S)-N-((5-(ETHYLSULFONYL)PYRIDIN-2-YL)METHYL)-7-
HETNAM 2 98N ISOPROPYL-6-(((1R,4S)-4-(TRIFLUOROMETHYL)CYCLOHEXYL)
HETNAM 3 98N METHYL)-6,7-DIHYDRO-5H-PYRROLO[3,4-B]PYRIDINE-3-
HETNAM 4 98N CARBOXAMIDE
FORMUL 9 98N 4(C27 H35 F3 N4 O3 S)
FORMUL 13 HOH *1026(H2 O)
HELIX 1 AA1 SER A 266 GLU A 283 1 18
HELIX 2 AA2 ARG A 288 GLN A 295 1 8
HELIX 3 AA3 ARG A 296 ASN A 298 5 3
HELIX 4 AA4 SER A 301 ARG A 310 1 10
HELIX 5 AA5 SER A 312 LEU A 338 1 27
HELIX 6 AA6 CYS A 345 MET A 365 1 21
HELIX 7 AA7 GLY A 384 GLY A 392 5 9
HELIX 8 AA8 CYS A 393 ALA A 409 1 17
HELIX 9 AA9 SER A 413 ILE A 426 1 14
HELIX 10 AB1 GLU A 435 THR A 457 1 23
HELIX 11 AB2 ARG A 459 LEU A 466 5 8
HELIX 12 AB3 PRO A 468 HIS A 490 1 23
HELIX 13 AB4 HIS A 490 PHE A 498 1 9
HELIX 14 AB5 PRO A 499 SER A 507 1 9
HELIX 15 AB6 SER B 266 GLU B 283 1 18
HELIX 16 AB7 ARG B 288 GLN B 295 1 8
HELIX 17 AB8 ARG B 296 ASN B 298 5 3
HELIX 18 AB9 SER B 301 ARG B 310 1 10
HELIX 19 AC1 SER B 312 LEU B 338 1 27
HELIX 20 AC2 CYS B 345 MET B 365 1 21
HELIX 21 AC3 GLY B 384 GLY B 392 5 9
HELIX 22 AC4 CYS B 393 ALA B 409 1 17
HELIX 23 AC5 SER B 413 ILE B 426 1 14
HELIX 24 AC6 GLU B 435 THR B 457 1 23
HELIX 25 AC7 ARG B 459 LEU B 466 5 8
HELIX 26 AC8 GLY B 470 HIS B 490 1 21
HELIX 27 AC9 ILE B 492 PHE B 498 1 7
HELIX 28 AD1 PRO B 499 SER B 507 1 9
HELIX 29 AD2 SER C 266 GLU C 283 1 18
HELIX 30 AD3 ARG C 288 GLN C 295 1 8
HELIX 31 AD4 ARG C 296 ASN C 298 5 3
HELIX 32 AD5 SER C 301 ARG C 310 1 10
HELIX 33 AD6 SER C 312 LEU C 338 1 27
HELIX 34 AD7 LEU C 338 LEU C 344 1 7
HELIX 35 AD8 CYS C 345 MET C 365 1 21
HELIX 36 AD9 GLY C 384 GLY C 392 5 9
HELIX 37 AE1 CYS C 393 ALA C 409 1 17
HELIX 38 AE2 SER C 413 ILE C 426 1 14
HELIX 39 AE3 GLU C 435 THR C 457 1 23
HELIX 40 AE4 ARG C 459 LEU C 466 5 8
HELIX 41 AE5 PRO C 468 HIS C 490 1 23
HELIX 42 AE6 HIS C 490 PHE C 498 1 9
HELIX 43 AE7 PRO C 499 SER C 507 1 9
HELIX 44 AE8 SER D 266 GLU D 283 1 18
HELIX 45 AE9 ARG D 288 GLN D 295 1 8
HELIX 46 AF1 SER D 301 ARG D 310 1 10
HELIX 47 AF2 SER D 312 LEU D 338 1 27
HELIX 48 AF3 GLY D 340 LEU D 344 5 5
HELIX 49 AF4 CYS D 345 MET D 365 1 21
HELIX 50 AF5 GLY D 384 GLY D 392 5 9
HELIX 51 AF6 CYS D 393 ALA D 409 1 17
HELIX 52 AF7 SER D 413 ILE D 426 1 14
HELIX 53 AF8 GLU D 435 THR D 457 1 23
HELIX 54 AF9 ARG D 459 LEU D 466 5 8
HELIX 55 AG1 PRO D 468 HIS D 490 1 23
HELIX 56 AG2 HIS D 490 PHE D 498 1 9
HELIX 57 AG3 PRO D 499 SER D 507 1 9
HELIX 58 AG4 LEU P 500 GLY P 506 1 7
HELIX 59 AG5 LEU Q 500 GLY Q 506 1 7
HELIX 60 AG6 LEU R 500 GLY R 506 1 7
HELIX 61 AG7 LEU S 500 GLY S 506 1 7
SHEET 1 AA1 3 TYR A 369 ASN A 370 0
SHEET 2 AA1 3 THR A 375 PHE A 378 -1 O THR A 375 N ASN A 370
SHEET 3 AA1 3 LYS A 381 GLY A 383 -1 O GLY A 383 N VAL A 376
SHEET 1 AA2 3 TYR B 369 ASN B 370 0
SHEET 2 AA2 3 THR B 375 PHE B 378 -1 O THR B 375 N ASN B 370
SHEET 3 AA2 3 LYS B 381 GLY B 383 -1 O LYS B 381 N PHE B 378
SHEET 1 AA3 3 TYR C 369 ASN C 370 0
SHEET 2 AA3 3 THR C 375 PHE C 378 -1 O THR C 375 N ASN C 370
SHEET 3 AA3 3 LYS C 381 GLY C 383 -1 O LYS C 381 N PHE C 378
SHEET 1 AA4 3 TYR D 369 ASN D 370 0
SHEET 2 AA4 3 THR D 375 PHE D 378 -1 O THR D 375 N ASN D 370
SHEET 3 AA4 3 LYS D 381 GLY D 383 -1 O LYS D 381 N PHE D 378
SITE 1 AC1 19 CYS A 285 GLN A 286 LEU A 287 TRP A 317
SITE 2 AC1 19 CYS A 320 HIS A 323 ARG A 364 MET A 365
SITE 3 AC1 19 ARG A 367 ALA A 368 PHE A 377 LEU A 391
SITE 4 AC1 19 CYS A 393 LEU A 396 ILE A 400 HIS A 479
SITE 5 AC1 19 ARG A 482 HOH A 770 HOH A 815
SITE 1 AC2 17 CYS B 285 GLN B 286 LEU B 287 HIS B 323
SITE 2 AC2 17 ARG B 364 MET B 365 ARG B 367 ALA B 368
SITE 3 AC2 17 PHE B 377 PHE B 378 PHE B 388 LEU B 391
SITE 4 AC2 17 CYS B 393 LEU B 396 HIS B 479 HOH B 770
SITE 5 AC2 17 HOH B 795
SITE 1 AC3 17 CYS C 285 GLN C 286 LEU C 287 TRP C 317
SITE 2 AC3 17 HIS C 323 ARG C 364 MET C 365 ARG C 367
SITE 3 AC3 17 ALA C 368 PHE C 377 LEU C 391 CYS C 393
SITE 4 AC3 17 LEU C 396 HIS C 479 ARG C 482 HOH C 763
SITE 5 AC3 17 HOH C 849
SITE 1 AC4 18 CYS D 285 GLN D 286 LEU D 287 TRP D 317
SITE 2 AC4 18 CYS D 320 HIS D 323 ARG D 364 MET D 365
SITE 3 AC4 18 ARG D 367 ALA D 368 PHE D 377 LEU D 391
SITE 4 AC4 18 CYS D 393 LEU D 396 HIS D 479 ARG D 482
SITE 5 AC4 18 HOH D 765 HOH D 808
CRYST1 86.187 68.468 96.717 90.00 110.32 90.00 P 1 21 1 8
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 0.011603 0.000000 0.004296 0.00000
SCALE2 0.000000 0.014605 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011026 0.00000
(ATOM LINES ARE NOT SHOWN.)
END