HEADER MEMBRANE PROTEIN 16-MAY-08 3D5K
TITLE CRYSTAL STRUCTURE OF THE OPRM CHANNEL IN A NON-SYMMETRICAL SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER MEMBRANE PROTEIN OPRM;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: OPRM;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: OPRM, OPRK, PA0427;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C43;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAD33
KEYWDS MEMBRANE PROTEIN, CHANNEL, BETA-ALPHA-BARREL, ANTIBIOTIC RESISTANCE,
KEYWDS 2 LIPOPROTEIN, MEMBRANE, OUTER MEMBRANE, PALMITATE, TRANSMEMBRANE,
KEYWDS 3 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PHAN,I.BROUTIN,A.DUCRUIX
REVDAT 4 01-NOV-23 3D5K 1 REMARK SEQADV LINK
REVDAT 3 18-APR-12 3D5K 1 JRNL VERSN
REVDAT 2 21-APR-10 3D5K 1 JRNL
REVDAT 1 02-JUN-09 3D5K 0
JRNL AUTH G.PHAN,H.BENABDELHAK,M.B.LASCOMBE,P.BENAS,S.RETY,M.PICARD,
JRNL AUTH 2 A.DUCRUIX,C.ETCHEBEST,I.BROUTIN
JRNL TITL STRUCTURAL AND DYNAMICAL INSIGHTS INTO THE OPENING MECHANISM
JRNL TITL 2 OF P. AERUGINOSA OPRM CHANNEL.
JRNL REF STRUCTURE V. 18 507 2010
JRNL REFN ISSN 0969-2126
JRNL PMID 20399187
JRNL DOI 10.1016/J.STR.2010.01.018
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 65916
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) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5058
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4703
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 342
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10470
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 539
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
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): 0.412
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.295
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.236
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.063
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10637 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14460 ; 0.888 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1359 ; 4.349 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 513 ;35.675 ;24.386
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1713 ;14.031 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 90 ;15.600 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1659 ; 0.054 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8202 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4798 ; 0.162 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7447 ; 0.287 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 521 ; 0.119 ; 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): 38 ; 0.218 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.043 ; 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): 6773 ; 0.265 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10776 ; 0.505 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3975 ; 0.691 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3684 ; 1.238 ; 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 : NULL
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 3D5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-06
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 : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69761
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 36.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 1WP1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE 1M, PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 36.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 172.25000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 172.25000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.10000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -203.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR A 456
REMARK 465 GLN A 457
REMARK 465 GLN A 458
REMARK 465 GLN A 459
REMARK 465 THR A 460
REMARK 465 ALA A 461
REMARK 465 LYS A 462
REMARK 465 LYS A 463
REMARK 465 GLU A 464
REMARK 465 ASP A 465
REMARK 465 PRO A 466
REMARK 465 GLN A 467
REMARK 465 ALA A 468
REMARK 465 HIS A 469
REMARK 465 HIS A 470
REMARK 465 HIS A 471
REMARK 465 HIS A 472
REMARK 465 HIS A 473
REMARK 465 HIS A 474
REMARK 465 THR B 456
REMARK 465 GLN B 457
REMARK 465 GLN B 458
REMARK 465 GLN B 459
REMARK 465 THR B 460
REMARK 465 ALA B 461
REMARK 465 LYS B 462
REMARK 465 LYS B 463
REMARK 465 GLU B 464
REMARK 465 ASP B 465
REMARK 465 PRO B 466
REMARK 465 GLN B 467
REMARK 465 ALA B 468
REMARK 465 HIS B 469
REMARK 465 HIS B 470
REMARK 465 HIS B 471
REMARK 465 HIS B 472
REMARK 465 HIS B 473
REMARK 465 HIS B 474
REMARK 465 THR C 456
REMARK 465 GLN C 457
REMARK 465 GLN C 458
REMARK 465 GLN C 459
REMARK 465 THR C 460
REMARK 465 ALA C 461
REMARK 465 LYS C 462
REMARK 465 LYS C 463
REMARK 465 GLU C 464
REMARK 465 ASP C 465
REMARK 465 PRO C 466
REMARK 465 GLN C 467
REMARK 465 ALA C 468
REMARK 465 HIS C 469
REMARK 465 HIS C 470
REMARK 465 HIS C 471
REMARK 465 HIS C 472
REMARK 465 HIS C 473
REMARK 465 HIS C 474
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 SCY A 1 N SER A 2 1.76
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 SCY A 1 C SER A 2 N 0.162
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 SCY A 1 CA - C - N ANGL. DEV. = 32.3 DEGREES
REMARK 500 SCY A 1 O - C - N ANGL. DEV. = -42.1 DEGREES
REMARK 500 THR B 106 N - CA - CB ANGL. DEV. = 17.4 DEGREES
REMARK 500 THR B 106 N - CA - C ANGL. DEV. = -17.7 DEGREES
REMARK 500 ALA B 337 N - CA - CB ANGL. DEV. = 20.9 DEGREES
REMARK 500 SCY C 1 O - C - N ANGL. DEV. = -12.2 DEGREES
REMARK 500 SER C 2 C - N - CA ANGL. DEV. = 28.2 DEGREES
REMARK 500 GLN C 453 CA - C - N ANGL. DEV. = -16.3 DEGREES
REMARK 500 GLN C 453 O - C - N ANGL. DEV. = 15.5 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 PRO A 13 43.83 -85.87
REMARK 500 PHE A 317 39.11 -88.19
REMARK 500 PRO B 13 42.67 -85.68
REMARK 500 GLU B 259 124.94 -35.99
REMARK 500 PRO C 13 46.49 -86.81
REMARK 500 LEU C 316 -70.31 -67.28
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 THR B 105 THR B 106 -138.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SCY A 1 32.01
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 NA A 475 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 371 OD2
REMARK 620 2 GLN C 229 O 105.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 478 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 66 O
REMARK 620 2 THR B 146 O 113.0
REMARK 620 3 HOH B 513 O 94.6 148.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 476 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 228 O
REMARK 620 2 ASN B 232 OD1 71.7
REMARK 620 3 TYR C 24 OH 77.8 72.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 480 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 418 O
REMARK 620 2 HOH B 544 O 122.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 475 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 263 O
REMARK 620 2 HOH C 478 O 107.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 476 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 274 OD1
REMARK 620 2 ASP C 274 OD2 41.1
REMARK 620 3 ALA C 361 O 126.4 165.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 476
DBREF 3D5K A 1 468 UNP Q51487 OPRM_PSEAE 18 485
DBREF 3D5K B 1 468 UNP Q51487 OPRM_PSEAE 18 485
DBREF 3D5K C 1 468 UNP Q51487 OPRM_PSEAE 18 485
SEQADV 3D5K HIS A 469 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS A 470 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS A 471 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS A 472 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS A 473 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS A 474 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS B 469 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS B 470 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS B 471 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS B 472 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS B 473 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS B 474 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS C 469 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS C 470 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS C 471 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS C 472 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS C 473 UNP Q51487 EXPRESSION TAG
SEQADV 3D5K HIS C 474 UNP Q51487 EXPRESSION TAG
SEQRES 1 A 474 SCY SER LEU ILE PRO ASP TYR GLN ARG PRO GLU ALA PRO
SEQRES 2 A 474 VAL ALA ALA ALA TYR PRO GLN GLY GLN ALA TYR GLY GLN
SEQRES 3 A 474 ASN THR GLY ALA ALA ALA VAL PRO ALA ALA ASP ILE GLY
SEQRES 4 A 474 TRP ARG GLU PHE PHE ARG ASP PRO GLN LEU GLN GLN LEU
SEQRES 5 A 474 ILE GLY VAL ALA LEU GLU ASN ASN ARG ASP LEU ARG VAL
SEQRES 6 A 474 ALA ALA LEU ASN VAL GLU ALA PHE ARG ALA GLN TYR ARG
SEQRES 7 A 474 ILE GLN ARG ALA ASP LEU PHE PRO ARG ILE GLY VAL ASP
SEQRES 8 A 474 GLY SER GLY THR ARG GLN ARG LEU PRO GLY ASP LEU SER
SEQRES 9 A 474 THR THR GLY SER PRO ALA ILE SER SER GLN TYR GLY VAL
SEQRES 10 A 474 THR LEU GLY THR THR ALA TRP GLU LEU ASP LEU PHE GLY
SEQRES 11 A 474 ARG LEU ARG SER LEU ARG ASP GLN ALA LEU GLU GLN TYR
SEQRES 12 A 474 LEU ALA THR GLU GLN ALA GLN ARG SER ALA GLN THR THR
SEQRES 13 A 474 LEU VAL ALA SER VAL ALA THR ALA TYR LEU THR LEU LYS
SEQRES 14 A 474 ALA ASP GLN ALA GLN LEU GLN LEU THR LYS ASP THR LEU
SEQRES 15 A 474 GLY THR TYR GLN LYS SER PHE ASP LEU THR GLN ARG SER
SEQRES 16 A 474 TYR ASP VAL GLY VAL ALA SER ALA LEU ASP LEU ARG GLN
SEQRES 17 A 474 ALA GLN THR ALA VAL GLU GLY ALA ARG ALA THR LEU ALA
SEQRES 18 A 474 GLN TYR THR ARG LEU VAL ALA GLN ASP GLN ASN ALA LEU
SEQRES 19 A 474 VAL LEU LEU LEU GLY SER GLY ILE PRO ALA ASN LEU PRO
SEQRES 20 A 474 GLN GLY LEU GLY LEU ASP GLN THR LEU LEU THR GLU VAL
SEQRES 21 A 474 PRO ALA GLY LEU PRO SER ASP LEU LEU GLN ARG ARG PRO
SEQRES 22 A 474 ASP ILE LEU GLU ALA GLU HIS GLN LEU MET ALA ALA ASN
SEQRES 23 A 474 ALA SER ILE GLY ALA ALA ARG ALA ALA PHE PHE PRO SER
SEQRES 24 A 474 ILE SER LEU THR ALA ASN ALA GLY THR MET SER ARG GLN
SEQRES 25 A 474 LEU SER GLY LEU PHE ASP ALA GLY SER GLY SER TRP LEU
SEQRES 26 A 474 PHE GLN PRO SER ILE ASN LEU PRO ILE PHE THR ALA GLY
SEQRES 27 A 474 SER LEU ARG ALA SER LEU ASP TYR ALA LYS ILE GLN LYS
SEQRES 28 A 474 ASP ILE ASN VAL ALA GLN TYR GLU LYS ALA ILE GLN THR
SEQRES 29 A 474 ALA PHE GLN GLU VAL ALA ASP GLY LEU ALA ALA ARG GLY
SEQRES 30 A 474 THR PHE THR GLU GLN LEU GLN ALA GLN ARG ASP LEU VAL
SEQRES 31 A 474 LYS ALA SER ASP GLU TYR TYR GLN LEU ALA ASP LYS ARG
SEQRES 32 A 474 TYR ARG THR GLY VAL ASP ASN TYR LEU THR LEU LEU ASP
SEQRES 33 A 474 ALA GLN ARG SER LEU PHE THR ALA GLN GLN GLN LEU ILE
SEQRES 34 A 474 THR ASP ARG LEU ASN GLN LEU THR SER GLU VAL ASN LEU
SEQRES 35 A 474 TYR LYS ALA LEU GLY GLY GLY TRP ASN GLN GLN THR VAL
SEQRES 36 A 474 THR GLN GLN GLN THR ALA LYS LYS GLU ASP PRO GLN ALA
SEQRES 37 A 474 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 474 SCY SER LEU ILE PRO ASP TYR GLN ARG PRO GLU ALA PRO
SEQRES 2 B 474 VAL ALA ALA ALA TYR PRO GLN GLY GLN ALA TYR GLY GLN
SEQRES 3 B 474 ASN THR GLY ALA ALA ALA VAL PRO ALA ALA ASP ILE GLY
SEQRES 4 B 474 TRP ARG GLU PHE PHE ARG ASP PRO GLN LEU GLN GLN LEU
SEQRES 5 B 474 ILE GLY VAL ALA LEU GLU ASN ASN ARG ASP LEU ARG VAL
SEQRES 6 B 474 ALA ALA LEU ASN VAL GLU ALA PHE ARG ALA GLN TYR ARG
SEQRES 7 B 474 ILE GLN ARG ALA ASP LEU PHE PRO ARG ILE GLY VAL ASP
SEQRES 8 B 474 GLY SER GLY THR ARG GLN ARG LEU PRO GLY ASP LEU SER
SEQRES 9 B 474 THR THR GLY SER PRO ALA ILE SER SER GLN TYR GLY VAL
SEQRES 10 B 474 THR LEU GLY THR THR ALA TRP GLU LEU ASP LEU PHE GLY
SEQRES 11 B 474 ARG LEU ARG SER LEU ARG ASP GLN ALA LEU GLU GLN TYR
SEQRES 12 B 474 LEU ALA THR GLU GLN ALA GLN ARG SER ALA GLN THR THR
SEQRES 13 B 474 LEU VAL ALA SER VAL ALA THR ALA TYR LEU THR LEU LYS
SEQRES 14 B 474 ALA ASP GLN ALA GLN LEU GLN LEU THR LYS ASP THR LEU
SEQRES 15 B 474 GLY THR TYR GLN LYS SER PHE ASP LEU THR GLN ARG SER
SEQRES 16 B 474 TYR ASP VAL GLY VAL ALA SER ALA LEU ASP LEU ARG GLN
SEQRES 17 B 474 ALA GLN THR ALA VAL GLU GLY ALA ARG ALA THR LEU ALA
SEQRES 18 B 474 GLN TYR THR ARG LEU VAL ALA GLN ASP GLN ASN ALA LEU
SEQRES 19 B 474 VAL LEU LEU LEU GLY SER GLY ILE PRO ALA ASN LEU PRO
SEQRES 20 B 474 GLN GLY LEU GLY LEU ASP GLN THR LEU LEU THR GLU VAL
SEQRES 21 B 474 PRO ALA GLY LEU PRO SER ASP LEU LEU GLN ARG ARG PRO
SEQRES 22 B 474 ASP ILE LEU GLU ALA GLU HIS GLN LEU MET ALA ALA ASN
SEQRES 23 B 474 ALA SER ILE GLY ALA ALA ARG ALA ALA PHE PHE PRO SER
SEQRES 24 B 474 ILE SER LEU THR ALA ASN ALA GLY THR MET SER ARG GLN
SEQRES 25 B 474 LEU SER GLY LEU PHE ASP ALA GLY SER GLY SER TRP LEU
SEQRES 26 B 474 PHE GLN PRO SER ILE ASN LEU PRO ILE PHE THR ALA GLY
SEQRES 27 B 474 SER LEU ARG ALA SER LEU ASP TYR ALA LYS ILE GLN LYS
SEQRES 28 B 474 ASP ILE ASN VAL ALA GLN TYR GLU LYS ALA ILE GLN THR
SEQRES 29 B 474 ALA PHE GLN GLU VAL ALA ASP GLY LEU ALA ALA ARG GLY
SEQRES 30 B 474 THR PHE THR GLU GLN LEU GLN ALA GLN ARG ASP LEU VAL
SEQRES 31 B 474 LYS ALA SER ASP GLU TYR TYR GLN LEU ALA ASP LYS ARG
SEQRES 32 B 474 TYR ARG THR GLY VAL ASP ASN TYR LEU THR LEU LEU ASP
SEQRES 33 B 474 ALA GLN ARG SER LEU PHE THR ALA GLN GLN GLN LEU ILE
SEQRES 34 B 474 THR ASP ARG LEU ASN GLN LEU THR SER GLU VAL ASN LEU
SEQRES 35 B 474 TYR LYS ALA LEU GLY GLY GLY TRP ASN GLN GLN THR VAL
SEQRES 36 B 474 THR GLN GLN GLN THR ALA LYS LYS GLU ASP PRO GLN ALA
SEQRES 37 B 474 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 474 SCY SER LEU ILE PRO ASP TYR GLN ARG PRO GLU ALA PRO
SEQRES 2 C 474 VAL ALA ALA ALA TYR PRO GLN GLY GLN ALA TYR GLY GLN
SEQRES 3 C 474 ASN THR GLY ALA ALA ALA VAL PRO ALA ALA ASP ILE GLY
SEQRES 4 C 474 TRP ARG GLU PHE PHE ARG ASP PRO GLN LEU GLN GLN LEU
SEQRES 5 C 474 ILE GLY VAL ALA LEU GLU ASN ASN ARG ASP LEU ARG VAL
SEQRES 6 C 474 ALA ALA LEU ASN VAL GLU ALA PHE ARG ALA GLN TYR ARG
SEQRES 7 C 474 ILE GLN ARG ALA ASP LEU PHE PRO ARG ILE GLY VAL ASP
SEQRES 8 C 474 GLY SER GLY THR ARG GLN ARG LEU PRO GLY ASP LEU SER
SEQRES 9 C 474 THR THR GLY SER PRO ALA ILE SER SER GLN TYR GLY VAL
SEQRES 10 C 474 THR LEU GLY THR THR ALA TRP GLU LEU ASP LEU PHE GLY
SEQRES 11 C 474 ARG LEU ARG SER LEU ARG ASP GLN ALA LEU GLU GLN TYR
SEQRES 12 C 474 LEU ALA THR GLU GLN ALA GLN ARG SER ALA GLN THR THR
SEQRES 13 C 474 LEU VAL ALA SER VAL ALA THR ALA TYR LEU THR LEU LYS
SEQRES 14 C 474 ALA ASP GLN ALA GLN LEU GLN LEU THR LYS ASP THR LEU
SEQRES 15 C 474 GLY THR TYR GLN LYS SER PHE ASP LEU THR GLN ARG SER
SEQRES 16 C 474 TYR ASP VAL GLY VAL ALA SER ALA LEU ASP LEU ARG GLN
SEQRES 17 C 474 ALA GLN THR ALA VAL GLU GLY ALA ARG ALA THR LEU ALA
SEQRES 18 C 474 GLN TYR THR ARG LEU VAL ALA GLN ASP GLN ASN ALA LEU
SEQRES 19 C 474 VAL LEU LEU LEU GLY SER GLY ILE PRO ALA ASN LEU PRO
SEQRES 20 C 474 GLN GLY LEU GLY LEU ASP GLN THR LEU LEU THR GLU VAL
SEQRES 21 C 474 PRO ALA GLY LEU PRO SER ASP LEU LEU GLN ARG ARG PRO
SEQRES 22 C 474 ASP ILE LEU GLU ALA GLU HIS GLN LEU MET ALA ALA ASN
SEQRES 23 C 474 ALA SER ILE GLY ALA ALA ARG ALA ALA PHE PHE PRO SER
SEQRES 24 C 474 ILE SER LEU THR ALA ASN ALA GLY THR MET SER ARG GLN
SEQRES 25 C 474 LEU SER GLY LEU PHE ASP ALA GLY SER GLY SER TRP LEU
SEQRES 26 C 474 PHE GLN PRO SER ILE ASN LEU PRO ILE PHE THR ALA GLY
SEQRES 27 C 474 SER LEU ARG ALA SER LEU ASP TYR ALA LYS ILE GLN LYS
SEQRES 28 C 474 ASP ILE ASN VAL ALA GLN TYR GLU LYS ALA ILE GLN THR
SEQRES 29 C 474 ALA PHE GLN GLU VAL ALA ASP GLY LEU ALA ALA ARG GLY
SEQRES 30 C 474 THR PHE THR GLU GLN LEU GLN ALA GLN ARG ASP LEU VAL
SEQRES 31 C 474 LYS ALA SER ASP GLU TYR TYR GLN LEU ALA ASP LYS ARG
SEQRES 32 C 474 TYR ARG THR GLY VAL ASP ASN TYR LEU THR LEU LEU ASP
SEQRES 33 C 474 ALA GLN ARG SER LEU PHE THR ALA GLN GLN GLN LEU ILE
SEQRES 34 C 474 THR ASP ARG LEU ASN GLN LEU THR SER GLU VAL ASN LEU
SEQRES 35 C 474 TYR LYS ALA LEU GLY GLY GLY TRP ASN GLN GLN THR VAL
SEQRES 36 C 474 THR GLN GLN GLN THR ALA LYS LYS GLU ASP PRO GLN ALA
SEQRES 37 C 474 HIS HIS HIS HIS HIS HIS
MODRES 3D5K SCY A 1 CYS S-ACETYL-CYSTEINE
MODRES 3D5K SCY B 1 CYS S-ACETYL-CYSTEINE
MODRES 3D5K SCY C 1 CYS S-ACETYL-CYSTEINE
HET SCY A 1 9
HET SCY B 1 9
HET SCY C 1 9
HET NA A 475 1
HET NA A 476 1
HET CL B 475 1
HET NA B 476 1
HET NA B 477 1
HET NA B 478 1
HET NA B 479 1
HET NA B 480 1
HET NA C 475 1
HET NA C 476 1
HETNAM SCY S-ACETYL-CYSTEINE
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 SCY 3(C5 H9 N O3 S)
FORMUL 4 NA 9(NA 1+)
FORMUL 6 CL CL 1-
FORMUL 14 HOH *539(H2 O)
HELIX 1 1 GLY A 39 PHE A 44 1 6
HELIX 2 2 ASP A 46 ASN A 60 1 15
HELIX 3 3 ASN A 60 ASP A 83 1 24
HELIX 4 4 GLY A 130 ASP A 197 1 68
HELIX 5 5 SER A 202 GLY A 239 1 38
HELIX 6 6 LEU A 264 SER A 266 5 3
HELIX 7 7 ASP A 267 ARG A 272 1 6
HELIX 8 8 ARG A 272 ALA A 294 1 23
HELIX 9 9 GLY A 338 THR A 406 1 69
HELIX 10 10 ASN A 410 GLY A 447 1 38
HELIX 11 11 PRO B 34 ILE B 38 5 5
HELIX 12 12 GLY B 39 PHE B 44 1 6
HELIX 13 13 ASP B 46 ASN B 60 1 15
HELIX 14 14 ASN B 60 ASP B 83 1 24
HELIX 15 15 GLY B 130 VAL B 198 1 69
HELIX 16 16 SER B 202 GLY B 239 1 38
HELIX 17 17 LEU B 264 SER B 266 5 3
HELIX 18 18 ASP B 267 ARG B 272 1 6
HELIX 19 19 ARG B 272 ALA B 294 1 23
HELIX 20 20 ALA B 295 PHE B 297 5 3
HELIX 21 21 GLN B 312 LEU B 316 5 5
HELIX 22 22 GLY B 338 THR B 406 1 69
HELIX 23 23 TYR B 411 LEU B 446 1 36
HELIX 24 24 PRO C 34 ILE C 38 5 5
HELIX 25 25 GLY C 39 PHE C 44 1 6
HELIX 26 26 ASP C 46 ASN C 60 1 15
HELIX 27 27 ASN C 60 ASP C 83 1 24
HELIX 28 28 GLY C 130 VAL C 198 1 69
HELIX 29 29 SER C 202 GLY C 239 1 38
HELIX 30 30 LEU C 264 SER C 266 5 3
HELIX 31 31 ASP C 267 ARG C 272 1 6
HELIX 32 32 ARG C 272 ALA C 294 1 23
HELIX 33 33 GLN C 312 LEU C 316 5 5
HELIX 34 34 GLY C 338 GLY C 377 1 40
HELIX 35 35 THR C 378 THR C 406 1 29
HELIX 36 36 ASN C 410 LEU C 446 1 37
SHEET 1 A13 ILE A 88 LEU A 99 0
SHEET 2 A13 ALA A 110 LEU A 126 -1 O ALA A 110 N LEU A 99
SHEET 3 A13 SER A 299 SER A 310 -1 O SER A 310 N TYR A 115
SHEET 4 A13 GLY A 322 PHE A 335 -1 O ASN A 331 N SER A 299
SHEET 5 A13 ILE C 88 LEU C 99 -1 O GLY C 92 N ILE A 330
SHEET 6 A13 ALA C 110 LEU C 126 -1 O THR C 118 N ASP C 91
SHEET 7 A13 SER C 299 SER C 310 -1 O SER C 310 N TYR C 115
SHEET 8 A13 GLY C 322 PHE C 335 -1 O SER C 329 N SER C 301
SHEET 9 A13 ILE B 88 LEU B 99 -1 N ILE B 88 O PHE C 335
SHEET 10 A13 ALA B 110 LEU B 126 -1 O GLY B 116 N SER B 93
SHEET 11 A13 SER B 299 SER B 310 -1 O SER B 310 N TYR B 115
SHEET 12 A13 GLY B 322 PHE B 335 -1 O SER B 329 N SER B 301
SHEET 13 A13 ILE A 88 LEU A 99 -1 N GLY A 92 O ILE B 330
LINK C SCY A 1 N SER A 2 1555 1555 1.50
LINK C SCY B 1 N SER B 2 1555 1555 1.28
LINK C SCY C 1 N SER C 2 1555 1555 1.27
LINK OD2 ASP A 371 NA NA A 475 1555 1555 2.41
LINK O TRP A 450 NA NA A 476 1555 1555 3.08
LINK NA NA A 475 O GLN C 229 1555 1555 2.92
LINK O ALA B 66 NA NA B 478 1555 1555 3.01
LINK O THR B 146 NA NA B 478 1555 1555 2.81
LINK OE1 GLN B 154 NA NA B 479 1555 1555 3.08
LINK O ALA B 228 NA NA B 476 1555 1555 3.18
LINK OD1 ASN B 232 NA NA B 476 1555 1555 3.14
LINK O LEU B 256 NA NA B 477 1555 1555 2.90
LINK O GLN B 418 NA NA B 480 1555 1555 3.03
LINK NA NA B 476 OH TYR C 24 1555 1555 2.84
LINK NA NA B 478 O HOH B 513 1555 1555 2.60
LINK NA NA B 480 O HOH B 544 1555 1555 2.97
LINK O GLY C 263 NA NA C 475 1555 1555 2.55
LINK OD1 ASP C 274 NA NA C 476 1555 1555 3.02
LINK OD2 ASP C 274 NA NA C 476 1555 1555 3.19
LINK O ALA C 361 NA NA C 476 1555 1555 2.80
LINK NA NA C 475 O HOH C 478 1555 1555 2.49
SITE 1 AC1 3 GLN A 367 ASP A 371 GLN C 229
SITE 1 AC2 3 TRP A 40 GLN A 154 TRP A 450
SITE 1 AC3 4 ARG B 194 LEU B 256 LEU B 257 ARG B 432
SITE 1 AC4 3 ALA B 228 ASN B 232 TYR C 24
SITE 1 AC5 3 ARG B 45 ASP B 46 LEU B 256
SITE 1 AC6 4 ALA B 66 THR B 146 GLN B 150 HOH B 513
SITE 1 AC7 3 TRP B 40 GLN B 154 TRP B 450
SITE 1 AC8 3 TYR B 185 GLN B 418 HOH B 544
SITE 1 AC9 3 GLY C 29 GLY C 263 HOH C 478
SITE 1 BC1 3 ARG C 272 ASP C 274 ALA C 361
CRYST1 73.900 70.200 344.500 90.00 90.00 90.00 P 21 21 21 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013532 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014245 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002903 0.00000
HETATM 1 N SCY A 1 1.262 -1.217 -9.990 1.00 66.65 N
HETATM 2 CA SCY A 1 0.884 0.161 -10.191 1.00 66.65 C
HETATM 3 CB SCY A 1 2.017 1.048 -9.737 1.00 66.66 C
HETATM 4 SG SCY A 1 1.754 2.719 -10.264 1.00 66.84 S
HETATM 5 CD SCY A 1 1.156 3.354 -8.916 1.00 67.10 C
HETATM 6 OCD SCY A 1 1.958 3.887 -8.186 1.00 67.28 O
HETATM 7 CE SCY A 1 -0.334 3.194 -8.633 1.00 67.16 C
HETATM 8 C SCY A 1 0.633 0.431 -11.665 1.00 66.63 C
HETATM 9 O SCY A 1 -0.247 1.171 -12.031 1.00 66.54 O
(ATOM LINES ARE NOT SHOWN.)
END
