HEADER SIGNALING PROTEIN 25-JUL-12 4GAI
TITLE CRYSTAL STRUCTURE OF EBI-005, A CHIMERA OF HUMAN IL-1BETA AND IL-1RA
CAVEAT 4GAI CHIRALITY DEVIATION FOR THE FOLLOWING RESIDUE OF CHAIN A:
CAVEAT 2 4GAI THR 134 CB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EBI-005;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IL-1BETA, IL-1RA, IL-1R1, IL-1 SIGNALING, BETA-TREFOIL, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HOU,S.A.TOWNSON,J.T.KOVALCHIN,A.MASCI,O.KINER,Y.SHU,B.KING,
AUTHOR 2 C.THOMAS,K.C.GARCIA,E.S.FURFINE,T.M.BARNES
REVDAT 4 28-FEB-24 4GAI 1 REMARK
REVDAT 3 15-NOV-17 4GAI 1 REMARK
REVDAT 2 27-MAR-13 4GAI 1 JRNL
REVDAT 1 20-FEB-13 4GAI 0
JRNL AUTH J.HOU,S.A.TOWNSON,J.T.KOVALCHIN,A.MASCI,O.KINER,Y.SHU,
JRNL AUTH 2 B.M.KING,E.SCHIRMER,K.GOLDEN,C.THOMAS,K.C.GARCIA,
JRNL AUTH 3 G.ZARBIS-PAPASTOITSIS,E.S.FURFINE,T.M.BARNES
JRNL TITL DESIGN OF A SUPERIOR CYTOKINE ANTAGONIST FOR TOPICAL
JRNL TITL 2 OPHTHALMIC USE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 3913 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23431173
JRNL DOI 10.1073/PNAS.1217996110
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 51814
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2638
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3512
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 202
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2385
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 354
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38000
REMARK 3 B22 (A**2) : 1.60000
REMARK 3 B33 (A**2) : -1.22000
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): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.490
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2557 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3478 ; 1.342 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 325 ; 6.810 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 124 ;34.947 ;25.968
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 496 ;14.029 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;14.209 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 381 ; 0.258 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1936 ; 0.004 ; 0.021
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): 1529 ; 1.211 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2510 ; 1.990 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1028 ; 3.055 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 951 ; 4.928 ; 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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 152
REMARK 3 RESIDUE RANGE : A 201 A 412
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1400 -16.7340 -11.5590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0212 T22: 0.0079
REMARK 3 T33: 0.0264 T12: 0.0097
REMARK 3 T13: 0.0083 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 2.1284 L22: 1.7273
REMARK 3 L33: 2.6645 L12: -0.4005
REMARK 3 L13: 0.1743 L23: 0.1704
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: -0.0032 S13: -0.0071
REMARK 3 S21: -0.0856 S22: -0.0203 S23: 0.0262
REMARK 3 S31: 0.0239 S32: -0.0597 S33: -0.0116
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 151
REMARK 3 RESIDUE RANGE : B 201 B 342
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7990 -16.3960 -39.6150
REMARK 3 T TENSOR
REMARK 3 T11: 0.1098 T22: 0.0786
REMARK 3 T33: 0.0407 T12: 0.0237
REMARK 3 T13: 0.0204 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 2.5142 L22: 1.7936
REMARK 3 L33: 3.7067 L12: -0.6178
REMARK 3 L13: 0.7278 L23: 0.0542
REMARK 3 S TENSOR
REMARK 3 S11: 0.0451 S12: 0.2829 S13: 0.0327
REMARK 3 S21: -0.2010 S22: -0.0667 S23: 0.0136
REMARK 3 S31: -0.0115 S32: 0.1585 S33: 0.0217
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 4GAI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073943.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-11
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 : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51907
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.58200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 200 MM MGCL2, 100 MM
REMARK 280 HEPES, PH 7.5, 0.5% W/V N-DODECY- -D-MALTOSIDE (DDM), VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 108.13300
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 108.13300
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 21.69600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.45500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.69600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.45500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 108.13300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.69600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 33.45500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 108.13300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.69600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 33.45500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 SER A 153
REMARK 465 GLY B 48
REMARK 465 GLU B 49
REMARK 465 GLU B 50
REMARK 465 SER B 51
REMARK 465 ASN B 52
REMARK 465 ASP B 53
REMARK 465 LYS B 54
REMARK 465 ASP B 138
REMARK 465 GLU B 139
REMARK 465 GLY B 140
REMARK 465 VAL B 141
REMARK 465 SER B 152
REMARK 465 SER B 153
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 228 O HOH A 406 1.94
REMARK 500 O HOH A 388 O HOH A 398 2.03
REMARK 500 O HOH B 325 O HOH B 336 2.11
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 MET A 94 CG MET A 94 SD -0.175
REMARK 500 GLU A 95 CG GLU A 95 CD 0.162
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 ASN A 22 43.57 36.50
REMARK 500 ASN B 107 -2.50 77.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GAF RELATED DB: PDB
DBREF 4GAI A 1 153 PDB 4GAI 4GAI 1 153
DBREF 4GAI B 1 153 PDB 4GAI 4GAI 1 153
SEQRES 1 A 153 ALA PRO VAL ARG SER LEU ASN CYS ARG ILE TRP ASP VAL
SEQRES 2 A 153 ASN GLN LYS THR PHE TYR LEU ARG ASN ASN GLN LEU VAL
SEQRES 3 A 153 ALA GLY TYR LEU GLN GLY PRO ASN VAL ASN LEU GLU GLU
SEQRES 4 A 153 LYS PHE SER MET SER PHE VAL GLN GLY GLU GLU SER ASN
SEQRES 5 A 153 ASP LYS ILE PRO VAL ALA LEU GLY LEU LYS GLU LYS ASN
SEQRES 6 A 153 LEU TYR LEU SER CYS VAL LEU LYS ASP ASP LYS PRO THR
SEQRES 7 A 153 LEU GLN LEU GLU SER VAL ASP PRO LYS ASN TYR PRO LYS
SEQRES 8 A 153 LYS LYS MET GLU LYS ARG PHE VAL PHE ASN LYS ILE GLU
SEQRES 9 A 153 ILE ASN ASN LYS LEU GLU PHE GLU SER ALA GLN PHE PRO
SEQRES 10 A 153 ASN TRP PHE LEU CYS THR ALA MET GLU ALA ASP GLN PRO
SEQRES 11 A 153 VAL SER LEU THR ASN MET PRO ASP GLU GLY VAL MET VAL
SEQRES 12 A 153 THR LYS PHE TYR MET GLN PHE VAL SER SER
SEQRES 1 B 153 ALA PRO VAL ARG SER LEU ASN CYS ARG ILE TRP ASP VAL
SEQRES 2 B 153 ASN GLN LYS THR PHE TYR LEU ARG ASN ASN GLN LEU VAL
SEQRES 3 B 153 ALA GLY TYR LEU GLN GLY PRO ASN VAL ASN LEU GLU GLU
SEQRES 4 B 153 LYS PHE SER MET SER PHE VAL GLN GLY GLU GLU SER ASN
SEQRES 5 B 153 ASP LYS ILE PRO VAL ALA LEU GLY LEU LYS GLU LYS ASN
SEQRES 6 B 153 LEU TYR LEU SER CYS VAL LEU LYS ASP ASP LYS PRO THR
SEQRES 7 B 153 LEU GLN LEU GLU SER VAL ASP PRO LYS ASN TYR PRO LYS
SEQRES 8 B 153 LYS LYS MET GLU LYS ARG PHE VAL PHE ASN LYS ILE GLU
SEQRES 9 B 153 ILE ASN ASN LYS LEU GLU PHE GLU SER ALA GLN PHE PRO
SEQRES 10 B 153 ASN TRP PHE LEU CYS THR ALA MET GLU ALA ASP GLN PRO
SEQRES 11 B 153 VAL SER LEU THR ASN MET PRO ASP GLU GLY VAL MET VAL
SEQRES 12 B 153 THR LYS PHE TYR MET GLN PHE VAL SER SER
FORMUL 3 HOH *354(H2 O)
HELIX 1 1 GLN A 31 GLU A 38 5 8
HELIX 2 2 GLU A 95 PHE A 98 5 4
HELIX 3 3 GLN B 31 GLU B 38 5 8
HELIX 4 4 GLU B 95 ARG B 97 5 3
SHEET 1 A 7 SER A 5 ASP A 12 0
SHEET 2 A 7 PHE A 41 PHE A 45 -1 O PHE A 41 N CYS A 8
SHEET 3 A 7 ILE A 55 LEU A 61 -1 O GLY A 60 N SER A 42
SHEET 4 A 7 PHE A 100 ILE A 105 -1 O PHE A 100 N VAL A 57
SHEET 5 A 7 LYS A 108 SER A 113 -1 O GLU A 112 N ASN A 101
SHEET 6 A 7 PHE A 146 PHE A 150 -1 O PHE A 146 N LEU A 109
SHEET 7 A 7 SER A 5 ASP A 12 -1 N TRP A 11 O TYR A 147
SHEET 1 B 3 THR A 17 ARG A 21 0
SHEET 2 B 3 GLN A 24 GLY A 28 -1 O GLN A 24 N ARG A 21
SHEET 3 B 3 GLN A 129 PRO A 130 -1 O GLN A 129 N ALA A 27
SHEET 1 C 2 LEU A 66 LYS A 73 0
SHEET 2 C 2 LYS A 76 SER A 83 -1 O GLU A 82 N TYR A 67
SHEET 1 D 2 PHE A 120 CYS A 122 0
SHEET 2 D 2 SER A 132 THR A 134 -1 O SER A 132 N CYS A 122
SHEET 1 E 7 ARG B 4 ASP B 12 0
SHEET 2 E 7 PHE B 41 PHE B 45 -1 O MET B 43 N LEU B 6
SHEET 3 E 7 PRO B 56 LEU B 61 -1 O GLY B 60 N SER B 42
SHEET 4 E 7 VAL B 99 ILE B 105 -1 O PHE B 100 N VAL B 57
SHEET 5 E 7 LYS B 108 SER B 113 -1 O GLU B 112 N ASN B 101
SHEET 6 E 7 PHE B 146 PHE B 150 -1 O PHE B 146 N LEU B 109
SHEET 7 E 7 ARG B 4 ASP B 12 -1 N TRP B 11 O TYR B 147
SHEET 1 F 3 THR B 17 ARG B 21 0
SHEET 2 F 3 GLN B 24 GLY B 28 -1 O VAL B 26 N TYR B 19
SHEET 3 F 3 GLN B 129 PRO B 130 -1 O GLN B 129 N ALA B 27
SHEET 1 G 2 LEU B 66 LYS B 73 0
SHEET 2 G 2 LYS B 76 SER B 83 -1 O THR B 78 N VAL B 71
SHEET 1 H 2 PHE B 120 CYS B 122 0
SHEET 2 H 2 SER B 132 THR B 134 -1 O THR B 134 N PHE B 120
CISPEP 1 TYR A 89 PRO A 90 0 -2.99
CISPEP 2 TYR B 89 PRO B 90 0 -1.78
CRYST1 43.392 66.910 216.266 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 0.023046 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014945 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004624 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
