HEADER HYDROLASE/HYDROLASE INHIBITOR 21-JUL-11 3T11
TITLE DIMERIC INHIBITOR OF HIV-1 PROTEASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 PROTEASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 501-599;
COMPND 5 SYNONYM: PR, RETROPEPSIN;
COMPND 6 EC: 3.4.23.16;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11676;
SOURCE 5 GENE: GAG-POL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS HIV-1 PROTEASE, BETA BAREL, RETROVIRAL ASPARTYL PROTEASE, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BRYNDA,P.REZACOVA,G.K.SASKOVA,M.KOZISEK,J.KONVALINKA
REVDAT 3 13-SEP-23 3T11 1 REMARK
REVDAT 2 08-NOV-17 3T11 1 REMARK
REVDAT 1 22-AUG-12 3T11 0
JRNL AUTH J.BRYNDA,P.REZACOVA,G.K.SASKOVA,M.KOZISEK,J.KONVALINKA
JRNL TITL DIMERIC INHIBITOR OF HIV-1 PROTEASE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 9197
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 466
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) : 2.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 601
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1508
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 0.25000
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): 0.336
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.247
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.190
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.723
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1632 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2225 ; 1.684 ; 2.035
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 204 ; 6.859 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 55 ;41.167 ;25.273
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 289 ;14.445 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;11.070 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 258 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1191 ; 0.009 ; 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): 988 ; 0.791 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1610 ; 1.444 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 644 ; 2.158 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 611 ; 3.181 ; 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 1 A 99 4
REMARK 3 1 B 1 B 99 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 745 ; 0.630 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 745 ; 0.980 ; 2.000
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 1 C 1 4
REMARK 3 1 D 1 D 1 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 32 ; 0.060 ; 0.500
REMARK 3 MEDIUM THERMAL 2 B (A**2): 32 ; 1.300 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 9
REMARK 3 RESIDUE RANGE : A 86 A 99
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1270 -8.3410 14.8300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0948 T22: 0.0640
REMARK 3 T33: 0.0161 T12: 0.0250
REMARK 3 T13: -0.0231 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.1123 L22: 1.5364
REMARK 3 L33: 1.3827 L12: 0.1093
REMARK 3 L13: -0.4245 L23: -0.6047
REMARK 3 S TENSOR
REMARK 3 S11: 0.1455 S12: 0.0809 S13: 0.0363
REMARK 3 S21: -0.1088 S22: -0.0436 S23: 0.1064
REMARK 3 S31: 0.1836 S32: -0.0535 S33: -0.1019
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 : A 10 A 32
REMARK 3 RESIDUE RANGE : A 63 A 85
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3450 -2.5450 5.1850
REMARK 3 T TENSOR
REMARK 3 T11: 0.0798 T22: 0.0624
REMARK 3 T33: 0.0577 T12: 0.0245
REMARK 3 T13: 0.0095 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0192 L22: 1.5497
REMARK 3 L33: 2.5247 L12: -0.0315
REMARK 3 L13: 0.1744 L23: -1.3294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: 0.0079 S13: 0.0193
REMARK 3 S21: -0.1425 S22: -0.1164 S23: 0.0680
REMARK 3 S31: 0.1620 S32: 0.0958 S33: 0.0896
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 33 A 62
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2210 9.5870 2.8650
REMARK 3 T TENSOR
REMARK 3 T11: 0.1036 T22: 0.0802
REMARK 3 T33: 0.0224 T12: -0.0162
REMARK 3 T13: 0.0141 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 1.6119 L22: 1.0025
REMARK 3 L33: 2.6010 L12: -1.2708
REMARK 3 L13: 2.0463 L23: -1.6133
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: 0.1083 S13: 0.0591
REMARK 3 S21: -0.0223 S22: -0.0902 S23: -0.0466
REMARK 3 S31: 0.0223 S32: 0.1527 S33: 0.0758
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 9
REMARK 3 RESIDUE RANGE : B 86 B 99
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7490 -5.9920 20.2000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0829 T22: 0.0655
REMARK 3 T33: 0.0709 T12: 0.0383
REMARK 3 T13: -0.0049 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.4834 L22: 1.7967
REMARK 3 L33: 1.6917 L12: 0.4797
REMARK 3 L13: -0.0761 L23: -1.5641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0828 S12: -0.0196 S13: 0.0209
REMARK 3 S21: 0.0379 S22: 0.1431 S23: 0.2265
REMARK 3 S31: 0.0361 S32: -0.1577 S33: -0.2258
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 10 B 32
REMARK 3 RESIDUE RANGE : B 63 B 85
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7880 -1.4470 30.5290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0692 T22: 0.1045
REMARK 3 T33: 0.0195 T12: -0.0099
REMARK 3 T13: 0.0248 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.7564 L22: 1.9403
REMARK 3 L33: 0.4936 L12: 0.3528
REMARK 3 L13: 0.3538 L23: -0.1932
REMARK 3 S TENSOR
REMARK 3 S11: 0.0202 S12: -0.0580 S13: 0.0113
REMARK 3 S21: 0.1263 S22: 0.0331 S23: 0.0671
REMARK 3 S31: -0.0943 S32: -0.0451 S33: -0.0533
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 33 B 62
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5850 1.6540 33.9680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1261 T22: 0.0698
REMARK 3 T33: 0.0077 T12: -0.0564
REMARK 3 T13: -0.0151 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 2.9469 L22: 1.5237
REMARK 3 L33: 1.4403 L12: 0.5729
REMARK 3 L13: -0.7789 L23: -1.4714
REMARK 3 S TENSOR
REMARK 3 S11: 0.1972 S12: -0.1752 S13: -0.1003
REMARK 3 S21: 0.2494 S22: -0.2615 S23: -0.0747
REMARK 3 S31: -0.2498 S32: 0.2405 S33: 0.0643
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: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3T11 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000066901.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : CU FINE FOCUS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GOEBEL MIRRORS
REMARK 200 OPTICS : GOEBEL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : MAR345
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9704
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220
REMARK 200 RESOLUTION RANGE LOW (A) : 38.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : 0.51000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1U8G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 15.37750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.26200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.61050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.26200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 15.37750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.61050
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 43 CD CE NZ
REMARK 470 ARG B 41 CZ NH1 NH2
REMARK 470 LYS B 43 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 GLU A 34 152.45 -45.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 BME A 103
REMARK 610 BME B 102
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3T1 A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3T1 B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 102
DBREF 3T11 A 1 99 UNP P03367 POL_HV1BR 501 599
DBREF 3T11 B 1 99 UNP P03367 POL_HV1BR 501 599
SEQRES 1 A 99 PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE
SEQRES 2 A 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR
SEQRES 3 A 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO
SEQRES 4 A 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY
SEQRES 5 A 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU
SEQRES 6 A 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY
SEQRES 7 A 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR
SEQRES 8 A 99 GLN ILE GLY CYS THR LEU ASN PHE
SEQRES 1 B 99 PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE
SEQRES 2 B 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR
SEQRES 3 B 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO
SEQRES 4 B 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY
SEQRES 5 B 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU
SEQRES 6 B 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY
SEQRES 7 B 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR
SEQRES 8 B 99 GLN ILE GLY CYS THR LEU ASN PHE
HET 3T1 A 101 32
HET CL A 102 1
HET BME A 103 1
HET 3T1 B 101 32
HET BME B 102 1
HETNAM 3T1 (3S,11S)-11-(3-CHLORO-4-HYDROXY-5-METHOXYPHENYL)-3-
HETNAM 2 3T1 PHENYL-2,3,4,5,10,11-HEXAHYDRO-1H-DIBENZO[B,E][1,
HETNAM 3 3T1 4]DIAZEPIN-1-ONE
HETNAM CL CHLORIDE ION
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 3 3T1 2(C26 H23 CL N2 O3)
FORMUL 4 CL CL 1-
FORMUL 5 BME 2(C2 H6 O S)
FORMUL 8 HOH *71(H2 O)
HELIX 1 1 GLY A 86 ILE A 93 1 8
HELIX 2 2 GLY B 86 THR B 91 1 6
HELIX 3 3 GLN B 92 GLY B 94 5 3
SHEET 1 A 4 GLN A 2 ILE A 3 0
SHEET 2 A 4 THR B 96 ASN B 98 -1 O LEU B 97 N ILE A 3
SHEET 3 A 4 THR A 96 ASN A 98 -1 N THR A 96 O ASN B 98
SHEET 4 A 4 GLN B 2 THR B 4 -1 O ILE B 3 N LEU A 97
SHEET 1 B 8 LYS A 43 GLY A 49 0
SHEET 2 B 8 GLY A 52 ILE A 66 -1 O GLN A 58 N LYS A 43
SHEET 3 B 8 HIS A 69 VAL A 77 -1 O ALA A 71 N ILE A 64
SHEET 4 B 8 VAL A 32 LEU A 33 1 N LEU A 33 O LEU A 76
SHEET 5 B 8 ILE A 84 ILE A 85 -1 O ILE A 84 N VAL A 32
SHEET 6 B 8 GLN A 18 LEU A 24 1 N LEU A 23 O ILE A 85
SHEET 7 B 8 LEU A 10 ILE A 15 -1 N ILE A 13 O LYS A 20
SHEET 8 B 8 GLY A 52 ILE A 66 -1 O GLU A 65 N LYS A 14
SHEET 1 C 8 LYS B 43 GLY B 49 0
SHEET 2 C 8 GLY B 52 ILE B 66 -1 O GLN B 58 N LYS B 43
SHEET 3 C 8 HIS B 69 VAL B 77 -1 O VAL B 75 N TYR B 59
SHEET 4 C 8 VAL B 32 LEU B 33 1 N LEU B 33 O LEU B 76
SHEET 5 C 8 ILE B 84 ILE B 85 -1 O ILE B 84 N VAL B 32
SHEET 6 C 8 GLN B 18 LEU B 24 1 N LEU B 23 O ILE B 85
SHEET 7 C 8 LEU B 10 ILE B 15 -1 N ILE B 13 O LYS B 20
SHEET 8 C 8 GLY B 52 ILE B 66 -1 O GLU B 65 N LYS B 14
SITE 1 AC1 15 GLY A 27 ALA A 28 VAL A 32 ILE A 47
SITE 2 AC1 15 GLY A 48 PRO A 79 THR A 80 CL A 102
SITE 3 AC1 15 HOH A 201 HOH A 217 HOH A 225 ARG B 8
SITE 4 AC1 15 PRO B 81 VAL B 82 3T1 B 101
SITE 1 AC2 6 GLY A 49 ILE A 50 3T1 A 101 GLY B 49
SITE 2 AC2 6 ILE B 50 3T1 B 101
SITE 1 AC3 1 CYS A 67
SITE 1 AC4 16 ARG A 8 LEU A 23 ILE A 50 PRO A 81
SITE 2 AC4 16 VAL A 82 3T1 A 101 CL A 102 THR B 4
SITE 3 AC4 16 GLY B 27 ALA B 28 ILE B 47 GLY B 48
SITE 4 AC4 16 THR B 80 HOH B 205 HOH B 207 HOH B 220
SITE 1 AC5 1 CYS B 67
CRYST1 30.755 49.221 122.524 90.00 90.00 90.00 P 21 21 21 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 0.032515 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008162 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
