HEADER STRUCTURAL PROTEIN 14-MAY-01 1H4R
TITLE CRYSTAL STRUCTURE OF THE FERM DOMAIN OF MERLIN, THE NEUROFIBROMATOSIS
TITLE 2 2 TUMOR SUPPRESSOR PROTEIN.
CAVEAT 1H4R THERE ARE CHIRALITY ERRORS IN C-ALPHA CENTERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MERLIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: FERM DOMAIN RESIDUES 1-313;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: GATEWAY PDEST15;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHGM313;
SOURCE 10 OTHER_DETAILS: RECOMBINANTLY EXPRESSED IN BL21-RIL CELLS AS A HEXA-
SOURCE 11 HISTIDINE AND GST TAGGED PROTEIN. THE TAG WAS REMOVED BY RTEV
SOURCE 12 CLEAVAGE.
KEYWDS FERM, NEUROFIBROMATOSIS, NF2, STRUCTURAL PROTEIN, CYTOSKELETON, ANTI-
KEYWDS 2 ONCOGENE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.COOPER,B.S.KANG,P.SHEFFIELD,Y.DEVEDJIEV,Z.S.DEREWENDA
REVDAT 5 13-DEC-23 1H4R 1 REMARK
REVDAT 4 15-MAY-19 1H4R 1 REMARK
REVDAT 3 24-FEB-09 1H4R 1 VERSN
REVDAT 2 28-FEB-02 1H4R 1 JRNL
REVDAT 1 16-JAN-02 1H4R 0
JRNL AUTH B.S.KANG,D.R.COOPER,Y.DEVEDJIEV,U.DEREWENDA,Z.S.DEREWENDA
JRNL TITL THE STRUCTURE OF THE FERM DOMAIN OF MERLIN, THE
JRNL TITL 2 NEUROFIBROMATOSIS TYPE 2 GENE PRODUCT.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 58 381 2002
JRNL REFN ISSN 0907-4449
JRNL PMID 11856822
JRNL DOI 10.1107/S0907444901021175
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0.36
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 66303
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.500
REMARK 3 FREE R VALUE TEST SET COUNT : 985
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4917
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4912
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 861
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.130
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.675
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5040 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4555 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6803 ; 1.390 ; 1.960
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 10620 ; 0.759 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 726 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5465 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1050 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1069 ; 0.225 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4442 ; 0.209 ; 0.300
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): 687 ; 0.239 ; 0.500
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): 28 ; 0.251 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 73 ; 0.244 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 55 ; 0.346 ; 0.500
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): 2940 ; 0.805 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4759 ; 1.510 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2100 ; 2.220 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2044 ; 3.706 ; 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 : BABINET MODEL PLUS 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 1H4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1290008033.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .9200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68182
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.66200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.330
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GC6.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN WAS CRYSTALLIZED USING
REMARK 280 HANGING-DROP VAPOR DIFFUSION WIHTH 56% AMMONIUM SULFATE, 2%
REMARK 280 DIOXANE, 100 MM CACODYLATE, PH 6.5. A 1:1 RATIO OF PROTEIN TO
REMARK 280 WELL SOLUTION WAS USED., PH 6.50, VAPOR DIFFUSION, HANGING DROP
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 43.50900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.38200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.66400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.38200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.50900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.66400
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ACTS AS A MEMBRANE STABILIZING PROTEIN.
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 -1
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLY A 3
REMARK 465 ALA A 4
REMARK 465 ILE A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 ARG A 8
REMARK 465 MET A 9
REMARK 465 SER A 10
REMARK 465 PHE A 11
REMARK 465 SER A 12
REMARK 465 SER A 13
REMARK 465 LEU A 14
REMARK 465 LYS A 15
REMARK 465 ARG A 16
REMARK 465 LYS A 17
REMARK 465 GLN A 18
REMARK 465 PRO A 19
REMARK 465 GLY B -1
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLY B 3
REMARK 465 ALA B 4
REMARK 465 ILE B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 ARG B 8
REMARK 465 MET B 9
REMARK 465 SER B 10
REMARK 465 PHE B 11
REMARK 465 SER B 12
REMARK 465 SER B 13
REMARK 465 LEU B 14
REMARK 465 LYS B 15
REMARK 465 ARG B 16
REMARK 465 LYS B 17
REMARK 465 GLN B 18
REMARK 465 PRO B 19
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 20 CG CD CE NZ
REMARK 480 ARG A 160 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 20 CG CD CE NZ
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 CE LYS A 20 O HOH A 2004 0.27
REMARK 500 CD LYS A 20 O HOH A 2004 1.32
REMARK 500 NZ LYS A 20 O HOH A 2004 1.68
REMARK 500 O HOH A 2333 O HOH B 2147 1.86
REMARK 500 O HOH A 2244 O HOH A 2245 1.86
REMARK 500 O HOH A 2109 O HOH A 2110 1.89
REMARK 500 O HOH A 2390 O HOH A 2395 1.92
REMARK 500 O HOH B 2172 O HOH B 2312 1.98
REMARK 500 O HOH A 2008 O HOH A 2039 2.02
REMARK 500 O HOH A 2147 O HOH B 2139 2.03
REMARK 500 OE1 GLU B 215 O HOH B 2307 2.06
REMARK 500 O HOH A 2167 O HOH A 2320 2.07
REMARK 500 O HOH B 2069 O HOH B 2146 2.08
REMARK 500 O HOH B 2109 O HOH B 2110 2.08
REMARK 500 O HOH A 2297 O HOH B 2139 2.08
REMARK 500 O HOH B 2080 O HOH B 2304 2.09
REMARK 500 O HOH B 2112 O HOH B 2130 2.10
REMARK 500 N LYS A 20 O HOH A 2002 2.12
REMARK 500 OE2 GLU A 38 O HOH A 2043 2.12
REMARK 500 O HOH B 2202 O HOH B 2292 2.13
REMARK 500 O HOH A 2165 O HOH A 2318 2.14
REMARK 500 NZ LYS B 79 O ASP B 83 2.15
REMARK 500 O TYR A 266 O HOH A 2397 2.16
REMARK 500 OE1 GLN A 115 O HOH A 2216 2.17
REMARK 500 O HOH B 2402 O HOH B 2403 2.17
REMARK 500 O HOH B 2187 O HOH B 2346 2.17
REMARK 500 O HOH B 2106 O HOH B 2316 2.18
REMARK 500 O HOH B 2038 O HOH B 2075 2.18
REMARK 500 O HOH A 2002 O HOH A 2003 2.18
REMARK 500 O HOH A 2079 O HOH A 2146 2.19
REMARK 500 O HOH A 2405 O HOH A 2407 2.19
REMARK 500 O HOH B 2209 O HOH B 2392 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2419 O HOH B 2372 1455 1.57
REMARK 500 O HOH A 2401 O HOH B 2119 1455 1.83
REMARK 500 O HOH B 2075 O HOH B 2339 2664 1.95
REMARK 500 NZ LYS A 20 NH2 ARG B 198 2565 2.02
REMARK 500 NZ LYS A 20 NH1 ARG B 198 2565 2.10
REMARK 500 CD LYS B 20 O HOH A 2158 2664 2.10
REMARK 500 O HOH A 2033 O HOH A 2382 2565 2.11
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 ASP A 70 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP B 268 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ALA B 313 N - CA - C ANGL. DEV. = 20.6 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 LYS A 69 -127.36 59.48
REMARK 500 ASP A 268 -128.27 78.19
REMARK 500 LYS B 69 -128.02 63.97
REMARK 500 GLN B 178 68.25 -105.52
REMARK 500 ASP B 268 -141.20 68.00
REMARK 500 LYS B 312 -171.09 165.45
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 A2023 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A2024 DISTANCE = 7.61 ANGSTROMS
REMARK 525 HOH A2059 DISTANCE = 7.84 ANGSTROMS
REMARK 525 HOH A2063 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A2080 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A2087 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A2092 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A2105 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A2108 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH A2155 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A2169 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A2182 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B2016 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B2027 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH B2084 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH B2090 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH B2148 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B2204 DISTANCE = 6.24 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1315
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL GLYCINE IS FROM RTEV CLEAVAGE.
DBREF 1H4R A -1 -1 PDB 1H4R 1H4R -1 -1
DBREF 1H4R A 1 313 UNP P35240 MERL_HUMAN 1 313
DBREF 1H4R B -1 -1 PDB 1H4R 1H4R -1 -1
DBREF 1H4R B 1 313 UNP P35240 MERL_HUMAN 1 313
SEQRES 1 A 314 GLY MET ALA GLY ALA ILE ALA SER ARG MET SER PHE SER
SEQRES 2 A 314 SER LEU LYS ARG LYS GLN PRO LYS THR PHE THR VAL ARG
SEQRES 3 A 314 ILE VAL THR MET ASP ALA GLU MET GLU PHE ASN CYS GLU
SEQRES 4 A 314 MET LYS TRP LYS GLY LYS ASP LEU PHE ASP LEU VAL CYS
SEQRES 5 A 314 ARG THR LEU GLY LEU ARG GLU THR TRP PHE PHE GLY LEU
SEQRES 6 A 314 GLN TYR THR ILE LYS ASP THR VAL ALA TRP LEU LYS MET
SEQRES 7 A 314 ASP LYS LYS VAL LEU ASP HIS ASP VAL SER LYS GLU GLU
SEQRES 8 A 314 PRO VAL THR PHE HIS PHE LEU ALA LYS PHE TYR PRO GLU
SEQRES 9 A 314 ASN ALA GLU GLU GLU LEU VAL GLN GLU ILE THR GLN HIS
SEQRES 10 A 314 LEU PHE PHE LEU GLN VAL LYS LYS GLN ILE LEU ASP GLU
SEQRES 11 A 314 LYS ILE TYR CYS PRO PRO GLU ALA SER VAL LEU LEU ALA
SEQRES 12 A 314 SER TYR ALA VAL GLN ALA LYS TYR GLY ASP TYR ASP PRO
SEQRES 13 A 314 SER VAL HIS LYS ARG GLY PHE LEU ALA GLN GLU GLU LEU
SEQRES 14 A 314 LEU PRO LYS ARG VAL ILE ASN LEU TYR GLN MET THR PRO
SEQRES 15 A 314 GLU MET TRP GLU GLU ARG ILE THR ALA TRP TYR ALA GLU
SEQRES 16 A 314 HIS ARG GLY ARG ALA ARG ASP GLU ALA GLU MET GLU TYR
SEQRES 17 A 314 LEU LYS ILE ALA GLN ASP LEU GLU MET TYR GLY VAL ASN
SEQRES 18 A 314 TYR PHE ALA ILE ARG ASN LYS LYS GLY THR GLU LEU LEU
SEQRES 19 A 314 LEU GLY VAL ASP ALA LEU GLY LEU HIS ILE TYR ASP PRO
SEQRES 20 A 314 GLU ASN ARG LEU THR PRO LYS ILE SER PHE PRO TRP ASN
SEQRES 21 A 314 GLU ILE ARG ASN ILE SER TYR SER ASP LYS GLU PHE THR
SEQRES 22 A 314 ILE LYS PRO LEU ASP LYS LYS ILE ASP VAL PHE LYS PHE
SEQRES 23 A 314 ASN SER SER LYS LEU ARG VAL ASN LYS LEU ILE LEU GLN
SEQRES 24 A 314 LEU CYS ILE GLY ASN HIS ASP LEU PHE MET ARG ARG ARG
SEQRES 25 A 314 LYS ALA
SEQRES 1 B 314 GLY MET ALA GLY ALA ILE ALA SER ARG MET SER PHE SER
SEQRES 2 B 314 SER LEU LYS ARG LYS GLN PRO LYS THR PHE THR VAL ARG
SEQRES 3 B 314 ILE VAL THR MET ASP ALA GLU MET GLU PHE ASN CYS GLU
SEQRES 4 B 314 MET LYS TRP LYS GLY LYS ASP LEU PHE ASP LEU VAL CYS
SEQRES 5 B 314 ARG THR LEU GLY LEU ARG GLU THR TRP PHE PHE GLY LEU
SEQRES 6 B 314 GLN TYR THR ILE LYS ASP THR VAL ALA TRP LEU LYS MET
SEQRES 7 B 314 ASP LYS LYS VAL LEU ASP HIS ASP VAL SER LYS GLU GLU
SEQRES 8 B 314 PRO VAL THR PHE HIS PHE LEU ALA LYS PHE TYR PRO GLU
SEQRES 9 B 314 ASN ALA GLU GLU GLU LEU VAL GLN GLU ILE THR GLN HIS
SEQRES 10 B 314 LEU PHE PHE LEU GLN VAL LYS LYS GLN ILE LEU ASP GLU
SEQRES 11 B 314 LYS ILE TYR CYS PRO PRO GLU ALA SER VAL LEU LEU ALA
SEQRES 12 B 314 SER TYR ALA VAL GLN ALA LYS TYR GLY ASP TYR ASP PRO
SEQRES 13 B 314 SER VAL HIS LYS ARG GLY PHE LEU ALA GLN GLU GLU LEU
SEQRES 14 B 314 LEU PRO LYS ARG VAL ILE ASN LEU TYR GLN MET THR PRO
SEQRES 15 B 314 GLU MET TRP GLU GLU ARG ILE THR ALA TRP TYR ALA GLU
SEQRES 16 B 314 HIS ARG GLY ARG ALA ARG ASP GLU ALA GLU MET GLU TYR
SEQRES 17 B 314 LEU LYS ILE ALA GLN ASP LEU GLU MET TYR GLY VAL ASN
SEQRES 18 B 314 TYR PHE ALA ILE ARG ASN LYS LYS GLY THR GLU LEU LEU
SEQRES 19 B 314 LEU GLY VAL ASP ALA LEU GLY LEU HIS ILE TYR ASP PRO
SEQRES 20 B 314 GLU ASN ARG LEU THR PRO LYS ILE SER PHE PRO TRP ASN
SEQRES 21 B 314 GLU ILE ARG ASN ILE SER TYR SER ASP LYS GLU PHE THR
SEQRES 22 B 314 ILE LYS PRO LEU ASP LYS LYS ILE ASP VAL PHE LYS PHE
SEQRES 23 B 314 ASN SER SER LYS LEU ARG VAL ASN LYS LEU ILE LEU GLN
SEQRES 24 B 314 LEU CYS ILE GLY ASN HIS ASP LEU PHE MET ARG ARG ARG
SEQRES 25 B 314 LYS ALA
HET SO4 A1314 5
HET SO4 A1315 5
HET SO4 A1316 5
HET SO4 A1317 5
HET SO4 B1314 5
HET SO4 B1315 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 9 HOH *861(H2 O)
HELIX 1 1 LYS A 42 GLY A 55 1 14
HELIX 2 2 GLU A 58 TRP A 60 5 3
HELIX 3 3 VAL A 81 HIS A 84 5 4
HELIX 4 4 ASN A 104 LEU A 109 1 6
HELIX 5 5 GLN A 111 ASP A 128 1 18
HELIX 6 6 PRO A 134 GLY A 151 1 18
HELIX 7 7 PRO A 170 ASN A 175 1 6
HELIX 8 8 THR A 180 GLU A 194 1 15
HELIX 9 9 ALA A 199 GLN A 212 1 14
HELIX 10 10 LYS A 289 ARG A 311 1 23
HELIX 11 11 LYS B 42 GLY B 55 1 14
HELIX 12 12 GLU B 58 TRP B 60 5 3
HELIX 13 13 VAL B 81 HIS B 84 5 4
HELIX 14 14 ASN B 104 LEU B 109 1 6
HELIX 15 15 GLN B 111 ASP B 128 1 18
HELIX 16 16 PRO B 134 GLY B 151 1 18
HELIX 17 17 PRO B 170 TYR B 177 1 8
HELIX 18 18 THR B 180 GLU B 194 1 15
HELIX 19 19 ALA B 199 GLN B 212 1 14
HELIX 20 20 LYS B 289 LYS B 312 1 24
SHEET 1 AA 5 GLU A 32 GLU A 38 0
SHEET 2 AA 5 THR A 21 VAL A 27 -1 O PHE A 22 N CYS A 37
SHEET 3 AA 5 VAL A 92 ALA A 98 1 O VAL A 92 N ARG A 25
SHEET 4 AA 5 PHE A 62 ILE A 68 -1 O GLY A 63 N LEU A 97
SHEET 5 AA 5 THR A 71 TRP A 74 -1 O THR A 71 N ILE A 68
SHEET 1 AB 7 ILE A 254 PRO A 257 0
SHEET 2 AB 7 GLY A 240 TYR A 244 -1 O LEU A 241 N PHE A 256
SHEET 3 AB 7 GLU A 231 VAL A 236 -1 O LEU A 233 N TYR A 244
SHEET 4 AB 7 ASN A 220 ASN A 226 -1 O ASN A 220 N VAL A 236
SHEET 5 AB 7 PHE A 283 ASN A 286 -1 O ASN A 286 N ARG A 225
SHEET 6 AB 7 GLU A 270 PRO A 275 -1 O PHE A 271 N PHE A 285
SHEET 7 AB 7 ILE A 261 SER A 267 -1 N ARG A 262 O LYS A 274
SHEET 1 BA 5 GLU B 32 GLU B 38 0
SHEET 2 BA 5 THR B 21 VAL B 27 -1 O PHE B 22 N CYS B 37
SHEET 3 BA 5 VAL B 92 ALA B 98 1 O VAL B 92 N ARG B 25
SHEET 4 BA 5 PHE B 62 ILE B 68 -1 O GLY B 63 N LEU B 97
SHEET 5 BA 5 THR B 71 TRP B 74 -1 O THR B 71 N ILE B 68
SHEET 1 BB 7 ILE B 254 PRO B 257 0
SHEET 2 BB 7 GLY B 240 TYR B 244 -1 O LEU B 241 N PHE B 256
SHEET 3 BB 7 GLU B 231 VAL B 236 -1 O LEU B 233 N TYR B 244
SHEET 4 BB 7 ASN B 220 ASN B 226 -1 O ASN B 220 N VAL B 236
SHEET 5 BB 7 PHE B 283 ASN B 286 -1 O ASN B 286 N ARG B 225
SHEET 6 BB 7 GLU B 270 PRO B 275 -1 O PHE B 271 N PHE B 285
SHEET 7 BB 7 ILE B 261 SER B 267 -1 N ARG B 262 O LYS B 274
CISPEP 1 GLU A 90 PRO A 91 0 -0.37
CISPEP 2 GLU B 90 PRO B 91 0 0.12
SITE 1 AC1 5 ASP A 237 HIS A 242 TYR A 244 HOH A2439
SITE 2 AC1 5 HOH A2440
SITE 1 AC2 6 TYR A 144 GLU A 194 HIS A 195 ARG A 198
SITE 2 AC2 6 HOH A2441 HOH A2442
SITE 1 AC3 6 TYR A 132 ARG A 172 HOH A2443 HOH A2444
SITE 2 AC3 6 ALA B 313 HOH B2415
SITE 1 AC4 4 LYS A 40 LYS A 80 GLY B 151 ASP B 152
SITE 1 AC5 5 TYR B 144 GLU B 194 HIS B 195 ARG B 198
SITE 2 AC5 5 HOH B2416
SITE 1 AC6 5 GLY A 151 ASP A 152 LYS B 40 LYS B 80
SITE 2 AC6 5 HOH B2417
CRYST1 87.018 89.328 96.764 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 0.011492 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011195 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010334 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
