HEADER OXIDOREDUCTASE 02-DEC-98 1EQU
TITLE TYPE 1 17-BETA HYDROXYSTEROID DEHYDROGENASE EQUILIN COMPLEXED WITH
TITLE 2 NADP+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ESTRADIOL 17 BETA-DEHYDROGENASE 1);
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.62
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS HYDROXYSTEROID DEHYDROGENASE, SHORT CHAIN DEHYDROGENASE, REDUCTASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.SAWICKI,M.ERMAN,T.PURANEN,P.VIHKO,D.GHOSH
REVDAT 5 09-AUG-23 1EQU 1 REMARK LINK
REVDAT 4 24-FEB-09 1EQU 1 VERSN
REVDAT 3 01-APR-03 1EQU 1 JRNL
REVDAT 2 15-DEC-99 1EQU 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 02-DEC-99 1EQU 0
JRNL AUTH M.W.SAWICKI,M.ERMAN,T.PURANEN,P.VIHKO,D.GHOSH
JRNL TITL STRUCTURE OF THE TERNARY COMPLEX OF HUMAN
JRNL TITL 2 17BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 1 WITH
JRNL TITL 3 3-HYDROXYESTRA-1,3,5,7-TETRAEN-17-ONE (EQUILIN) AND NADP+.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 840 1999
JRNL REFN ISSN 0027-8424
JRNL PMID 9927655
JRNL DOI 10.1073/PNAS.96.3.840
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 9322
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 SET) : 0.182
REMARK 3 FREE R VALUE : 0.315
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 494
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.030
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 18
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.650
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.06
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.610
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 3.500 ; 100.00
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 2 POSITIONAL (A) : 3.500 ; 10.000
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 3 POSITIONAL (A) : 3.500 ; 5.000
REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE EXTENDED LOOP REGION OF THE B SUBUNIT (186-200) WAS
REMARK 3 MODELED AFTER THE APO STRUCTURE EXTENDED LOOP
REMARK 4
REMARK 4 1EQU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-98.
REMARK 100 THE DEPOSITION ID IS D_1000000195.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-97
REMARK 200 TEMPERATURE (KELVIN) : 130.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11408
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
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 : 1.700
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: 1BHS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAP. DIFF. FROM 28% PEG 4000 IN HEPES
REMARK 280 BUFFER, PH 7.5, CONTAINING 1 MM EQUILIN, PH 7.50
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 22.01000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.42000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.08000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.42000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.01000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.08000
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: 8170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 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 285
REMARK 465 ASP A 286
REMARK 465 VAL A 287
REMARK 465 PRO A 288
REMARK 465 ALA A 289
REMARK 465 LYS A 290
REMARK 465 ALA A 291
REMARK 465 GLU A 292
REMARK 465 ALA A 293
REMARK 465 GLY A 294
REMARK 465 ALA A 295
REMARK 465 GLU A 296
REMARK 465 ALA A 297
REMARK 465 GLY A 298
REMARK 465 GLY A 299
REMARK 465 GLY A 300
REMARK 465 ALA A 301
REMARK 465 GLY A 302
REMARK 465 PRO A 303
REMARK 465 GLY A 304
REMARK 465 ALA A 305
REMARK 465 GLU A 306
REMARK 465 ASP A 307
REMARK 465 GLU A 308
REMARK 465 ALA A 309
REMARK 465 GLY A 310
REMARK 465 ARG A 311
REMARK 465 SER A 312
REMARK 465 ALA A 313
REMARK 465 VAL A 314
REMARK 465 GLY A 315
REMARK 465 ASP A 316
REMARK 465 PRO A 317
REMARK 465 GLU A 318
REMARK 465 LEU A 319
REMARK 465 GLY A 320
REMARK 465 ASP A 321
REMARK 465 PRO A 322
REMARK 465 PRO A 323
REMARK 465 ALA A 324
REMARK 465 ALA A 325
REMARK 465 PRO A 326
REMARK 465 GLN A 327
REMARK 465 GLY B 285
REMARK 465 ASP B 286
REMARK 465 VAL B 287
REMARK 465 PRO B 288
REMARK 465 ALA B 289
REMARK 465 LYS B 290
REMARK 465 ALA B 291
REMARK 465 GLU B 292
REMARK 465 ALA B 293
REMARK 465 GLY B 294
REMARK 465 ALA B 295
REMARK 465 GLU B 296
REMARK 465 ALA B 297
REMARK 465 GLY B 298
REMARK 465 GLY B 299
REMARK 465 GLY B 300
REMARK 465 ALA B 301
REMARK 465 GLY B 302
REMARK 465 PRO B 303
REMARK 465 GLY B 304
REMARK 465 ALA B 305
REMARK 465 GLU B 306
REMARK 465 ASP B 307
REMARK 465 GLU B 308
REMARK 465 ALA B 309
REMARK 465 GLY B 310
REMARK 465 ARG B 311
REMARK 465 SER B 312
REMARK 465 ALA B 313
REMARK 465 VAL B 314
REMARK 465 GLY B 315
REMARK 465 ASP B 316
REMARK 465 PRO B 317
REMARK 465 GLU B 318
REMARK 465 LEU B 319
REMARK 465 GLY B 320
REMARK 465 ASP B 321
REMARK 465 PRO B 322
REMARK 465 PRO B 323
REMARK 465 ALA B 324
REMARK 465 ALA B 325
REMARK 465 PRO B 326
REMARK 465 GLN B 327
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 CA VAL B 188 O GLN B 231 1.92
REMARK 500 O VAL B 196 NZ LYS B 223 1.94
REMARK 500 N HIS B 189 O GLN B 231 2.00
REMARK 500 CB VAL B 188 O GLN B 231 2.12
REMARK 500 CB SER B 199 CE2 TYR B 216 2.17
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 CE1 TYR A 216 O GLY B 198 3655 1.65
REMARK 500 CD1 TYR A 216 O GLY B 198 3655 1.96
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 ASP B 205 C ARG B 206 N 0.267
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 PRO A 55 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 LEU B 62 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 CYS B 185 CA - C - N ANGL. DEV. = -20.3 DEGREES
REMARK 500 CYS B 185 O - C - N ANGL. DEV. = 13.2 DEGREES
REMARK 500 GLY B 186 C - N - CA ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASP B 205 O - C - N ANGL. DEV. = -14.4 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 THR A 3 97.28 -57.89
REMARK 500 GLN A 28 43.27 18.45
REMARK 500 LYS A 40 -15.59 -47.54
REMARK 500 CYS A 54 94.71 -54.24
REMARK 500 PRO A 55 145.00 -24.00
REMARK 500 ARG A 67 43.47 -95.59
REMARK 500 ASP A 68 103.70 -163.07
REMARK 500 ALA A 91 154.21 -47.52
REMARK 500 PHE A 151 18.82 53.26
REMARK 500 ASP A 153 -72.65 -50.56
REMARK 500 HIS A 189 87.12 -61.69
REMARK 500 GLU A 194 1.20 -57.69
REMARK 500 LYS A 195 -40.60 -149.90
REMARK 500 PRO A 200 -16.27 -48.85
REMARK 500 GLU A 228 -31.61 -155.94
REMARK 500 ALA A 229 13.11 -145.68
REMARK 500 ARG A 281 41.55 -80.02
REMARK 500 GLU A 282 -46.68 -142.46
REMARK 500 ARG B 2 -161.28 -164.37
REMARK 500 THR B 3 106.78 -59.67
REMARK 500 SER B 24 33.29 -78.87
REMARK 500 SER B 27 1.65 -64.60
REMARK 500 GLN B 28 22.22 40.93
REMARK 500 THR B 41 4.83 -62.23
REMARK 500 PRO B 55 163.96 -43.00
REMARK 500 LEU B 59 109.16 -168.20
REMARK 500 LEU B 64 127.08 -171.52
REMARK 500 VAL B 66 -0.39 -50.87
REMARK 500 THR B 80 -38.07 -31.81
REMARK 500 ALA B 91 170.70 -58.44
REMARK 500 LEU B 95 124.08 -170.22
REMARK 500 VAL B 115 -62.58 -107.04
REMARK 500 SER B 142 153.66 172.77
REMARK 500 PHE B 151 14.42 55.91
REMARK 500 GLU B 184 85.78 -57.39
REMARK 500 HIS B 189 82.87 -68.68
REMARK 500 ALA B 191 -73.49 -36.58
REMARK 500 PHE B 192 -65.07 -28.73
REMARK 500 ASP B 205 34.91 -64.75
REMARK 500 ARG B 206 27.66 -172.21
REMARK 500 ILE B 209 -30.80 -37.31
REMARK 500 ARG B 227 -10.00 -58.15
REMARK 500 PRO B 233 -37.99 -36.63
REMARK 500 ASP B 268 36.45 -74.77
REMARK 500 ALA B 278 -73.96 -49.37
REMARK 500 MET B 279 -15.22 -49.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 218 0.09 SIDE CHAIN
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 CYS B 185 -10.91
REMARK 500 ASP B 205 -20.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 328
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EQI A 329
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 328
DBREF 1EQU A 1 327 UNP P14061 DHB1_HUMAN 1 327
DBREF 1EQU B 1 327 UNP P14061 DHB1_HUMAN 1 327
SEQRES 1 A 327 ALA ARG THR VAL VAL LEU ILE THR GLY CYS SER SER GLY
SEQRES 2 A 327 ILE GLY LEU HIS LEU ALA VAL ARG LEU ALA SER ASP PRO
SEQRES 3 A 327 SER GLN SER PHE LYS VAL TYR ALA THR LEU ARG ASP LEU
SEQRES 4 A 327 LYS THR GLN GLY ARG LEU TRP GLU ALA ALA ARG ALA LEU
SEQRES 5 A 327 ALA CYS PRO PRO GLY SER LEU GLU THR LEU GLN LEU ASP
SEQRES 6 A 327 VAL ARG ASP SER LYS SER VAL ALA ALA ALA ARG GLU ARG
SEQRES 7 A 327 VAL THR GLU GLY ARG VAL ASP VAL LEU VAL CYS ASN ALA
SEQRES 8 A 327 GLY LEU GLY LEU LEU GLY PRO LEU GLU ALA LEU GLY GLU
SEQRES 9 A 327 ASP ALA VAL ALA SER VAL LEU ASP VAL ASN VAL VAL GLY
SEQRES 10 A 327 THR VAL ARG MET LEU GLN ALA PHE LEU PRO ASP MET LYS
SEQRES 11 A 327 ARG ARG GLY SER GLY ARG VAL LEU VAL THR GLY SER VAL
SEQRES 12 A 327 GLY GLY LEU MET GLY LEU PRO PHE ASN ASP VAL TYR CYS
SEQRES 13 A 327 ALA SER LYS PHE ALA LEU GLU GLY LEU CYS GLU SER LEU
SEQRES 14 A 327 ALA VAL LEU LEU LEU PRO PHE GLY VAL HIS LEU SER LEU
SEQRES 15 A 327 ILE GLU CYS GLY PRO VAL HIS THR ALA PHE MET GLU LYS
SEQRES 16 A 327 VAL LEU GLY SER PRO GLU GLU VAL LEU ASP ARG THR ASP
SEQRES 17 A 327 ILE HIS THR PHE HIS ARG PHE TYR GLN TYR LEU ALA HIS
SEQRES 18 A 327 SER LYS GLN VAL PHE ARG GLU ALA ALA GLN ASN PRO GLU
SEQRES 19 A 327 GLU VAL ALA GLU VAL PHE LEU THR ALA LEU ARG ALA PRO
SEQRES 20 A 327 LYS PRO THR LEU ARG TYR PHE THR THR GLU ARG PHE LEU
SEQRES 21 A 327 PRO LEU LEU ARG MET ARG LEU ASP ASP PRO SER GLY SER
SEQRES 22 A 327 ASN TYR VAL THR ALA MET HIS ARG GLU VAL PHE GLY ASP
SEQRES 23 A 327 VAL PRO ALA LYS ALA GLU ALA GLY ALA GLU ALA GLY GLY
SEQRES 24 A 327 GLY ALA GLY PRO GLY ALA GLU ASP GLU ALA GLY ARG SER
SEQRES 25 A 327 ALA VAL GLY ASP PRO GLU LEU GLY ASP PRO PRO ALA ALA
SEQRES 26 A 327 PRO GLN
SEQRES 1 B 327 ALA ARG THR VAL VAL LEU ILE THR GLY CYS SER SER GLY
SEQRES 2 B 327 ILE GLY LEU HIS LEU ALA VAL ARG LEU ALA SER ASP PRO
SEQRES 3 B 327 SER GLN SER PHE LYS VAL TYR ALA THR LEU ARG ASP LEU
SEQRES 4 B 327 LYS THR GLN GLY ARG LEU TRP GLU ALA ALA ARG ALA LEU
SEQRES 5 B 327 ALA CYS PRO PRO GLY SER LEU GLU THR LEU GLN LEU ASP
SEQRES 6 B 327 VAL ARG ASP SER LYS SER VAL ALA ALA ALA ARG GLU ARG
SEQRES 7 B 327 VAL THR GLU GLY ARG VAL ASP VAL LEU VAL CYS ASN ALA
SEQRES 8 B 327 GLY LEU GLY LEU LEU GLY PRO LEU GLU ALA LEU GLY GLU
SEQRES 9 B 327 ASP ALA VAL ALA SER VAL LEU ASP VAL ASN VAL VAL GLY
SEQRES 10 B 327 THR VAL ARG MET LEU GLN ALA PHE LEU PRO ASP MET LYS
SEQRES 11 B 327 ARG ARG GLY SER GLY ARG VAL LEU VAL THR GLY SER VAL
SEQRES 12 B 327 GLY GLY LEU MET GLY LEU PRO PHE ASN ASP VAL TYR CYS
SEQRES 13 B 327 ALA SER LYS PHE ALA LEU GLU GLY LEU CYS GLU SER LEU
SEQRES 14 B 327 ALA VAL LEU LEU LEU PRO PHE GLY VAL HIS LEU SER LEU
SEQRES 15 B 327 ILE GLU CYS GLY PRO VAL HIS THR ALA PHE MET GLU LYS
SEQRES 16 B 327 VAL LEU GLY SER PRO GLU GLU VAL LEU ASP ARG THR ASP
SEQRES 17 B 327 ILE HIS THR PHE HIS ARG PHE TYR GLN TYR LEU ALA HIS
SEQRES 18 B 327 SER LYS GLN VAL PHE ARG GLU ALA ALA GLN ASN PRO GLU
SEQRES 19 B 327 GLU VAL ALA GLU VAL PHE LEU THR ALA LEU ARG ALA PRO
SEQRES 20 B 327 LYS PRO THR LEU ARG TYR PHE THR THR GLU ARG PHE LEU
SEQRES 21 B 327 PRO LEU LEU ARG MET ARG LEU ASP ASP PRO SER GLY SER
SEQRES 22 B 327 ASN TYR VAL THR ALA MET HIS ARG GLU VAL PHE GLY ASP
SEQRES 23 B 327 VAL PRO ALA LYS ALA GLU ALA GLY ALA GLU ALA GLY GLY
SEQRES 24 B 327 GLY ALA GLY PRO GLY ALA GLU ASP GLU ALA GLY ARG SER
SEQRES 25 B 327 ALA VAL GLY ASP PRO GLU LEU GLY ASP PRO PRO ALA ALA
SEQRES 26 B 327 PRO GLN
HET NAP A 328 48
HET EQI A 329 20
HET NAP B 328 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM EQI EQUILIN
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 EQI C18 H20 O2
FORMUL 6 HOH *18(H2 O)
HELIX 1 1 ILE A 14 ALA A 23 1 10
HELIX 2 2 LEU A 39 THR A 41 5 3
HELIX 3 3 GLY A 43 ALA A 51 1 9
HELIX 4 4 SER A 69 GLU A 77 1 9
HELIX 5 5 LEU A 99 ALA A 101 5 3
HELIX 6 6 GLU A 104 ASN A 114 1 11
HELIX 7 7 VAL A 116 ARG A 132 1 17
HELIX 8 8 VAL A 143 GLY A 145 5 3
HELIX 9 9 ASP A 153 LEU A 173 1 21
HELIX 10 10 LEU A 174 PHE A 176 5 3
HELIX 11 11 PHE A 192 LEU A 197 1 6
HELIX 12 12 GLU A 202 ARG A 206 5 5
HELIX 13 13 ILE A 209 ALA A 229 1 21
HELIX 14 14 PRO A 233 ARG A 245 1 13
HELIX 15 15 LEU A 260 LEU A 267 1 8
HELIX 16 16 SER A 273 VAL A 283 1 11
HELIX 17 17 ILE B 14 ALA B 23 1 10
HELIX 18 18 LEU B 39 THR B 41 5 3
HELIX 19 19 GLY B 43 ALA B 51 1 9
HELIX 20 20 SER B 69 GLU B 77 1 9
HELIX 21 21 LEU B 99 ALA B 101 5 3
HELIX 22 22 GLU B 104 ASN B 114 1 11
HELIX 23 23 VAL B 116 ARG B 132 1 17
HELIX 24 24 VAL B 143 GLY B 145 5 3
HELIX 25 25 ASP B 153 LEU B 173 1 21
HELIX 26 26 LEU B 174 PHE B 176 5 3
HELIX 27 27 ALA B 191 GLU B 194 1 4
HELIX 28 28 GLU B 202 LEU B 204 5 3
HELIX 29 29 ILE B 209 ALA B 229 1 21
HELIX 30 30 PRO B 233 ARG B 245 1 13
HELIX 31 31 LEU B 260 LEU B 267 1 8
HELIX 32 32 SER B 273 VAL B 283 1 11
SHEET 1 1 7 ARG A 252 PHE A 254 0
SHEET 2 1 7 VAL A 178 CYS A 185 1 N GLU A 184 O TYR A 253
SHEET 3 1 7 GLY A 135 SER A 142 1 O VAL A 139 N ILE A 183
SHEET 4 1 7 VAL A 86 CYS A 89 1 N CYS A 89 O LEU A 138
SHEET 5 1 7 VAL A 4 ILE A 7 1 N LEU A 6 O VAL A 86
SHEET 6 1 7 LYS A 31 LEU A 36 1 N TYR A 33 O VAL A 5
SHEET 7 1 7 LEU A 59 GLN A 63 1 N GLU A 60 O VAL A 32
SHEET 1 2 7 ARG B 252 PHE B 254 0
SHEET 2 2 7 VAL B 178 CYS B 185 1 N GLU B 184 O TYR B 253
SHEET 3 2 7 GLY B 135 SER B 142 1 O VAL B 139 N ILE B 183
SHEET 4 2 7 VAL B 86 CYS B 89 1 N CYS B 89 O LEU B 138
SHEET 5 2 7 VAL B 4 ILE B 7 1 N LEU B 6 O VAL B 86
SHEET 6 2 7 LYS B 31 LEU B 36 1 N TYR B 33 O VAL B 5
SHEET 7 2 7 LEU B 59 GLN B 63 1 N GLU B 60 O VAL B 32
LINK OG1 THR A 190 O1N NAP A 328 1555 1555 2.02
LINK NH1 ARG B 37 O3X NAP B 328 1555 1555 1.88
SITE 1 AC1 21 SER A 11 SER A 12 GLY A 13 ILE A 14
SITE 2 AC1 21 ARG A 37 LEU A 64 ASP A 65 VAL A 66
SITE 3 AC1 21 ASN A 90 ALA A 91 GLY A 92 LEU A 93
SITE 4 AC1 21 THR A 140 GLY A 141 SER A 142 TYR A 155
SITE 5 AC1 21 VAL A 188 THR A 190 ALA A 191 PHE A 192
SITE 6 AC1 21 EQI A 329
SITE 1 AC2 11 SER A 142 VAL A 143 GLY A 144 LEU A 149
SITE 2 AC2 11 TYR A 155 PHE A 192 TYR A 218 HIS A 221
SITE 3 AC2 11 ARG A 258 GLU A 282 NAP A 328
SITE 1 AC3 23 GLY B 9 SER B 11 SER B 12 ILE B 14
SITE 2 AC3 23 ARG B 37 LEU B 64 ASP B 65 VAL B 66
SITE 3 AC3 23 ARG B 67 ASN B 90 ALA B 91 GLY B 92
SITE 4 AC3 23 LEU B 93 VAL B 113 THR B 140 GLY B 141
SITE 5 AC3 23 SER B 142 TYR B 155 LYS B 159 CYS B 185
SITE 6 AC3 23 VAL B 188 THR B 190 MET B 193
CRYST1 44.020 114.160 114.840 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 0.022717 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008760 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008708 0.00000
MTRIX1 1 0.968030 0.240107 -0.072577 -0.49600 1
MTRIX2 1 0.240103 -0.970707 -0.008915 22.81120 1
MTRIX3 1 -0.072592 -0.008796 -0.997323 61.86040 1
(ATOM LINES ARE NOT SHOWN.)
END