HEADER HORMONE 11-NOV-09 2WXZ
TITLE CRYSTAL STRUCTURE OF RAT ANGIOTENSINOGEN IN C2 SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOTENSINOGEN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SERPIN A8;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ANGIOTENSINOGEN;
COMPND 8 CHAIN: C;
COMPND 9 SYNONYM: SERPIN A8;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PSUMO3;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSUMO3-MANGT;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 12 ORGANISM_COMMON: RAT;
SOURCE 13 ORGANISM_TAXID: 10116;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR: PSUMO3;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PSUMO3-MANGT
KEYWDS HORMONE, ANGIOTENSINOGEN, RENIN, ANGIOTENSIN, HYPERTENSION,
KEYWDS 2 GLYCOPROTEIN, VASOCONSTRICTOR, VASOACTIVE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ZHOU,Z.WEI,R.W.CARRELL,R.J.READ
REVDAT 2 10-NOV-10 2WXZ 1 JRNL
REVDAT 1 20-OCT-10 2WXZ 0
JRNL AUTH A.ZHOU,R.W.CARRELL,M.P.MURPHY,Z.WEI,Y.YAN,P.L.STANLEY,
JRNL AUTH 2 P.E.STEIN,F.B.PIPKIN,R.J.READ
JRNL TITL A REDOX SWITCH IN ANGIOTENSINOGEN MODULATES ANGIOTENSIN
JRNL TITL 2 RELEASE.
JRNL REF NATURE V. 468 108 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20927107
JRNL DOI 10.1038/NATURE09505
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0099
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 22489
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) : 0.283
REMARK 3 R VALUE (WORKING SET) : 0.282
REMARK 3 FREE R VALUE : 0.310
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1212
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.4000
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.4360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6473
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : -1.35000
REMARK 3 B33 (A**2) : 1.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.50000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.478
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.512
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 60.573
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.883
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.868
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6620 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4445 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9014 ; 0.929 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10900 ; 0.834 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 831 ; 5.409 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 277 ;37.159 ;24.296
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1088 ;15.610 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;15.571 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1056 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7276 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1284 ; 0.001 ; 0.020
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): 4177 ; 0.254 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1668 ; 0.023 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6763 ; 0.467 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2443 ; 0.343 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2248 ; 0.633 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : C A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 4 C 20 4
REMARK 3 1 A 4 A 20 4
REMARK 3 2 C 91 C 96 4
REMARK 3 2 A 91 A 96 4
REMARK 3 3 C 97 C 230 2
REMARK 3 3 A 97 A 230 2
REMARK 3 4 C 231 C 238 4
REMARK 3 4 A 231 A 238 4
REMARK 3 5 C 239 C 401 2
REMARK 3 5 A 239 A 401 2
REMARK 3 6 C 402 C 421 6
REMARK 3 6 A 402 A 421 6
REMARK 3 7 C 422 C 455 2
REMARK 3 7 A 422 A 455 2
REMARK 3 8 C 21 C 90 2
REMARK 3 8 A 21 A 90 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2223 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 2223 ; 0.01 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3099 ; 0.04 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 3099 ; 0.04 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 42 ; 0.24 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 42 ; 0.24 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 2223 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 2223 ; 0.02 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3099 ; 0.02 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 3099 ; 0.02 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 42 ; 0.03 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 42 ; 0.03 ; 10.00
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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 6 C 450
REMARK 3 ORIGIN FOR THE GROUP (A): -38.2435 33.2701 21.4122
REMARK 3 T TENSOR
REMARK 3 T11: 0.3363 T22: 0.1544
REMARK 3 T33: 0.2542 T12: 0.0455
REMARK 3 T13: 0.0123 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 2.6972 L22: 1.6493
REMARK 3 L33: 3.5969 L12: -0.0043
REMARK 3 L13: -1.4865 L23: -0.4519
REMARK 3 S TENSOR
REMARK 3 S11: -0.1059 S12: -0.4427 S13: -0.1040
REMARK 3 S21: -0.0364 S22: 0.0102 S23: -0.1271
REMARK 3 S31: 0.1035 S32: 0.3333 S33: 0.0957
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 450
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1147 19.4994 58.5557
REMARK 3 T TENSOR
REMARK 3 T11: 0.0603 T22: 0.1125
REMARK 3 T33: 0.1090 T12: -0.0079
REMARK 3 T13: -0.0670 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 5.0108 L22: 1.7290
REMARK 3 L33: 3.4266 L12: -1.1411
REMARK 3 L13: -2.3172 L23: 0.4073
REMARK 3 S TENSOR
REMARK 3 S11: 0.1908 S12: 0.4185 S13: 0.0539
REMARK 3 S21: -0.1145 S22: -0.1117 S23: 0.0976
REMARK 3 S31: -0.1986 S32: 0.2330 S33: -0.0791
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 2WXZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-09.
REMARK 100 THE PDBE ID CODE IS EBI-41691.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.045
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23736
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 41.60
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.7
REMARK 200 R MERGE (I) : 0.22
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.1
REMARK 200 R MERGE FOR SHELL (I) : 1.04
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG3350, 0.2M MGSO4, 0.1M TRIS
REMARK 280 -HCL, PH7.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 65.24950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.76950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.24950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.76950
REMARK 290 SMTRY3 4 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ASP A 1
REMARK 465 ARG A 2
REMARK 465 VAL A 3
REMARK 465 TYR A 4
REMARK 465 ILE A 5
REMARK 465 LEU A 21
REMARK 465 GLU A 22
REMARK 465 ASN A 23
REMARK 465 PRO A 24
REMARK 465 SER A 25
REMARK 465 VAL A 26
REMARK 465 GLU A 27
REMARK 465 GLY A 93
REMARK 465 GLN A 160
REMARK 465 GLY A 161
REMARK 465 GLY A 162
REMARK 465 SER A 163
REMARK 465 SER A 164
REMARK 465 SER A 165
REMARK 465 GLN A 166
REMARK 465 THR A 167
REMARK 465 GLU A 404
REMARK 465 GLU A 405
REMARK 465 GLN A 406
REMARK 465 PRO A 407
REMARK 465 THR A 408
REMARK 465 GLU A 409
REMARK 465 SER A 410
REMARK 465 ASN A 451
REMARK 465 VAL A 452
REMARK 465 VAL A 453
REMARK 465 ASP C 1
REMARK 465 ARG C 2
REMARK 465 VAL C 3
REMARK 465 TYR C 4
REMARK 465 ILE C 5
REMARK 465 LEU C 21
REMARK 465 GLU C 22
REMARK 465 ASN C 23
REMARK 465 PRO C 24
REMARK 465 SER C 25
REMARK 465 VAL C 26
REMARK 465 GLU C 27
REMARK 465 GLY C 93
REMARK 465 GLN C 160
REMARK 465 GLY C 161
REMARK 465 GLY C 162
REMARK 465 SER C 163
REMARK 465 SER C 164
REMARK 465 SER C 165
REMARK 465 GLN C 166
REMARK 465 THR C 167
REMARK 465 GLU C 403
REMARK 465 GLU C 404
REMARK 465 GLU C 405
REMARK 465 GLN C 406
REMARK 465 PRO C 407
REMARK 465 THR C 408
REMARK 465 GLU C 409
REMARK 465 SER C 410
REMARK 465 ALA C 411
REMARK 465 GLN C 412
REMARK 465 GLN C 413
REMARK 465 PRO C 414
REMARK 465 GLY C 415
REMARK 465 SER C 416
REMARK 465 PRO C 417
REMARK 465 GLU C 418
REMARK 465 ASN C 451
REMARK 465 VAL C 452
REMARK 465 VAL C 453
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 7 129.53 -38.60
REMARK 500 GLU A 134 89.63 -67.09
REMARK 500 ALA A 199 59.85 -94.47
REMARK 500 ASN A 231 96.05 -66.17
REMARK 500 LEU A 372 51.32 -112.73
REMARK 500 PRO A 427 128.09 -36.39
REMARK 500 PRO A 449 41.22 -95.77
REMARK 500 PRO C 7 129.39 -39.23
REMARK 500 GLU C 134 89.66 -67.14
REMARK 500 ASN C 231 96.05 -67.05
REMARK 500 LEU C 333 40.15 -104.06
REMARK 500 LEU C 372 52.42 -113.13
REMARK 500 PRO C 427 128.16 -37.99
REMARK 500 PRO C 449 40.85 -94.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2X0B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANGIOTENSINOGEN
REMARK 900 COMPLEXED WITH RENIN
REMARK 900 RELATED ID: 2WXY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ANGIOTENSINOGEN IN
REMARK 900 THE REDUCED FORM
REMARK 900 RELATED ID: 2WY1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RAT ANGIOTENSINOGEN IN
REMARK 900 P321 SPACE GROUP
REMARK 900 RELATED ID: 2WY0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ANGIOTENSINOGEN IN
REMARK 900 THE OXIDISED FORM WITH SPACE GROUP P6122
REMARK 900 RELATED ID: 2WXW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANGIOTENSINOGEN
REMARK 900 RELATED ID: 2WXX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ANGIOTENSINOGEN IN
REMARK 900 THE OXIDISED FORM
DBREF 2WXZ A 1 453 UNP P01015 ANGT_RAT 25 477
DBREF 2WXZ C 1 453 UNP P01015 ANGT_RAT 25 477
SEQADV 2WXZ VAL A 80 UNP P01015 MET 104 CONFLICT
SEQRES 1 A 453 ASP ARG VAL TYR ILE HIS PRO PHE HIS LEU LEU TYR TYR
SEQRES 2 A 453 SER LYS SER THR CYS ALA GLN LEU GLU ASN PRO SER VAL
SEQRES 3 A 453 GLU THR LEU PRO GLU PRO THR PHE GLU PRO VAL PRO ILE
SEQRES 4 A 453 GLN ALA LYS THR SER PRO VAL ASP GLU LYS THR LEU ARG
SEQRES 5 A 453 ASP LYS LEU VAL LEU ALA THR GLU LYS LEU GLU ALA GLU
SEQRES 6 A 453 ASP ARG GLN ARG ALA ALA GLN VAL ALA MET ILE ALA ASN
SEQRES 7 A 453 PHE VAL GLY PHE ARG MET TYR LYS MET LEU SER GLU ALA
SEQRES 8 A 453 ARG GLY VAL ALA SER GLY ALA VAL LEU SER PRO PRO ALA
SEQRES 9 A 453 LEU PHE GLY THR LEU VAL SER PHE TYR LEU GLY SER LEU
SEQRES 10 A 453 ASP PRO THR ALA SER GLN LEU GLN VAL LEU LEU GLY VAL
SEQRES 11 A 453 PRO VAL LYS GLU GLY ASP CYS THR SER ARG LEU ASP GLY
SEQRES 12 A 453 HIS LYS VAL LEU THR ALA LEU GLN ALA VAL GLN GLY LEU
SEQRES 13 A 453 LEU VAL THR GLN GLY GLY SER SER SER GLN THR PRO LEU
SEQRES 14 A 453 LEU GLN SER THR VAL VAL GLY LEU PHE THR ALA PRO GLY
SEQRES 15 A 453 LEU ARG LEU LYS GLN PRO PHE VAL GLU SER LEU GLY PRO
SEQRES 16 A 453 PHE THR PRO ALA ILE PHE PRO ARG SER LEU ASP LEU SER
SEQRES 17 A 453 THR ASP PRO VAL LEU ALA ALA GLN LYS ILE ASN ARG PHE
SEQRES 18 A 453 VAL GLN ALA VAL THR GLY TRP LYS MET ASN LEU PRO LEU
SEQRES 19 A 453 GLU GLY VAL SER THR ASP SER THR LEU PHE PHE ASN THR
SEQRES 20 A 453 TYR VAL HIS PHE GLN GLY LYS MET ARG GLY PHE SER GLN
SEQRES 21 A 453 LEU THR GLY LEU HIS GLU PHE TRP VAL ASP ASN SER THR
SEQRES 22 A 453 SER VAL SER VAL PRO MET LEU SER GLY THR GLY ASN PHE
SEQRES 23 A 453 GLN HIS TRP SER ASP ALA GLN ASN ASN PHE SER VAL THR
SEQRES 24 A 453 ARG VAL PRO LEU GLY GLU SER VAL THR LEU LEU LEU ILE
SEQRES 25 A 453 GLN PRO GLN CYS ALA SER ASP LEU ASP ARG VAL GLU VAL
SEQRES 26 A 453 LEU VAL PHE GLN HIS ASP PHE LEU THR TRP ILE LYS ASN
SEQRES 27 A 453 PRO PRO PRO ARG ALA ILE ARG LEU THR LEU PRO GLN LEU
SEQRES 28 A 453 GLU ILE ARG GLY SER TYR ASN LEU GLN ASP LEU LEU ALA
SEQRES 29 A 453 GLN ALA LYS LEU SER THR LEU LEU GLY ALA GLU ALA ASN
SEQRES 30 A 453 LEU GLY LYS MET GLY ASP THR ASN PRO ARG VAL GLY GLU
SEQRES 31 A 453 VAL LEU ASN SER ILE LEU LEU GLU LEU GLN ALA GLY GLU
SEQRES 32 A 453 GLU GLU GLN PRO THR GLU SER ALA GLN GLN PRO GLY SER
SEQRES 33 A 453 PRO GLU VAL LEU ASP VAL THR LEU SER SER PRO PHE LEU
SEQRES 34 A 453 PHE ALA ILE TYR GLU ARG ASP SER GLY ALA LEU HIS PHE
SEQRES 35 A 453 LEU GLY ARG VAL ASP ASN PRO GLN ASN VAL VAL
SEQRES 1 C 453 ASP ARG VAL TYR ILE HIS PRO PHE HIS LEU LEU TYR TYR
SEQRES 2 C 453 SER LYS SER THR CYS ALA GLN LEU GLU ASN PRO SER VAL
SEQRES 3 C 453 GLU THR LEU PRO GLU PRO THR PHE GLU PRO VAL PRO ILE
SEQRES 4 C 453 GLN ALA LYS THR SER PRO VAL ASP GLU LYS THR LEU ARG
SEQRES 5 C 453 ASP LYS LEU VAL LEU ALA THR GLU LYS LEU GLU ALA GLU
SEQRES 6 C 453 ASP ARG GLN ARG ALA ALA GLN VAL ALA MET ILE ALA ASN
SEQRES 7 C 453 PHE MET GLY PHE ARG MET TYR LYS MET LEU SER GLU ALA
SEQRES 8 C 453 ARG GLY VAL ALA SER GLY ALA VAL LEU SER PRO PRO ALA
SEQRES 9 C 453 LEU PHE GLY THR LEU VAL SER PHE TYR LEU GLY SER LEU
SEQRES 10 C 453 ASP PRO THR ALA SER GLN LEU GLN VAL LEU LEU GLY VAL
SEQRES 11 C 453 PRO VAL LYS GLU GLY ASP CYS THR SER ARG LEU ASP GLY
SEQRES 12 C 453 HIS LYS VAL LEU THR ALA LEU GLN ALA VAL GLN GLY LEU
SEQRES 13 C 453 LEU VAL THR GLN GLY GLY SER SER SER GLN THR PRO LEU
SEQRES 14 C 453 LEU GLN SER THR VAL VAL GLY LEU PHE THR ALA PRO GLY
SEQRES 15 C 453 LEU ARG LEU LYS GLN PRO PHE VAL GLU SER LEU GLY PRO
SEQRES 16 C 453 PHE THR PRO ALA ILE PHE PRO ARG SER LEU ASP LEU SER
SEQRES 17 C 453 THR ASP PRO VAL LEU ALA ALA GLN LYS ILE ASN ARG PHE
SEQRES 18 C 453 VAL GLN ALA VAL THR GLY TRP LYS MET ASN LEU PRO LEU
SEQRES 19 C 453 GLU GLY VAL SER THR ASP SER THR LEU PHE PHE ASN THR
SEQRES 20 C 453 TYR VAL HIS PHE GLN GLY LYS MET ARG GLY PHE SER GLN
SEQRES 21 C 453 LEU THR GLY LEU HIS GLU PHE TRP VAL ASP ASN SER THR
SEQRES 22 C 453 SER VAL SER VAL PRO MET LEU SER GLY THR GLY ASN PHE
SEQRES 23 C 453 GLN HIS TRP SER ASP ALA GLN ASN ASN PHE SER VAL THR
SEQRES 24 C 453 ARG VAL PRO LEU GLY GLU SER VAL THR LEU LEU LEU ILE
SEQRES 25 C 453 GLN PRO GLN CYS ALA SER ASP LEU ASP ARG VAL GLU VAL
SEQRES 26 C 453 LEU VAL PHE GLN HIS ASP PHE LEU THR TRP ILE LYS ASN
SEQRES 27 C 453 PRO PRO PRO ARG ALA ILE ARG LEU THR LEU PRO GLN LEU
SEQRES 28 C 453 GLU ILE ARG GLY SER TYR ASN LEU GLN ASP LEU LEU ALA
SEQRES 29 C 453 GLN ALA LYS LEU SER THR LEU LEU GLY ALA GLU ALA ASN
SEQRES 30 C 453 LEU GLY LYS MET GLY ASP THR ASN PRO ARG VAL GLY GLU
SEQRES 31 C 453 VAL LEU ASN SER ILE LEU LEU GLU LEU GLN ALA GLY GLU
SEQRES 32 C 453 GLU GLU GLN PRO THR GLU SER ALA GLN GLN PRO GLY SER
SEQRES 33 C 453 PRO GLU VAL LEU ASP VAL THR LEU SER SER PRO PHE LEU
SEQRES 34 C 453 PHE ALA ILE TYR GLU ARG ASP SER GLY ALA LEU HIS PHE
SEQRES 35 C 453 LEU GLY ARG VAL ASP ASN PRO GLN ASN VAL VAL
HELIX 1 1 SER A 14 GLN A 20 1 7
HELIX 2 2 ASP A 47 LYS A 61 1 15
HELIX 3 3 GLU A 63 ARG A 92 1 30
HELIX 4 4 SER A 101 GLY A 115 1 15
HELIX 5 5 LEU A 117 LEU A 128 1 12
HELIX 6 6 ASP A 142 VAL A 158 1 17
HELIX 7 7 GLN A 187 LEU A 193 1 7
HELIX 8 8 ASP A 210 GLY A 227 1 18
HELIX 9 9 CYS A 316 SER A 318 5 3
HELIX 10 10 ASP A 319 PHE A 328 1 10
HELIX 11 11 LEU A 359 ALA A 366 1 8
HELIX 12 12 LEU A 378 MET A 381 5 4
HELIX 13 13 SER C 14 GLN C 20 1 7
HELIX 14 14 ASP C 47 LYS C 61 1 15
HELIX 15 15 GLU C 63 ARG C 92 1 30
HELIX 16 16 SER C 101 GLY C 115 1 15
HELIX 17 17 LEU C 117 LEU C 128 1 12
HELIX 18 18 ASP C 142 VAL C 158 1 17
HELIX 19 19 GLN C 187 LEU C 193 1 7
HELIX 20 20 ASP C 210 GLY C 227 1 18
HELIX 21 21 CYS C 316 SER C 318 5 3
HELIX 22 22 ASP C 319 PHE C 328 1 10
HELIX 23 23 LEU C 359 ALA C 366 1 8
HELIX 24 24 LEU C 378 MET C 381 5 4
SHEET 1 AA 2 THR A 33 PHE A 34 0
SHEET 2 AA 2 LEU A 185 LYS A 186 -1 O LEU A 185 N PHE A 34
SHEET 1 AB 6 VAL A 37 PRO A 38 0
SHEET 2 AB 6 ILE A 200 SER A 204 1 O PRO A 202 N VAL A 37
SHEET 3 AB 6 LEU A 169 THR A 179 1 O VAL A 175 N PHE A 201
SHEET 4 AB 6 LEU A 243 MET A 255 -1 O PHE A 244 N PHE A 178
SHEET 5 AB 6 LEU A 392 ALA A 401 1 O LEU A 392 N THR A 247
SHEET 6 AB 6 LEU A 351 ASN A 358 -1 O LEU A 351 N LEU A 399
SHEET 1 AC 7 GLY A 97 LEU A 100 0
SHEET 2 AC 7 ALA A 439 VAL A 446 -1 O LEU A 443 N LEU A 100
SHEET 3 AC 7 PHE A 428 GLU A 434 -1 O PHE A 428 N VAL A 446
SHEET 4 AC 7 VAL A 307 PRO A 314 -1 O THR A 308 N TYR A 433
SHEET 5 AC 7 PHE A 296 PRO A 302 -1 O SER A 297 N GLN A 313
SHEET 6 AC 7 MET A 279 ASP A 291 -1 O GLN A 287 N ARG A 300
SHEET 7 AC 7 ARG A 342 PRO A 349 -1 O ARG A 342 N PHE A 286
SHEET 1 AD 7 GLY A 97 LEU A 100 0
SHEET 2 AD 7 ALA A 439 VAL A 446 -1 O LEU A 443 N LEU A 100
SHEET 3 AD 7 PHE A 428 GLU A 434 -1 O PHE A 428 N VAL A 446
SHEET 4 AD 7 VAL A 307 PRO A 314 -1 O THR A 308 N TYR A 433
SHEET 5 AD 7 PHE A 296 PRO A 302 -1 O SER A 297 N GLN A 313
SHEET 6 AD 7 MET A 279 ASP A 291 -1 O GLN A 287 N ARG A 300
SHEET 7 AD 7 SER A 259 GLN A 260 -1 O SER A 259 N SER A 281
SHEET 1 AE 2 ARG A 342 PRO A 349 0
SHEET 2 AE 2 MET A 279 ASP A 291 -1 O LEU A 280 N LEU A 348
SHEET 1 AF 2 HIS A 265 ASP A 270 0
SHEET 2 AF 2 THR A 273 VAL A 277 -1 O THR A 273 N ASP A 270
SHEET 1 CA 2 THR C 33 PHE C 34 0
SHEET 2 CA 2 LEU C 185 LYS C 186 -1 O LEU C 185 N PHE C 34
SHEET 1 CB 6 VAL C 37 PRO C 38 0
SHEET 2 CB 6 ILE C 200 SER C 204 1 O PRO C 202 N VAL C 37
SHEET 3 CB 6 LEU C 169 THR C 179 1 O VAL C 175 N PHE C 201
SHEET 4 CB 6 LEU C 243 MET C 255 -1 O PHE C 244 N PHE C 178
SHEET 5 CB 6 LEU C 392 ALA C 401 1 O LEU C 392 N THR C 247
SHEET 6 CB 6 LEU C 351 ASN C 358 -1 O LEU C 351 N LEU C 399
SHEET 1 CC 7 GLY C 97 LEU C 100 0
SHEET 2 CC 7 ALA C 439 VAL C 446 -1 O LEU C 443 N LEU C 100
SHEET 3 CC 7 PHE C 428 GLU C 434 -1 O PHE C 428 N VAL C 446
SHEET 4 CC 7 VAL C 307 PRO C 314 -1 O THR C 308 N TYR C 433
SHEET 5 CC 7 PHE C 296 PRO C 302 -1 O SER C 297 N GLN C 313
SHEET 6 CC 7 MET C 279 ASP C 291 -1 O GLN C 287 N ARG C 300
SHEET 7 CC 7 ARG C 342 PRO C 349 -1 O ARG C 342 N PHE C 286
SHEET 1 CD 7 GLY C 97 LEU C 100 0
SHEET 2 CD 7 ALA C 439 VAL C 446 -1 O LEU C 443 N LEU C 100
SHEET 3 CD 7 PHE C 428 GLU C 434 -1 O PHE C 428 N VAL C 446
SHEET 4 CD 7 VAL C 307 PRO C 314 -1 O THR C 308 N TYR C 433
SHEET 5 CD 7 PHE C 296 PRO C 302 -1 O SER C 297 N GLN C 313
SHEET 6 CD 7 MET C 279 ASP C 291 -1 O GLN C 287 N ARG C 300
SHEET 7 CD 7 SER C 259 GLN C 260 -1 O SER C 259 N SER C 281
SHEET 1 CE 2 ARG C 342 PRO C 349 0
SHEET 2 CE 2 MET C 279 ASP C 291 -1 O LEU C 280 N LEU C 348
SHEET 1 CF 2 HIS C 265 ASP C 270 0
SHEET 2 CF 2 THR C 273 VAL C 277 -1 O THR C 273 N ASP C 270
SSBOND 1 CYS A 18 CYS A 137 1555 1555 2.04
SSBOND 2 CYS C 18 CYS C 137 1555 1555 2.03
CRYST1 130.499 49.539 150.275 90.00 90.84 90.00 C 1 2 1 4
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 0.007663 0.000000 0.000112 0.00000
SCALE2 0.000000 0.020186 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006655 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
